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2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
catalytic mechanism
-
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
-
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
-
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
-
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
-
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
-
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
-
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be deprotonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
the reaction of DHAR proceeds by a bi-uni-uni-uniping-pong enzymatic mechanism. In step 1, the DHA molecule is bound to the catalytic cysteine residue of the reduced form of DHAR (DHAR-S-) and is reduced to ascorbate. This reduction involves nucleophilic attack by the catalytic cysteine residue and the formation of cysteine sulfenic acid (sulfenylated DHAR, DHAR-SOH). In step 2, the reactive sulfenic acid at the catalytic cysteine residue reacts with GSH bound at the G-site and generates the mixed disulfide (DHAR-S-SG). Subsequently, the second GSH molecule binds to the H-site and may be de-protonated to GS-. Then, the GSH bound with the catalytic cysteine residue is removed by the nucleophilic attack of GS- at the H-site. As a result, a catalytic cysteine residue is reduced and one molecule of glutathione disulfide (GSSG) is released (step 3). Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
-
-
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
-
-
-
-
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2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
glutathione + dehydroascorbate
GSSG + ascorbate
GSH + 1,2,3-trioxocyclopentane
GSSG + ?
-
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
GSH + isodehydroascorbate
GSSG + isoascorbate
-
-
-
-
?
L-acetylcysteine + dehydroascorbate
N,N'-diacetyl-L-cystine + ascorbate
-
4% of the activity with GSH
-
-
?
L-Cys + dehydroascorbate
? + ascorbate
-
8% of the activity with GSH
-
-
?
additional information
?
-
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
2 glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
r
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
glutathione disulfide + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
vitamin C-conserving mechanism
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
the enzyme is critical for maintenance of an appropriate level of ascorbate in plant cells
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
Prunus sp.
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
regenerates ascorbate after it is oxidized during normal aerobic metabolism
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
ir
glutathione + dehydroascorbate
GSSG + ascorbate
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
specific for glutathione as hydrogen donor
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
-
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
L-threo-diastereomer is reduced faster than the L-erythro-dehydroascorbate and D-erythro-dehydroascorbate
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
specific for glutathione as hydrogen donor
-
-
?
GSH + dehydroascorbate
GSSG + ascorbate
-
L-threo-dehydroascorbate is the best and D-threo-dehydroascorbate is the worst substrate of the four dehydroascorbate stereoisomers
-
-
?
additional information
?
-
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
the activity of DHARs is coupled to oxidation of glutathione, which is also required for spontaneous, nonenzymatic reduction of DHA to ascorbate
-
-
-
additional information
?
-
the activity of DHARs is coupled to oxidation of glutathione, which is also required for spontaneous, nonenzymatic reduction of DHA to ascorbate
-
-
-
additional information
?
-
the activity of DHARs is coupled to oxidation of glutathione, which is also required for spontaneous, nonenzymatic reduction of DHA to ascorbate
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
GRX1is a typical CPYC-type GRX, which is reduced by GSH and exhibits disulfide reductase, dehydroascorbate reductase, and deglutathionylation activities
-
-
-
additional information
?
-
-
GRX1is a typical CPYC-type GRX, which is reduced by GSH and exhibits disulfide reductase, dehydroascorbate reductase, and deglutathionylation activities
-
-
-
additional information
?
-
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
-
the activity of DHARs is coupled to oxidation of glutathione, which is also required for spontaneous, nonenzymatic reduction of DHA to ascorbate
-
-
-
additional information
?
-
enzyme nlGSTO shows broad substrate specificity as thiol transferase, see also EC 2.5.1.18
-
-
-
additional information
?
-
-
enzyme nlGSTO shows broad substrate specificity as thiol transferase, see also EC 2.5.1.18
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
no substrates: 1-chloro-2,4-dinitrobenzene, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, nitrobutyl chloride, 4-nitrophenyl acetate, 1,2-dichloro-4-nitrobenzene
-
-
?
additional information
?
-
no substrates: 1-chloro-2,4-dinitrobenzene, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, nitrobutyl chloride, 4-nitrophenyl acetate, 1,2-dichloro-4-nitrobenzene
-
-
?
additional information
?
-
no substrates: 1-chloro-2,4-dinitrobenzene, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, nitrobutyl chloride, 4-nitrophenyl acetate, 1,2-dichloro-4-nitrobenzene
-
-
?
additional information
?
-
-
no substrates: 1-chloro-2,4-dinitrobenzene, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, nitrobutyl chloride, 4-nitrophenyl acetate, 1,2-dichloro-4-nitrobenzene
-
-
?
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
no activity with NADPH, alpha-lipoic acid, or DL-lipoamide as electron donors. The enzyme is GSH-dependent
-
-
-
additional information
?
-
-
no activity with NADPH, alpha-lipoic acid, or DL-lipoamide as electron donors. The enzyme is GSH-dependent
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
additional information
?
-
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)
-
-
?
additional information
?
-
-
L-Cys-L-Gly is not active as hydrogen donor
-
-
?
additional information
?
-
the activity of DHARs is coupled to oxidation of glutathione, which is also required for spontaneous, nonenzymatic reduction of DHA to ascorbate
-
-
-
additional information
?
-
while the reduction of dehydroascorbate (DHA) to ascorbate can occur chemically at significant rates, DHAR is able to accelerate the reaction, in both cases reduced glutathione (GSH) is used as the reductant
-
-
-
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0.019 - 2.5
dehydroascorbate
additional information
additional information
-
0.019
dehydroascorbate
-
mutant enzyme C9S
0.026
dehydroascorbate
-
mutant enzyme C23S
0.05
dehydroascorbate
pH and temperature not specified in the publication, chloroplastic isozyme
0.053
dehydroascorbate
-
wild-type enzyme
0.058
dehydroascorbate
-
-
0.06
dehydroascorbate
-
recombinant enzyme form DHAR-1
0.068
dehydroascorbate
-
isoform DHAR1, at pH 6.5 and 25°C
0.068
dehydroascorbate
-
isoform DHAR2, at pH 6.5 and 25°C
0.07
dehydroascorbate
-
enzyme form DHAR-a
0.07
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
0.07
dehydroascorbate
-
isoform DHAR2, at pH 7.8 and 25°C
0.07
dehydroascorbate
pH and temperature not specified in the publication, chloroplastic isozyme DHAR1
0.07
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme
0.07
dehydroascorbate
-
pH and temperature not specified in the publication, plastidic isozyme DHAR2
0.08
dehydroascorbate
-
enzyme form DHAR-b
0.08
dehydroascorbate
Vmax: 34.12 micromol/min/mg
0.08
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme
0.09
dehydroascorbate
pH 8.0, 22°C, recombinant wild-type enzyme
0.09
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme DHAR2
0.11
dehydroascorbate
-
isoform DHAR1, at pH 7.8 and 25°C
0.11
dehydroascorbate
-
pH and temperature not specified in the publication, cytosolic isozyme DHAR1
0.113
dehydroascorbate
-
isoform DHAR1, at pH 6.5 and 25°C
0.115
dehydroascorbate
-
isoform DHAR1, at pH 6.5 and 25°C
0.118
dehydroascorbate
-
isoform DHAR2, at pH 6.5 and 25°C
0.119
dehydroascorbate
-
isoform DHAR4, at pH 6.5 and 25°C
0.13
dehydroascorbate
mutant D72A, pH not specified in the publication, temperature not specified in the publication
0.13
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme
0.1334
dehydroascorbate
at pH 7.0 and 40°C
0.15
dehydroascorbate
-
isoform DHAR3, at pH 6.5 and 25°C
0.16
dehydroascorbate
pH and temperature not specified in the publication, chloroplastic isozyme DHAR3B
0.17
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
0.18
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme DHAR3A
0.19
dehydroascorbate
25°C
0.19
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme
0.21
dehydroascorbate
-
-
0.23
dehydroascorbate
wild-type, pH not specified in the publication, temperature not specified in the publication
0.23
dehydroascorbate
pH and temperature not specified in the publication, chloroplastic isozyme DHAR1
0.23
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme DHAR2
0.245
dehydroascorbate
-
-
0.248
dehydroascorbate
-
isoform DHAR2, at pH 6.5 and 25°C
0.26
dehydroascorbate
-
-
0.32
dehydroascorbate
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)
0.32
dehydroascorbate
recombinant mutant L225A, pH 8.0, 30°C
0.34
dehydroascorbate
-
-
0.35
dehydroascorbate
-
-
0.35
dehydroascorbate
-
rice recombinant DHAR
0.35
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme
0.39
dehydroascorbate
-
-
0.39
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
0.39
dehydroascorbate
pH 7.0, temperature not specified in the publication
0.39
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme
0.43
dehydroascorbate
mutant containing six cysteine-to-serine mutations, with C-terminal residues FGLC deleted, pH 6.9, 30°C
0.48
dehydroascorbate
pH not specified in the publication, temperature not specified in the publication
0.48
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme DHAR3
0.5
dehydroascorbate
allelic variant D142 of GSTO2-2
0.5
dehydroascorbate
allelic variant N142 of GSTO2-2
0.51
dehydroascorbate
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin), C25S mutant
0.51
dehydroascorbate
wild-type, pH 6.9, 30°C
0.52
dehydroascorbate
mutant containing six cysteine-to-serine mutations with the C-terminal cysteine residue deleted, pH 6.9, 30°C
0.53
dehydroascorbate
mutant with C-terminal residues FGLC deleted, pH 6.9, 30°C
0.55
dehydroascorbate
recombinant mutant F28A, pH 8.0, 30°C
0.58
dehydroascorbate
-
-
0.6
dehydroascorbate
recombinant wild-type enzyme, pH 8.0, 30°C
0.6
dehydroascorbate
recombinant mutant R176A, pH 8.0, 30°C
0.67
dehydroascorbate
recombinant mutant P30A, pH 8.0, 30°C
0.7
dehydroascorbate
mutant S73A, pH not specified in the publication, temperature not specified in the publication
0.77
dehydroascorbate
recombinant mutant C29A, pH 8.0, 30°C
0.81
dehydroascorbate
pH and temperature not specified in the publication, cytosolic isozyme
0.97
dehydroascorbate
mutant K8A, pH not specified in the publication, temperature not specified in the publication
1.85
dehydroascorbate
-
-
2
dehydroascorbate
pH 6.3, temperature not specified in the publication
0.04
glutathione
pH and temperature not specified in the publication, cytosolic isozyme
0.04167
glutathione
at pH 7.0 and 40°C
0.27
glutathione
pH 8.0, 22°C, recombinant wild-type enzyme
0.74
glutathione
-
isoform DHAR1, at pH 6.5 and 25°C
0.84
glutathione
pH and temperature not specified in the publication, cytosolic isozyme
0.96
glutathione
pH not specified in the publication, temperature not specified in the publication
1
glutathione
-
rice recombinant DHAR
1.03
glutathione
Vmax: 136.20 micromol/min/mg
1.03
glutathione
pH and temperature not specified in the publication, cytosolic isozyme
1.079
glutathione
-
isoform DHAR3, at pH 6.5 and 25°C
1.1
glutathione
pH and temperature not specified in the publication, chloroplastic isozyme
1.27
glutathione
-
isoform DHAR1, at pH 7.8 and 25°C
1.27
glutathione
-
pH and temperature not specified in the publication, cytosolic isozyme DHAR1
1.344
glutathione
-
isoform DHAR2, at pH 6.5 and 25°C
1.41
glutathione
pH and temperature not specified in the publication, cytosolic isozyme
1.466
glutathione
-
isoform DHAR1, at pH 6.5 and 25°C
1.63
glutathione
pH not specified in the publication, temperature not specified in the publication
1.71
glutathione
mutant D72A, pH not specified in the publication, temperature not specified in the publication
2.22
glutathione
-
isoform DHAR2, at pH 7.8 and 25°C
2.22
glutathione
-
pH and temperature not specified in the publication, plastidic isozyme DHAR2
2.255
glutathione
-
isoform DHAR2, at pH 6.5 and 25°C
2.28
glutathione
wild-type, pH not specified in the publication, temperature not specified in the publication
2.28
glutathione
pH and temperature not specified in the publication, cytosolic isozyme DHAR2
2.38
glutathione
pH and temperature not specified in the publication, cytosolic isozyme
2.47
glutathione
pH not specified in the publication, temperature not specified in the publication
2.47
glutathione
pH and temperature not specified in the publication, cytosolic isozyme DHAR3
2.5
glutathione
pH and temperature not specified in the publication, cytosolic isozyme
2.507
glutathione
-
isoform DHAR2, at pH 6.5 and 25°C
2.705
glutathione
-
isoform DHAR1, at pH 6.5 and 25°C
2.883
glutathione
-
isoform DHAR4, at pH 6.5 and 25°C
3.01
glutathione
mutant K8A, pH not specified in the publication, temperature not specified in the publication
3.26
glutathione
mutant S73A, pH not specified in the publication, temperature not specified in the publication
3.7 - 5
glutathione
pH not specified in the publication, temperature not specified in the publication
3.7 - 5
glutathione
pH and temperature not specified in the publication, chloroplastic isozyme DHAR1
4.18
glutathione
mutant with C-terminal residues FGLC deleted, pH 6.9, 30°C
4.35
glutathione
pH and temperature not specified in the publication, cytosolic isozyme
4.82
glutathione
wild-type, pH 6.9, 30°C
5.97
glutathione
mutant containing six cysteine-to-serine mutations, with C-terminal residues FGLC deleted, pH 6.9, 30°C
7.8
glutathione
mutant containing six cysteine-to-serine mutations with the C-terminal cysteine residue deleted, pH 6.9, 30°C
11.4
glutathione
allelic variant D142 of GSTO2-2
11.8
glutathione
allelic variant N142 of GSTO2-2
12.71
glutathione
pH 6.3, temperature not specified in the publication
0.69
GSH
-
mutant enzyme C23S
0.95
GSH
-
mutant enzyme C9S
1.1
GSH
-
wild-type enzyme
1.1
GSH
-
enzyme form DHAR-a and recombinant enzyme form DHAR-a
1.1
GSH
-
mutant enzyme C9S/C26S
2.5
GSH
-
enzyme form DHAR-b
3.7
GSH
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin)
3.7
GSH
-
pH 6.8, in presence of 0.5 mM dehydroascorbate
4.32
GSH
-
pH 6.3, in presence of 0.3 mM dehydroascorbate
5.2
GSH
-
glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin), C25S mutant
additional information
additional information
AtDHAR2 is the first DHAR reported to behave as an allosteric enzyme, and its kcat/K0.5 for DHA is substantially higher than for GSH, suggesting that it has a considerably higher substrate specificity for DHA
-
additional information
additional information
AtDHAR2 is the first DHAR reported to behave as an allosteric enzyme, and its kcat/K0.5 for DHA is substantially higher than for GSH, suggesting that it has a considerably higher substrate specificity for DHA
-
additional information
additional information
AtDHAR2 is the first DHAR reported to behave as an allosteric enzyme, and its kcat/K0.5 for DHA is substantially higher than for GSH, suggesting that it has a considerably higher substrate specificity for DHA
-
additional information
additional information
chloroplastic DHAR displays similar values to the cytosolic isoform, despite having somewhat higher affinity for GSH
-
additional information
additional information
GSH and DHA reduction follows a Michaelis-Menten kinetic
-
additional information
additional information
-
GSH and DHA reduction follows a Michaelis-Menten kinetic
-
additional information
additional information
in Arabidopsis, the cytosolic DHAR1 exhibits higher affinity for DHA than the chloroplastic DHAR3, while their affinities for GSH are approximately the same
-
additional information
additional information
in Arabidopsis, the cytosolic DHAR1 exhibits higher affinity for DHA than the chloroplastic DHAR3, while their affinities for GSH are approximately the same
-
additional information
additional information
in Arabidopsis, the cytosolic DHAR1 exhibits higher affinity for DHA than the chloroplastic DHAR3, while their affinities for GSH are approximately the same
-
additional information
additional information
-
the chloroplastic DHAR of kiwifruit shows higher affinity for DHA than the cytosolic DHAR, while the affinity for GSH of the cytosolic isoform is higher than that of the chloroplastic isoform
-
additional information
additional information
the chloroplastic DHAR of kiwifruit shows higher affinity for DHA than the cytosolic DHAR, while the affinity for GSH of the cytosolic isoform is higher than that of the chloroplastic isoform
-
additional information
additional information
the chloroplastic DHAR of kiwifruit shows higher affinity for DHA than the cytosolic DHAR, while the affinity for GSH of the cytosolic isoform is higher than that of the chloroplastic isoform
-
additional information
additional information
the chloroplastic DHAR of kiwifruit shows higher affinity for DHA than the cytosolic DHAR, while the affinity for GSH of the cytosolic isoform is higher than that of the chloroplastic isoform
-
additional information
additional information
the DHA reaction follows Michaelis-Menten kinetics
-
additional information
additional information
-
the DHA reaction follows Michaelis-Menten kinetics
-
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evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
-
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
evolution
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DHA reductase (DHAR) belongs to the glutathione S-transferase (GST) superfamily. Unlike most other GSTs, DHARs have an active-site cysteine in place of serine, and rather than stabilizing the thiolate anion of GSH (GS-), this change confers the capacity for reversible disulfide bond formation with GSH as part of the catalytic mechanism
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malfunction
a mutant lacking all three DHAR isozymes (DELTAdhar), with negligible DHAR activity, is shown to be equivalent to wild-type plants in terms of growth and development, as well as ascorbate levels. Analysis of the DELTAdhar mutant shows that DHARs are required to couple hydrogen peroxide metabolism to glutathione oxidation and that this is functionally important for downstream activation of the salicylic acid pathway. Thus, the role of DHARs in ascorbate recycling remains controversial. DHAR activity is dispensable for growth and ascorbate homeostasis under low light. When subjected to high-light stress, both the wild-type plants and DELTAdhar mutants accumulate ascorbate to high levels, but minor differences are observed after a prolonged stress. The lower ascorbate accumulation of DELTAdhar relative to the wild-type is associated with a slight overaccumulation of threonate, an ascorbate degradation. A blockage of ascorbate accumulation in response to high light is also observed when glutathione deficiency is induced pharmacologically by buthionine sulfoximine treatment, providing extra evidence that, in high-light conditions, glutathione acts as a substitute for ascorbate reduction
malfunction
DHAR overexpression in maize leads to an increase in ascorbate and glutathione concentration, as well as a shift toward the reduced state for glutathione
malfunction
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DHAR-downregulated tobacco lines show reduced total ascorbate levels, lower dry weight, and diminished photosynthetic efficiency. DHAR overexpression in tobacco leads to an increase in ascorbate and glutathione concentration, as well as a shift toward the reduced state for glutathione
malfunction
multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects are observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3
malfunction
multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects were observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3
malfunction
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site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
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site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
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site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
malfunction
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. In Arabidopsis, disruption of DHAR2 decreases the ascorbate redox state but not its pool size, and plants exhibit increased ozone sensitivity, and glutathione oxidation is inhibited in all three dhar single-mutants following photo-oxidative stress
malfunction
the increase of AsA regeneration via enhanced DHAR activity modulates the ascorbate-glutathione cycle activity against photooxidative stress in Chlamydomonas reinhardtii
malfunction
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multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects were observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3
-
malfunction
-
multiple loss of DHAR functions markedly decreases glutathione oxidation triggered by catalase deficiency. No evidence is obtained that either GRs or MDHARs are upregulated in plants lacking DHAR function. 3-Aminotriazole (3-AT) decreases catalase to very low levels while inducing ascorbate peroxidase (APX) and DHAR activities. These effects are accompanied by extensive leaf bleaching, and glutathione oxidation is evident as marked accumulation of GSSG. No difference is observed in bleaching or glutathione contents between the wild-type control and any of the mutants. Loss-of-function mutants for DHAR suggest that ascorbate regeneration is the major route leading to GSSG accumulation in response to intracellular H2O2. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHAR isozymes (DHAR1-3) are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited. Similar effects are observed in dhar1/dhar2 and dhar1/dhar2/dhar3 mutants using 3-AT to inhibit catalase. The major contribution to both lesion formation and glutathione oxidation triggered by catalase deficiency appears to come from DHAR1 and DHAR2 with a minor but significant contribution from chloroplastic DHAR3
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malfunction
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site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
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metabolism
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isoform DHAR3 contributes, at least to some extent, to ascorbate recycling
metabolism
glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H2O2 detoxification. Response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during oxidative stress, overview. Interplay between different DHARs appears to be necessary to couple ascorbate and glutathione pools and to allow glutathione-related signaling during enhanced H2O2 metabolism
metabolism
nlGSTO exhibits DHA reductase and thiol transferase, which are responsible for antioxidant reactions. GSH is known to be a redox regulator. Thiol transferase is involved in GSH homeostasis, which is important for antioxidant defense. DHA reductase is responsible for maintaining the balance of ascorbate, which functions in scavenging reactive oxygen species
metabolism
the ascorbate glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress. Cytosolic DHAR1 and chloroplastic DHAR3 contribute approximately equally and constitute almost all the leaf DHAR activity, while DHAR2 makes a minor contribution
metabolism
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress. Isozyme DHAR1 also appears to be capable of transmembrane ion conductance. Cytosolic DHAR1 and chloroplastic DHAR3 contribute approximately equally and constitute almost all the leaf DHAR activity, while DHAR2 makes a minor contribution
metabolism
the enzyme is part of the ascorbate recycling pathways, overview
metabolism
the enzyme is part of the ascorbate-glutathione pathway, overview. This defense system is composed by enzymes such as the ascorbate peroxidase (APX, EC 1.11.1.11), the monodehydroascorbate reductase (MDHAR, EC 1.6.5.4), the dehydroascorbate reductase (DHAR, EC 1.8.5.1), and the glutathione reductase (GR, EC 1.6.4.2), and compounds, such as ascorbate (ASC), dehydroascorbate (DHA), reduced (GSH) and oxidized (GSSG) glutathione
metabolism
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glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H2O2 detoxification. Response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during oxidative stress, overview. Interplay between different DHARs appears to be necessary to couple ascorbate and glutathione pools and to allow glutathione-related signaling during enhanced H2O2 metabolism
-
metabolism
-
the ascorbate-glutathione pathway is recognized to be a key player in H2O2 metabolism, in which reduced glutathione (GSH) regenerates ascorbate by reducing dehydroascorbate (DHA), either chemically or via DHA reductase (DHAR). Importance of DHAR in coupling the ascorbate and glutathione pools with H2O2 metabolism, together with its functions in plant defense, growth, and development. The ascorbate-glutathione (or Foyer-Halliwell-Asada) pathway plays a central role in H2O2 detoxification in plants and operates in the cytosol, chloroplasts, mitochondria and peroxisomes. Although GSH oxidation is potentially mediated by some glutathione-transferases (GSTs) and peroxiredoxins (PRXs), DHAR is identified as being a key player in ensuring GSH oxidation during oxidative stress. Isozyme DHAR1 also appears to be capable of transmembrane ion conductance. Cytosolic DHAR1 and chloroplastic DHAR3 contribute approximately equally and constitute almost all the leaf DHAR activity, while DHAR2 makes a minor contribution
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physiological function
chemical compounds that generate reactive oxygen species or directly applied hydrogen peroxide (H2O2) are able to induce hypersensitive response-type necroses in tobacco mosaic virus-inoculated Xanthi-nc tobacco even at high temperatures (e.g. 30°C). Activity of dehydroascorbate reductase is significantly higher at 30°C, as compared with 20°C, suggesting that DHAR might contribute to the inhibition of hypersensitive response-type necroses at 30°C
physiological function
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monodehydroascorbate reductase 2 and DHAR5 (At1g19570) mRNA levels are upregulated in Arabidopsis roots colonized by the beneficial endophyticfungus Piriformospora indica. Insertional inactivation of the two genes show that they are crucial for maintaining the interaction between Piriformospora indica and Arabidopsis in a mutualistic state, and under drought stress in particular
physiological function
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OsDHAR transformed Escherichia coli BL21 cells show significantly higher DHAR activity and a lower level of reactive oxygen species than the Escherichia coli cells transformed by an empty vector. The DHAR-overexpressing Escherichia coli strain is more tolerant to oxidant- and heavy metalmediated stress conditions than the control Escherichia coli strain, suggesting that the overexpressed rice DHAR gene effectively functions in a prokaryotic system and provides protection to various oxidative stresses
physiological function
monodehydroascorbate reductase and dehydroascorbate reductase are key enzymes of the ascorbate-glutathione cycle that maintain reduced pools of ascorbic acid and serve as important antioxidants
physiological function
enzyme overexpression AsA pool size, AsA:DHA ratio and the tolerance to moderate light-, high light-, methyl viologen- or H2O2-induced oxidative stress
physiological function
enzyme-expressing transgenic rice plants enhanced the redox state by reducing both hydroperoxide and malondialdehyde levels under salt and methyl viologen stress conditions, which lead to better plant growth, ion leakage and quantum yield
physiological function
expression of the enzyme can effectively enhance the tolerance to oxidative stress by decreasing the accumulation of reactive oxygen species
physiological function
-
isoform DHAR3 is required for high-light stress tolerance
physiological function
-
the enzyme is important for stress tolerance via induction of antioxidant proteins and can improve stress tolerance in transgenic potato plants
physiological function
-
the enzyme plays a pivotal role in the modulation of cellular redox states under photooxidative stress
physiological function
the enzyme plays a protective role under oxidative and other abiotic stress conditions
physiological function
the increased level of antioxidants generated by the enzyme protects rice from oxidative damage and increases the yield of rice grains
physiological function
dehydroascorbate reductase (DHAR) is a key enzyme for glutathione (GSH)-dependent reduction of dehydroascorbate (DHA) to recycled ascorbate (AsA) in plants, and plays a major role against the toxicity of reactive oxygen species (ROS)
physiological function
DHARs are required to couple hydrogen peroxide metabolism to glutathione oxidation and that this is functionally important for downstream activation of the salicylic acid pathway. DHAR activity is dispensable for growth and ascorbate homeostasis under low light
physiological function
in addition to these secondary metabolites, antioxidant enzymes play a fundamental role in regulating both biotic and abiotic stress responses in plants. One of the important antioxidant enzymes in plants is dehydroascorbate reductase (DHAR), which is crucial in maintaining the cellular levels of ascorbate through the ascorbate-glutathione cycle. DHAR converts dehydroascorbate (DHA) to ascorbate using reducing equivalents from GSH, whereby GSH is converted to oxidized glutathione (GSSG) and ascorbate is recycled. DHAR plays an important role in regulating H2O2-induced OS through the ascorbate-glutathione cycle. Thus, DHAR is a key player in detoxification of ROS to effectively regulate the cellular redox homeostasis
physiological function
-
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
-
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
-
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
-
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
-
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
-
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
physiological function
the DHA reductases (DHARs) that catalyze the GSH-dependent DHA reduction allows plants to rapidly recycle ascorbate from DHA. Cooperation of DHARs and GSH is required for ascorbate accumulation under high-light stress in Arabidopsis thaliana
physiological function
the enzyme is part of the ascorbate-glutathione pathway. This defense system is composed by enzymes such as the ascorbate peroxidase (APX, EC 1.11.1.11), the monodehydroascorbate reductase (MDHAR, EC 1.6.5.4), the dehydroascorbate reductase (DHAR, EC 1.8.5.1), and the glutathione reductase (GR, EC 1.6.4.2), and compounds, such as ascorbate (ASC), dehydroascorbate (DHA), reduced (GSH) and oxidized (GSSG) glutathione. In this pathway, DHAR uses GSH to reduce DHA generated from the oxidation of ASC, thereby regenerating it. The enzyme plays a critical role in the ASC-GSH recycling reaction in higher plants
physiological function
the omega-class glutathione S-transferase (GST), nlGSTO, of the brown planthopper, Nilaparvata lugens, catalyzes the biotransformation of glutathione with 1-chloro-2,4-dinitrobenzene, a general substrate for GST, as well as with dehydroascorbate to synthesize ascorbate. As ascorbate is a reducing agent, nlGSTO may participate in antioxidant resistance
physiological function
-
the DHA reductases (DHARs) that catalyze the GSH-dependent DHA reduction allows plants to rapidly recycle ascorbate from DHA. Cooperation of DHARs and GSH is required for ascorbate accumulation under high-light stress in Arabidopsis thaliana
-
physiological function
-
pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants. DHAR is important in maintaining the ascorbate pool and its redox state. Although some GSTs and peroxiredoxins may contribute to GSH oxidation, analysis of Arabidopsis dhar mutants has identified the key role of DHAR in coupling H2O2 to GSH oxidation. The enzyme has important roles in ascorbate regeneration and in responses to environmental stress. The enzyme is important in coupling the ascorbate and glutathione pools with H2O2 metabolism
-
additional information
-
a high ascorbate level is required for aluminium tolerance
additional information
transcriptional regulation of DHAR, overview
additional information
-
transcriptional regulation of DHAR, overview
additional information
computational modeling analysis is performed to understand the potential of five plant metabolites including ascorbic acid (AA), reduced glutathione (GSH), serotonin, jasmonic acid (JA), and salicylic acid (SA) in ameliorating metal/metalloid stress in rice, using dehydroascorbate reductase (DHAR) as a model. Six metal/metalloid ions (As3+, As5+, Cd2+, Cu2+, Pb2+, Zn2+) are used in the study, and the relative affinity, binding geometry and electrostatic surfaces of secondary metabolites and ions with the active site of DHAR are predicted. The results reveal that all the metabolites and ions may potentially interact with the active catalytic site of DHAR. The free energies of binding (docking score) of the metabolites are manyfolds higher than those of the ions. On comparison, the docking score of As3+ is found to be 28.29% of that of AA. Further, compared to AA, SA has lower score, and GSH, JA and serotonin show 1.42, 1.30 and 1.18fold higher score than AA. Further analysis reveals that the electrostatic surfaces of the metabolites and ions overlap with one another. Statistical analysis is performed to determine the properties of the ligands which are crucial in facilitating interaction of the ligands. Molecular docking, ligand-receptor interactions analysis, detailed overview
additional information
-
determination and analysis of the NMR solution structure of isozyme PtrDHAR3A. DHARs have a monomeric state that is unlike most GSTs
additional information
determination and analysis of the NMR solution structure of isozyme PtrDHAR3A. DHARs have a monomeric state that is unlike most GSTs
additional information
determination and analysis of the NMR solution structure of isozyme PtrDHAR3A. DHARs have a monomeric state that is unlike most GSTs
additional information
determination and analysis of the NMR solution structure of isozyme PtrDHAR3A. DHARs have a monomeric state that is unlike most GSTs
additional information
-
DHARs have a monomeric state that is unlike most GSTs
additional information
-
DHARs have a monomeric state that is unlike most GSTs
additional information
-
DHARs have a monomeric state that is unlike most GSTs
additional information
DHARs have a monomeric state that is unlike most GSTs
additional information
DHARs have a monomeric state that is unlike most GSTs
additional information
DHARs have a monomeric state that is unlike most GSTs
additional information
DHARs have a monomeric state that is unlike most GSTs
additional information
putative substrate-binding sites, including Phe28, Cys29, Phe30, Arg176, and Lue225, are important for glutathione transferase and dehydroascorbate reductase activities
additional information
-
putative substrate-binding sites, including Phe28, Cys29, Phe30, Arg176, and Lue225, are important for glutathione transferase and dehydroascorbate reductase activities
additional information
the crystal structure of apo CrDHAR1 provides insights into the proposed mechanism centering on the strictly conserved Cys22, which is suggested to initiate the redox reactions of DHA and GSH, crucial roles of Asp21 and Cys22 in substrate binding and catalysis
additional information
-
the crystal structure of apo CrDHAR1 provides insights into the proposed mechanism centering on the strictly conserved Cys22, which is suggested to initiate the redox reactions of DHA and GSH, crucial roles of Asp21 and Cys22 in substrate binding and catalysis
additional information
three-dimensional structure analysis of isozyme AtDHAR2, DHARs have a monomeric state that is unlike most GSTs
additional information
three-dimensional structure analysis of isozyme AtDHAR2, DHARs have a monomeric state that is unlike most GSTs
additional information
three-dimensional structure analysis of isozyme AtDHAR2, DHARs have a monomeric state that is unlike most GSTs
additional information
three-dimensional structure analysis of isozyme OsDHAR1. DHARs have a monomeric state that is unlike most GSTs
additional information
three-dimensional structure analysis of isozyme PgDHAR1. DHARs have a monomeric state that is unlike most GSTs
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?
-
x * 28000, isoform DHAR1, SDS-PAGE
?
-
x * 32000, isoform DHAR2, SDS-PAGE
?
x * 23400, calculated from amino acid sequence
?
x * 8643, calculated from sequence
monomer
-
DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
monomer
DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
monomer
-
DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
monomer
DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
monomer
1 * 25000, SDS-PAGE
monomer
1 * 12000, SDS-PAGE
monomer
1 * 24897, calculated from amino acid sequence
monomer
-
1 * 32000, SDS-PAGE
monomer
1 * 25000, SDS-PAGE
monomer
-
1 * 26000, SDS-PAGE
monomer
DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
monomer
native PAGE, MALDI-TOF/MS
monomer
DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
monomer
-
1 * 86000, SDS-PAGE
monomer
1 * 29100, calculated, about 2900, MALDI-TOF
monomer
1 * 29700, calculated, about 2900, MALDI-TOF
monomer
DHARs have a monomeric state that is unlike most GSTs. The enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
monomer
1 * 26000, about, SDS-PAGE
monomer
-
1 * 23000, SDS-PAGE
monomer
-
1 * 25000, enzyme form DHAR-b, SDS-PAGE
monomer
-
1 * 26000, enzyme form DHAR-a, SDS-PAGE
monomer
-
electrospray ionization quadrupole-time-of-flight (ESI Q-TOF), 1 * 15000 Da (His-tagged fusion protein)
additional information
-
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
-
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
-
additional information
-
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
formation of an intramolecular disulfide between Cys27 and Cys30 within the CPYC active site of GRX2
additional information
formation of an intramolecular disulfide between Cys27 and Cys30 within the CPYC active site of GRX2
additional information
-
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
-
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
additional information
the enzyme consists of two domains. The N-terminal domain contains residues responsible for GSH binding (the G-site), which is structurally similar to, and has evolved from, the thioredoxin fold, whilst the C-terminal alpha-helical domain provides the majority of the binding site for the hydrophobic substrate (the H-site)
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C22A
site-directed mutagenesis, the mutation results in severe loss of the enzyme's function
D21A
site-directed mutagenesis, the mutation results in severe loss of the enzyme's function
D21N
site-directed mutagenesis, the mutation results in severe loss of the enzyme's function
K11A
site-directed mutagenesis, the mutant K11A exhibits about 50% reduced redox activity compared to wild-type
H97A
-
the mutant shows wild type activity
Q114H
-
the mutant shows reduced activity compared to the wild type enzyme
A140D
no alteration in specific activity compared to the wild type enzyme
E155
the deletion causes a 2-3fold increase in the specific activity with each substrate and a significant decrease in the enzyme's heat stability, it is also linked to abnormal arsenic excretion patterns
E208K
no alteration in specific activity compared to the wild type enzyme
N142D
no effect on the specific activity of the enzyme with any substrate
Y34A
complete loss of activity
C29A
site-directed mutagenesis, the mutant shows 8.1fold lower activity with dehydroascorbate compared to wild-type
F28A
site-directed mutagenesis, the mutant shows 2.6fold lower activity with dehydroascorbate compared to wild-type
F30L
site-directed mutagenesis, the mutant shows 6.8fold lower activity with dehydroascorbate compared to wild-type
L225A
site-directed mutagenesis, the mutant shows 3.8fold lower activity with dehydroascorbate compared to wild-type
R176A
site-directed mutagenesis, the mutant shows 3.6fold lower activity with dehydroascorbate compared to wild-type
K47A
the mutant shows about wild type activity
K8A
the mutation significantly reduces the enzymatic activity
D72A
reduction in catalytic efficincy. D72 is a glutathione-site residue
K8A
severe reduction in catalytic efficincy. K8 is a glutathione-site residue
S73A
reduction in catalytic efficincy. S73 is a glutathione-site residue
C23S
-
mutant enzyme has almost no activity
C26S
-
turnover number is 57% of the wild-type value, KM-value for dehydroascorbate is 2fold lower than the wild-type value, KM-value for GSH is 1.6old lower than the wild-type value
C9S
-
turnover number is 86% of the wild-type value, KM-value for dehydroascorbate is 2.8fold lower than the wild-type value, KM-value for GSH is 2fold lower than the wild-type value
C9S/C26S
-
turnover number is 43% of the wild-type value, KM-value for dehydroascorbate is 1.1fold higher than the wild-type value, KM-value for GSH is identical to the wild-type value
C25S
-
has equivalent specificity constants for dehydroascorbate and GSH, but may have a different catalytic mechanism
additional information
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
-
mutant dhar or T-DNA tag line SALK_026089, the expression level of dhar is only one-quarter that in the wild-type, the mutant completely lacks DHAR activity and is highly ozone sensitive
additional information
-
overexpression in transgenic Nicotiana tabacum plants, the Arabidopsis enzyme confers resistance to aluminium induced oxidative damage and growth inhibition. Transgenic Nicotiana tabacum plants overexpressing the Arabidosis thaliana DHAR show lower hydrogen peroxide content, less lipid peroxidation and lower level of oxidative DNA damage than wild-type SR-1 plants, overview
additional information
construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3
additional information
construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3
additional information
construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3
additional information
construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHARs are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited
additional information
construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHARs are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited
additional information
construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHARs are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited
additional information
generation of a mutant lacking all three DHAR isozymes (DELTAdhar), the mutant has negligible DHAR activity, but it is shown to be equivalent to wild-type plants in terms of growth and development, as well as ascorbate levels
additional information
generation of a mutant lacking all three DHAR isozymes (DELTAdhar), the mutant has negligible DHAR activity, but it is shown to be equivalent to wild-type plants in terms of growth and development, as well as ascorbate levels
additional information
generation of a mutant lacking all three DHAR isozymes (DELTAdhar), the mutant has negligible DHAR activity, but it is shown to be equivalent to wild-type plants in terms of growth and development, as well as ascorbate levels
additional information
generation of DELTAdhar Arabidopsis plants as well as a quadruple mutant line combining DELTAdhar with an additional vtc2 mutation that causes ascorbate deficiency. Measurements of ascorbate in these mutants under low- or high-light conditions indicate that DHARs have a nonnegligible impact on full ascorbate accumulation under high light, but that they are dispensable when ascorbate concentrations are low to moderate. Because GSH itself can reduce DHA nonenzymatically, the pad2 mutant is used that contains about 30% of the wild-type GSH level. The pad2 mutant accumulates ascorbate at a wild-type level under high light, but when the pad2 mutation is combined with DELTAdhar, there is near-complete inhibition of high-light-dependent ascorbate accumulation. The lack of ascorbate accumulation is consistent with a marked increase in the ascorbate degradation product threonate. These findings indicate that ascorbate recycling capacity is limited in DELTAdhar pad2 plants, and that both DHAR activity and GSH content set a threshold for high-light-induced ascorbate accumulation. Each gene knockout is confirmed by reverse transcription PCR. The measurement of DHAR activity reveals that DHAR1 and DHAR3 are the major isoforms, and that the triple DELTAdhar mutant has negligible DHAR activity. DHAR loss-of-function does not affect MDAR activity
additional information
generation of DELTAdhar Arabidopsis plants as well as a quadruple mutant line combining DELTAdhar with an additional vtc2 mutation that causes ascorbate deficiency. Measurements of ascorbate in these mutants under low- or high-light conditions indicate that DHARs have a nonnegligible impact on full ascorbate accumulation under high light, but that they are dispensable when ascorbate concentrations are low to moderate. Because GSH itself can reduce DHA nonenzymatically, the pad2 mutant is used that contains about 30% of the wild-type GSH level. The pad2 mutant accumulates ascorbate at a wild-type level under high light, but when the pad2 mutation is combined with DELTAdhar, there is near-complete inhibition of high-light-dependent ascorbate accumulation. The lack of ascorbate accumulation is consistent with a marked increase in the ascorbate degradation product threonate. These findings indicate that ascorbate recycling capacity is limited in DELTAdhar pad2 plants, and that both DHAR activity and GSH content set a threshold for high-light-induced ascorbate accumulation. Each gene knockout is confirmed by reverse transcription PCR. The measurement of DHAR activity reveals that DHAR1 and DHAR3 are the major isoforms, and that the triple DELTAdhar mutant has negligible DHAR activity. DHAR loss-of-function does not affect MDAR activity
additional information
generation of DELTAdhar Arabidopsis plants as well as a quadruple mutant line combining DELTAdhar with an additional vtc2 mutation that causes ascorbate deficiency. Measurements of ascorbate in these mutants under low- or high-light conditions indicate that DHARs have a nonnegligible impact on full ascorbate accumulation under high light, but that they are dispensable when ascorbate concentrations are low to moderate. Because GSH itself can reduce DHA nonenzymatically, the pad2 mutant is used that contains about 30% of the wild-type GSH level. The pad2 mutant accumulates ascorbate at a wild-type level under high light, but when the pad2 mutation is combined with DELTAdhar, there is near-complete inhibition of high-light-dependent ascorbate accumulation. The lack of ascorbate accumulation is consistent with a marked increase in the ascorbate degradation product threonate. These findings indicate that ascorbate recycling capacity is limited in DELTAdhar pad2 plants, and that both DHAR activity and GSH content set a threshold for high-light-induced ascorbate accumulation. Each gene knockout is confirmed by reverse transcription PCR. The measurement of DHAR activity reveals that DHAR1 and DHAR3 are the major isoforms, and that the triple DELTAdhar mutant has negligible DHAR activity. DHAR loss-of-function does not affect MDAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic Arabidopsis thaliana overexpressing AtDHAR1 maintain higher levels of ascorbate and chlorophyll with reduced levels of membrane damage compared to control plants following exposure to high light, high temperature, or following MV treatment
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic Arabidopsis thaliana overexpressing AtDHAR1 maintain higher levels of ascorbate and chlorophyll with reduced levels of membrane damage compared to control plants following exposure to high light, high temperature, or following MV treatment
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic Arabidopsis thaliana overexpressing AtDHAR1 maintain higher levels of ascorbate and chlorophyll with reduced levels of membrane damage compared to control plants following exposure to high light, high temperature, or following MV treatment
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic expression of AtDHAR2 in tobacco maintains a higher ascorbate level and its oxidation status compared to wild-type plants, resulting in enhanced tolerance to various stresses including ozone, drought, salt, polyethylene glycol (PEG), and aluminium. In Arabidopsis, disruption of DHAR2 decreases the ascorbate redox state but not its pool size, and plants exhibit increased ozone sensitivity, and glutathione oxidation is inhibited in all three dhar single-mutants following photo-oxidative stress
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic expression of AtDHAR2 in tobacco maintains a higher ascorbate level and its oxidation status compared to wild-type plants, resulting in enhanced tolerance to various stresses including ozone, drought, salt, polyethylene glycol (PEG), and aluminium. In Arabidopsis, disruption of DHAR2 decreases the ascorbate redox state but not its pool size, and plants exhibit increased ozone sensitivity, and glutathione oxidation is inhibited in all three dhar single-mutants following photo-oxidative stress
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic expression of AtDHAR2 in tobacco maintains a higher ascorbate level and its oxidation status compared to wild-type plants, resulting in enhanced tolerance to various stresses including ozone, drought, salt, polyethylene glycol (PEG), and aluminium. In Arabidopsis, disruption of DHAR2 decreases the ascorbate redox state but not its pool size, and plants exhibit increased ozone sensitivity, and glutathione oxidation is inhibited in all three dhar single-mutants following photo-oxidative stress
additional information
-
generation of DELTAdhar Arabidopsis plants as well as a quadruple mutant line combining DELTAdhar with an additional vtc2 mutation that causes ascorbate deficiency. Measurements of ascorbate in these mutants under low- or high-light conditions indicate that DHARs have a nonnegligible impact on full ascorbate accumulation under high light, but that they are dispensable when ascorbate concentrations are low to moderate. Because GSH itself can reduce DHA nonenzymatically, the pad2 mutant is used that contains about 30% of the wild-type GSH level. The pad2 mutant accumulates ascorbate at a wild-type level under high light, but when the pad2 mutation is combined with DELTAdhar, there is near-complete inhibition of high-light-dependent ascorbate accumulation. The lack of ascorbate accumulation is consistent with a marked increase in the ascorbate degradation product threonate. These findings indicate that ascorbate recycling capacity is limited in DELTAdhar pad2 plants, and that both DHAR activity and GSH content set a threshold for high-light-induced ascorbate accumulation. Each gene knockout is confirmed by reverse transcription PCR. The measurement of DHAR activity reveals that DHAR1 and DHAR3 are the major isoforms, and that the triple DELTAdhar mutant has negligible DHAR activity. DHAR loss-of-function does not affect MDAR activity
-
additional information
-
construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3. No effect on phenotype is observed in the absence of stress. When the different dhar mutant combinations are introduced into a catalase-deficient background (cat2), the combined presence of dhar1 and dhar2 decreased GSSG and total glutathione accumulation. When all 3 DHARs are knocked out, cat2-triggered glutathione oxidation is almost completely inhibited
-
additional information
-
construction of a complete set of single, double and triple mutants carrying T-DNAs in isozymes DHAR1, DHAR2, and DHAR3
-
additional information
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Transgenic Arabidopsis thaliana overexpressing AtDHAR1 maintain higher levels of ascorbate and chlorophyll with reduced levels of membrane damage compared to control plants following exposure to high light, high temperature, or following MV treatment
-
additional information
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
generation of truncated mutants CrDHAR1DELTAN (amino acids 5-226) or CrDHAR1DELTAC (amino acids 1-218)
additional information
-
generation of truncated mutants CrDHAR1DELTAN (amino acids 5-226) or CrDHAR1DELTAC (amino acids 1-218)
additional information
construcution of different mutants with containing cysteine-to-serine mutations and/or C-terminal residues deleted, kinetic analysis
additional information
construcution of different mutants with containing cysteine-to-serine mutations and/or C-terminal residues deleted, kinetic analysis
additional information
-
construcution of different mutants with containing cysteine-to-serine mutations and/or C-terminal residues deleted, kinetic analysis
additional information
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity. Despite only a small increase in ascorbate content, transgenic Arabidopsis thaliana expressing OsDHAR are more tolerant to salt stress than control plants. Even small changes in DHAR activity may improve tolerance to some environmental stresses
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
-
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
-
construction of overexpressing potato plants overexpressing both the cytosolic and the plastidic isozyme. the trangenic plants overexpressing the cytosolic isozyme show highly increased DHAR activities and ascorbate contents in leaves and tubers, while the plants overexpressing the plastidic isozyme show highly increased DHAR activities and ascorbate contents only in leaves, not in tubers
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
additional information
site-directed mutagenesis of the catalytic cysteine abolishes DHAR activity
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Crystallization and preliminary X-ray crystallographic studies of dehydroascorbate reductase (DHAR) from Oryza sativa L. japonica
Acta Crystallogr. Sect. F
70
781-785
2014
Oryza sativa Japonica Group (Q65XA0)
brenda
Krishna Das, B.; Kumar, A.; Maindola, P.; Mahanty, S.; Jain, S.K.; Reddy, M.K.; Arockiasamy, A.
Non-native ligands define the active site of Pennisetum glaucum (L.) R. Br dehydroascorbate reductase
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473
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Cenchrus americanus
brenda
Lallement, P.A.; Roret, T.; Tsan, P.; Gualberto, J.M.; Girardet, J.M.; Didierjean, C.; Rouhier, N.; Hecker, A.
Insights into ascorbate regeneration in plants investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa
Biochem. J.
473
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2016
Populus trichocarpa
brenda
Noshi, M.; Hatanaka, R.; Tanabe, N.; Terai, Y.; Maruta, T.; Shigeoka, S.
Redox regulation of ascorbate and glutathione by a chloroplastic dehydroascorbate reductase is required for high-light stress tolerance in Arabidopsis
Biosci. Biotechnol. Biochem.
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2016
Arabidopsis thaliana
brenda
Noshi, M.; Yamada, H.; Hatanaka, R.; Tanabe, N.; Tamoi, M.; Shigeoka, S.
Arabidopsis dehydroascorbate reductase 1 and 2 modulate redox states of ascorbate-glutathione cycle in the cytosol in response to photooxidative stress
Biosci. Biotechnol. Biochem.
81
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2017
Arabidopsis thaliana
brenda
Huang, G.J.; Deng, J.S.; Chen, H.J.; Huang, S.S.; Shih, C.C.; Lin, Y.H.
Dehydroascorbate reductase and monodehydroascorbate reductase activities of two metallothionein-like proteins from sweet potato (Ipomoea batatas [L.] Lam. Tainong 57) storage roots
Bot. Stud.
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2013
Ipomoea batatas
brenda
Chang, L.; Sun, H.; Yang, H.; Wang, X.; Su, Z.; Chen, F.; Wei, W.
Over-expression of dehydroascorbate reductase enhances oxidative stress tolerance in tobacco
Electron. J. Biotechnol.
25
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2017
Jatropha curcas (R9QAK3)
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brenda
Kim, Y.; Kim, I.; Shin, S.; Park, T.; Park, H.; Kim, Y.; Lee, G.; Kang, H.; Lee, S.; Yoon, H.
Overexpression of dehydroascorbate reductase confers enhanced tolerance to salt stress in rice plants (Oryza sativa L. japonica)
J. Agron. Crop Sci.
200
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2014
Oryza sativa Japonica Group (Q65XA0)
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brenda
Han, E.; Goo, Y.; Kim, Y.; Lee, S.
Proteomic analysis of dehydroascorbate reductase transgenic potato plants
J. Plant Biotechnol.
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2016
Sesamum indicum
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brenda
Shin, S.Y.; Kim, M.H.; Kim, Y.H.; Park, H.M.; Yoon, H.S.
Co-expression of monodehydroascorbate reductase and dehydroascorbate reductase from Brassica rapa effectively confers tolerance to freezing-induced oxidative stress
Mol. Cells
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2013
Brassica rapa
brenda
Xue, Y.; Miyakawa, T.; Nakamura, A.; Hatano, K.; Sawano, Y.; Tanokura, M.
Yam tuber storage protein reduces plant oxidants using the coupled reactions as carbonic anhydrase and dehydroascorbate reductase
Mol. Plant
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2015
Dioscorea japonica
brenda
Lin, S.T.; Chiou, C.W.; Chu, Y.L.; Hsiao, Y.; Tseng, Y.F.; Chen, Y.C.; Chen, H.J.; Chang, H.Y.; Lee, T.M.
Enhanced ascorbate regeneration via dehydroascorbate reductase confers tolerance to photo-oxidative stress in Chlamydomonas reinhardtii
Plant Cell Physiol.
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Chlamydomonas reinhardtii (A8I0K9), Chlamydomonas reinhardtii
brenda
Pandey, P.; Achary, V.M.; Kalasamudramu, V.; Mahanty, S.; Reddy, G.M.; Reddy, M.K.
Molecular and biochemical characterization of dehydroascorbate reductase from a stress adapted C4 plant, pearl millet [Pennisetum glaucum (L.) R. Br]
Plant Cell Rep.
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2014
Cenchrus americanus (U5XYA0), Cenchrus americanus
brenda
Liu, F.; Guo, X.; Yao, Y.; Tang, W.; Zhang, W.; Cao, S.; Han, Y.; Liu, Y.
Cloning and function characterization of two dehydroascorbate reductases from kiwifruit (Actinidia chinensis L.)
Plant Mol. Biol. Rep.
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2016
Actinidia chinensis
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brenda
Zhang, Y.J.; Wang, W.; Yang, H.L.; Li, Y.; Kang, X.Y.; Wang, X.R.; Yang, Z.L.
Molecular Properties and functional divergence of the dehydroascorbate reductase gene family in lower and higher plants
PLoS ONE
10
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2015
Arabidopsis thaliana (Q9FWR4), Brachypodium distachyon, Picea abies, Pinus taeda, Populus trichocarpa, Selaginella moellendorffii, Zea mays
brenda
Do, H.; Kim, I.S.; Jeon, B.W.; Lee, C.W.; Park, A.K.; Wi, A.R.; Shin, S.C.; Park, H.; Kim, Y.S.; Yoon, H.S.; Kim, H.W.; Lee, J.H.
Structural understanding of the recycling of oxidized ascorbate by dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica
Sci. Rep.
6
19498
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Oryza sativa Japonica Group (Q65XA0)
brenda
Bodra, N.; Young, D.; Astolfi Rosado, L.; Pallo, A.; Wahni, K.; De Proft, F.; Huang, J.; Van Breusegem, F.; Messens, J.
Arabidopsis thaliana dehydroascorbate reductase 2 Conformational flexibility during catalysis
Sci. Rep.
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42494
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Arabidopsis thaliana
brenda
Gao, X.-H.; Zaffagnini, M.; Bedhomme, M.; Michelet, L.; Cassier-Chauvat, C.; Decottignies, P.; Lemaire, S.D.
Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii kinetics and specificity in deglutathionylation reactions
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Chlamydomonas reinhardtii (A8IYH1), Chlamydomonas reinhardtii (A8JHA9)
brenda
Zaffagnini, M.; Michelet, L.; Massot, V.; Trost, P.; Lemaire, S.D.
Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin
J. Biol. Chem.
283
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Chlamydomonas reinhardtii (A8JHA9), Chlamydomonas reinhardtii
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Choudhury, S.; Moulick, D.; Mazumder, M.
Secondary metabolites protect against metal and metalloid stress in rice an in silico investigation using dehydroascorbate reductase
Acta Physiol. Plant.
43
3
2021
Oryza sativa Japonica Group (Q65XA0)
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brenda
Loi, M.; Leonardis, S.; Mul, G.; Logrieco, A.; Paciolla, C.
A novel and potentially multifaceted dehydroascorbate reductase increasing the antioxidant systems is induced by beauvericin in tomato
Antioxidants (Basel)
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435
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Solanum lycopersicum (Q4VDN8), Solanum lycopersicum
brenda
Saruta, F.; Yamada, N.; Yamamoto, K.
An omega-class glutathione S-transferase in the brown planthopper Nilaparvata lugens exhibits glutathione transferase and dehydroascorbate reductase activities
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Nilaparvata lugens (J9Q3Y4), Nilaparvata lugens
brenda
Ding, H.; Wang, B.; Han, Y.; Li, S.
The pivotal function of dehydroascorbate reductase in glutathione homeostasis in plants
J. Exp. Bot.
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2020
Acer saccharinum, Actinidia chinensis, Avena sativa, Brassica napus, Hordeum vulgare, Pisum sativum, Populus trichocarpa, Populus trichocarpa (D2WL73), Populus trichocarpa (D2WL74), Populus trichocarpa (D2WL75), Liriodendron chinense (A0A6C0W973), Pinus bungeana (B2ZHM6), Zea mays (C0P9V2), Ipomoea batatas (D2CGD4), Populus tomentosa (J9WN12), Populus tomentosa (J9WNR5), Populus tomentosa (J9WQY6), Solanum tuberosum (M1BA41), Oryza sativa Japonica Group (Q65XA0), Arabidopsis thaliana (Q8LE52), Arabidopsis thaliana (Q9FRL8), Arabidopsis thaliana (Q9FWR4), Spinacia oleracea (Q9T2H6), Cenchrus americanus (U5XYA0), Arabidopsis thaliana Col-0 (Q9FWR4)
brenda
Dell'Aglio, L.; Mhamdi, A.
What are the roles for dehydroascorbate reductases and glutathione in sustaining ascorbate accumulation?
Plant Physiol.
183
11-12
2020
Nicotiana benthamiana, Zea mays (C0P9V2), Arabidopsis thaliana (Q8LE52), Arabidopsis thaliana (Q9FRL8), Arabidopsis thaliana (Q9FWR4)
brenda
Terai, Y.; Ueno, H.; Ogawa, T.; Sawa, Y.; Miyagi, A.; Kawai-Yamada, M.; Ishikawa, T.; Maruta, T.
Dehydroascorbate reductases and glutathione set a threshold for high-light-induced ascorbate accumulation
Plant Physiol.
183
112-122
2020
Arabidopsis thaliana (Q8LE52), Arabidopsis thaliana (Q9FRL8), Arabidopsis thaliana (Q9FWR4), Arabidopsis thaliana Col-0 (Q8LE52), Arabidopsis thaliana Col-0 (Q9FRL8), Arabidopsis thaliana Col-0 (Q9FWR4)
brenda
Chang, H.Y.; Lin, S.T.; Ko, T.P.; Wu, S.M.; Lin, T.H.; Chang, Y.C.; Huang, K.F.; Lee, T.M.
Enzymatic characterization and crystal structure analysis of Chlamydomonas reinhardtii dehydroascorbate reductase and their implications for oxidative stress
Plant Physiol. Biochem.
120
144-155
2017
Chlamydomonas reinhardtii (A8I0K9), Chlamydomonas reinhardtii
brenda
Rahantaniaina, M.S.; Li, S.; Chatel-Innocenti, G.; Tuzet, A.; Mhamdi, A.; Vanacker, H.; Noctor, G.
Glutathione oxidation in response to intracellular H2O2 key but overlapping roles for dehydroascorbate reductases
Plant Signal. Behav.
12
e1356531
2017
Arabidopsis thaliana (Q8LE52), Arabidopsis thaliana (Q9FRL8), Arabidopsis thaliana (Q9FWR4), Arabidopsis thaliana Col-0 (Q8LE52), Arabidopsis thaliana Col-0 (Q9FRL8), Arabidopsis thaliana Col-0 (Q9FWR4)
brenda