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(E)-4-hydroxyphenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase]
1-aci-nitro-2-(4-hydroxyphenyl)-ethane + H2O + [oxidized NADPH-hemoprotein reductase]
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(E)-indol-3-ylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + glutathione + O2
S-[(E)-N-hydroxy(indol-3-yl)acetimidoyl]-L-glutathione + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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overall reaction
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(E)-p-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + glutathione + O2
S-[(Z)-N-hydroxy(p-hydroxyphenyl)acetimidoyl]-L-glutathione + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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overall reaction
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(E)-p-hydroxyphenylacetaldoxime + NADPH + H+ + 2-mercaptoethanol
(Z)-2-hydroxyethyl N,4-dihydroxybenzene-1-carboximidothioate + NADP+ + H2O
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CYP83B1 shows absolute specificity towards (E)-p-hydroxyphenylacetaldoxime as a substrate, and the (Z)-S-alkyl-thiohydroximate formed maintains the structural configuration of the oxime function as in the (E)-p-hydroxyphenylacetaldoxime substrate
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(E)-phenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + glutathione + O2
S-[(Z)-N-hydroxy(phenyl)acetimidoyl]-L-glutathione + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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overall reaction
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(E)-phenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase]
1-aci-nitro-2-phenylethane + H2O + [oxidized NADPH-hemoprotein reductase]
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1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol
(Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
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an (E)-omega-(methylthio)alkanal oxime + O2 + glutathione + [reduced NADPH-hemoprotein reductase]
an (E)-1-(glutathione-S-yl)-omega-(methylthio)alkylhydroximate + 2 H2O + [oxidized NADPH-hemoprotein reductase]
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indole-3-acetaldoxime + O2 + glutathione + [reduced NADPH-hemoprotein reductase]
1-aci-nitro-2-indolyl-ethane + H2O + [oxidized NADPH-hemoprotein reductase]
indole-3-acetaldoxime + [reduced NADPH-hemoprotein reductase] + O2
1-aci-nitro-2-indolyl-ethane + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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the aci-nitro compound formed reacts non-enzymatically with thiol compounds to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates
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p-hydroxyphenylacetaldoxime + [reduced NADPH-hemoprotein reductase] + cysteine + O2
S-(benzohydroximoyl)-L-cysteine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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overall reaction
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?
p-hydroxyphenylacetaldoxime + [reduced NADPH-hemoprotein reductase] + N-acetylcysteine + O2
S-(benzohydroximoyl)-N-acetyl-L-cysteine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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overall reaction
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additional information
?
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indole-3-acetaldoxime + O2 + glutathione + [reduced NADPH-hemoprotein reductase]
1-aci-nitro-2-indolyl-ethane + H2O + [oxidized NADPH-hemoprotein reductase]
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-
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?
indole-3-acetaldoxime + O2 + glutathione + [reduced NADPH-hemoprotein reductase]
1-aci-nitro-2-indolyl-ethane + H2O + [oxidized NADPH-hemoprotein reductase]
indole-3-acetaldoxime is the physiological substrate for CYP83B1
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additional information
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CYP83B1 catalyzes the conversion of the (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-thiohydroximate with retention of the configuration of the E-oxime intermediate in the final glucosinolate core structure. CYP83B1 from Arabidopsis thaliana cannot convert the (E)-p-hydroxyphenylacetaldoxime to the (Z)-isomer, which blocks the route towards cyanogenic glucoside synthesis
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additional information
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CYP83B1 cannot convert the (E)-p-hydroxyphenylacetaldoxime to the (Z)-isomer, which blocks the route towards cyanogenic glucoside synthesis. Instead CYP83B1 catalyzes the conversion of the (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-thiohydroximate with retention of the configuration of the E-oxime intermediate in the final glucosinolate core structure
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additional information
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CYP83B1 metabolizes aliphatic oximes with very low efficiency
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additional information
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isoform CYP83A1 catalyzes the initial conversion of aldoximes to thiohydroximates in the synthesis of glucosinolates not derived from tryptophan
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(E)-4-hydroxyphenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase]
1-aci-nitro-2-(4-hydroxyphenyl)-ethane + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
(E)-indol-3-ylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + glutathione + O2
S-[(E)-N-hydroxy(indol-3-yl)acetimidoyl]-L-glutathione + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
overall reaction
-
?
(E)-p-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + glutathione + O2
S-[(Z)-N-hydroxy(p-hydroxyphenyl)acetimidoyl]-L-glutathione + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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overall reaction
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?
(E)-phenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + glutathione + O2
S-[(Z)-N-hydroxy(phenyl)acetimidoyl]-L-glutathione + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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overall reaction
-
?
1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol
(Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
-
-
-
?
an (E)-omega-(methylthio)alkanal oxime + O2 + glutathione + [reduced NADPH-hemoprotein reductase]
an (E)-1-(glutathione-S-yl)-omega-(methylthio)alkylhydroximate + 2 H2O + [oxidized NADPH-hemoprotein reductase]
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-
-
?
indole-3-acetaldoxime + [reduced NADPH-hemoprotein reductase] + O2
1-aci-nitro-2-indolyl-ethane + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
the aci-nitro compound formed reacts non-enzymatically with thiol compounds to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates
-
?
additional information
?
-
CYP83B1 catalyzes the conversion of the (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-thiohydroximate with retention of the configuration of the E-oxime intermediate in the final glucosinolate core structure. CYP83B1 from Arabidopsis thaliana cannot convert the (E)-p-hydroxyphenylacetaldoxime to the (Z)-isomer, which blocks the route towards cyanogenic glucoside synthesis
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-
?
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physiological function
a CYP83B1 knockout mutant, rnt1-1, leads to the the presence of indole glucosinolates at various levels in different developmental stages. Plants overexpressing CYP83B1 contain elevated levels of aliphatic glucosinolates derived from methionine homologs, whereas the level of indole glucosinolates is almost constant in the overexpressing lines
physiological function
a T-DNA insertion in the CYP83B1 gene leads to plants with a phenotype that suggests severe auxin overproduction. Mutant seedlings are characterized by increased hypocotyl length, epinastic cotyledons, exfoliation of the hypocotyl, adventitious root formation from the hypocotyl, enhanced secondary root and root hair formation, and eventually callus formation and increasing disintegration of the seedling. Mutant seedlings contain reduced levels of indole glucosinolates. CYP83B1 overexpression leads to loss of apical dominance typical of auxin deficit
physiological function
aliphatic oximes derived from chain-elongated homologs of methionine are efficiently metabolized by isoform CYP83A1, whereas CYP83B1 metabolizes these substrates with very low efficiency. Aromatic oximes derived from phenylalanine, tryptophan, and tyrosine are metabolized by both enzymes, although CYP83B1 has higher affinity for these substrates than CYP83A1. Plants overexpressing CYP83B1 contain elevated levels of aliphatic glucosinolates derived from methionine homologs, whereas the level of indole glucosinolates is almost constant in the overexpressing lines
physiological function
lack of the CYP83B1 gene product leads to auxin excess and indole glucosinolate deficit, ectopic overexpression of CYP83A1 using a 35S promoter rescues phenotype. Indole-3-acetaldoxime has a 50-fold higher affinity toward CYP83B1 than toward CYP83A1, EC 1.14.14.43. Both enzymes also metabolize the phenylalanine- and tyrosine-derived aldoximes. Indole-3-acetaldoxime is the physiological substrate for CYP83B1
physiological function
model for the biosynthesis of Trp-derived glucosinolates and camalexin in Arabidopsis thaliana. The two first enzymes in biosynthesis are cytochromes P450 of the families CYP79 and CYP83, respectively. They convert the amino acids to activated aldoximes that react spontaneously with thiols to form thiol conjugates
physiological function
mutant plants have constitutively activated expression of the Atr1 Myb factor gene. The Atr1D mutant enhances the adventitious root formation of Cyp83B1 mutants, and Axr1, involved in RUB1 post-translational modifications, is necessary for cyp83B1 5-methyl tryptophan resistance. Cyp83B1 mutants have lesion-mimic phenotypes, suggesting that multiple stress pathways are activated by loss of Cyp83B1 function
physiological function
reduced epidermal fluorescence5 (ref5-1) mutant, identified leading to plants with defects in soluble phenylpropanoid accumulation, has a missense mutation in CYP83B1 and displays defects in glucosinolate biosynthesis and in phenylpropanoid accumulation
physiological function
the two key glucosinolate synthetic genes CYP83A1 and CYP83B1 are highly conserved within the Brassicaceae family
physiological function
inactivation of CYP83B1 leads to plants with a phenotype that suggests severe auxin overproduction, whereas CYP83B1 overexpression leads to loss of apical dominance typical of auxin deficit
physiological function
knockout of CYP83B1 leads to a strong auxin excess phenotype
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Clausen, M.; Kannangara, R.M.; Olsen, C.E.; Blomstedt, C.K.; Gleadow, R.M.; Jorgensen, K.; Bak, S.; Motawie, M.S.; Moller, B.L.
The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways
Plant J.
84
558-573
2015
Arabidopsis thaliana (O65782)
brenda
Smolen, G.; Bender, J.
Arabidopsis cytochrome P450 cyp83B1 mutations activate the tryptophan biosynthetic pathway
Genetics
160
323-332
2002
Arabidopsis thaliana (O65782), Arabidopsis thaliana
brenda
Zhu, B.; Wang, Z.; Yang, J.; Zhu, Z.; Wang, H.
Isolation and expression of glucosinolate synthesis genes CYP83A1 and CYP83B1 in Pak Choi (Brassica rapa L. ssp. chinensis var. communis (N. Tsen & S.H. Lee) Hanelt)
Int. J. Mol. Sci.
13
5832-5843
2012
Brassica rapa subsp. chinensis (B6VC79)
brenda
Hansen, C.H.; Du, L.; Naur, P.; Olsen, C.E.; Axelsen, K.B.; Hick, A.J.; Pickett, J.A.; Halkier, B.A.
CYP83B1 is the oxime-metabolizing enzyme in the glucosinolate pathway in Arabidopsis
J. Biol. Chem.
276
24790-24796
2001
Arabidopsis thaliana (O65782), Arabidopsis thaliana
brenda
Bak, S.; Tax, F.E.; Feldmann, K.A.; Galbraith, D.W.; Feyereisen, R.
CYP83B1, a cytochrome P450 at the metabolic branch point in auxin and indole glucosinolate biosynthesis in Arabidopsis
Plant Cell
13
101-111
2001
Arabidopsis thaliana (O65782)
brenda
Geu-Flores, F.; Moldrup, M.; Bttcher, C.; Olsen, C.; Scheel, D.; Halkier, B.
Cytosolic gamma-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in Arabidopsis
Plant Cell
23
2456-2469
2011
Arabidopsis thaliana (O65782)
brenda
Kim, J.I.; Dolan, W.L.; Anderson, N.A.; Chapple, C.
Indole glucosinolate biosynthesis limits phenylpropanoid accumulation in Arabidopsis thaliana
Plant Cell
27
1529-1546
2015
Arabidopsis thaliana (O65782), Arabidopsis thaliana
brenda
Bak, S.; Feyereisen, R.
The involvement of two p450 enzymes, CYP83B1 and CYP83A1, in auxin homeostasis and glucosinolate biosynthesis
Plant Physiol.
127
108-118
2001
Arabidopsis thaliana (O65782)
brenda
Naur, P.; Petersen, B.L.; Mikkelsen, M.D.; Bak, S.; Rasmussen, H.; Olsen, C.E.; Halkier, B.A.
CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis
Plant Physiol.
133
63-72
2003
Arabidopsis thaliana (O65782)
brenda
Bak, S.; Tax, F.; Feldmann, K.; Galbraith, D.; Feyereisen, R.
CYP83B1, a cytochrome P450 at the metabolic branch point in auxin and indole glucosinolate biosynthesis in Arabidopsis
Plant Cell
13
101-111
2001
Arabidopsis thaliana (O65782)
brenda
Clausen, M.; Kannangara, R.; Olsen, C.; Blomstedt, C.; Gleadow, R.; Jrgensen, K.; Bak, S.; Motawie, M.; Mller, B.
The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways
Plant J.
84
558-573
2015
Arabidopsis thaliana (O65782)
brenda
Bak, S.; Feyereisen, R.
The involvement of two p450 enzymes, CYP83B1 and CYP83A1, in auxin homeostasis and glucosinolate biosynthesis
Plant Physiol.
127
108-118
2001
Arabidopsis thaliana (O65782)
brenda