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2,3-butandione + NAD(P)H
butan-2-ol-3-one + NAD(P)+
-
33 mM, 12% of activity with hydroxypyruvate
-
?
2-dehydro-D-gluconate + NADPH + H+
D-gluconate + NADP+
-
-
-
?
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
acetoin + NAD(P)H + H+
2,3-butanediol + NAD(P)+
-
33 mM, 14% of activity with hydroxypyruvate
-
?
D-glycerate + NAD+
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
-
-
-
r
DL-glycerate + NAD+
3-hydroxypyruvate + NADH + H+
-
-
-
-
r
glyoxylate + NAD(P)H
glycolate + NAD(P)+
glyoxylate + NAD(P)H + H+
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NADH
glycolate + NAD+
-
-
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
glyoxylate + NADPH
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
-
-
-
?
hydroxypyruvate + NADH
D-glycerate + NAD+
-
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
hydroxypyruvate + NADPH
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
oxaloacetate + NAD(P)H
malate + NAD(P)+
-
33 mM, 32% of activity with hydroxypyruvate
-
?
phenylpyruvate + NADPH + H+
D-phenyllactate + NADP+
-
-
-
?
phenylpyruvate + NADPH + H+
phenyllactate + NADP+
pyruvate + NADPH + H+
lactate + NADP+
-
-
-
?
additional information
?
-
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
r
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
r
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
ir
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
ir
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
ir
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
ir
3-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
ir
3-hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
?
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
reaction of EC 1.1.1.237
-
-
?
D-glycerate + NAD+
3-hydroxypyruvate + NADH + H+
-
-
-
-
r
D-glycerate + NAD+
3-hydroxypyruvate + NADH + H+
-
-
-
-
r
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
-
-
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
the enzyme is involved in removal of the metabolic by-product from liver
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
cofactor NADH, 15% of activity with hydroxypyruvate, cofactor NADPH, 1.5% of activity with hydroxypyruvate
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
33 mM, 15% activity
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
activity with hydroxypyruvate and NADPH is 2fold higher than with other pair of reactants
-
ir
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
97% of the activity with 3-hydroxypyruvate
-
-
ir
glyoxylate + NADH + H+
glycolate + NAD+
97% of the activity with 3-hydroxypyruvate
-
-
ir
glyoxylate + NADH + H+
glycolate + NAD+
-
24% of the activity with 3-hydroxypyruvate
-
-
ir
glyoxylate + NADH + H+
glycolate + NAD+
-
60% of the activity with 3-hydroxypyruvate
-
-
ir
glyoxylate + NADH + H+
glycolate + NAD+
-
60% of the activity with 3-hydroxypyruvate
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
r
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
cofactor NADPH, 80% of activity with NADH, rate of oxidation reaction: 1.5% of reduction reaction only with cofactor NADH
-
r
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?, r
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?, ir
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
low activity
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
low activity
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
r
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
r
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
r
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADPH
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH
D-glycerate + NADP+
-
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
best substrate
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
isoform HPR3 prefers NADPH over NADH and glyoxylate over hydroxypyvruvate
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?, r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
key enzyme of the serine cycle
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
key enzyme of the serine cycle
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
phenylpyruvate + NADPH + H+
phenyllactate + NADP+
-
-
-
?
phenylpyruvate + NADPH + H+
phenyllactate + NADP+
-
-
-
?
additional information
?
-
the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
-
-
?
additional information
?
-
the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
-
-
?
additional information
?
-
the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
-
-
?
additional information
?
-
the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
-
-
?
additional information
?
-
the enzyme GLYR1 has negligible hydroxypyruvate dependent activity with NADPH
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
enzyme HPR2 shows relaxed substrate and cofactor specificity, it also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79). Irreversibility of the HPR2 reaction has been reported
-
-
-
additional information
?
-
-
enzyme HPR2 shows relaxed substrate and cofactor specificity, it also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79). Irreversibility of the HPR2 reaction has been reported
-
-
-
additional information
?
-
the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
-
-
-
additional information
?
-
the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
-
-
-
additional information
?
-
isoform HPPR2 has both hydroxyphenylpyruvate reductase and hydroxypyruvate reductase activities
-
-
-
additional information
?
-
enzyme HPR2 shows relaxed substrate and cofactor specificity, it also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79). Irreversibility of the HPR2 reaction has been reported
-
-
-
additional information
?
-
the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
-
-
-
additional information
?
-
the enzyme also has glyoxylate reductase (NADP+) activity (EC 1.1.1.79)
-
-
-
additional information
?
-
-
enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
-
-
?
additional information
?
-
-
structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview
-
-
?
additional information
?
-
enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
-
-
-
additional information
?
-
enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
-
-
-
additional information
?
-
-
enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
-
-
-
additional information
?
-
-
enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
-
-
-
additional information
?
-
-
enzyme catalyzes NAD(P)H-dependent reduction of hydroxypyruvate or glyoxylate, but does not catalyze the reverse reactions of D-glycerate or glycolate oxidation. No substrates: pyruvate, lactate, oxaloacetate, and 2-oxoglutarate
-
-
-
additional information
?
-
-
the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-hydroxyphenylpyruvate + NADPH + H+
3-(4-hydroxyphenyl)lactate + NADP+
-
-
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
-
-
-
r
glyoxylate + NAD(P)H
glycolate + NAD(P)+
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
hydroxypyruvate + NAD(P)H + H+
D-glycerate + NAD(P)+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
hydroxypyruvate + NADPH
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
additional information
?
-
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
-
-
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
the enzyme is involved in removal of the metabolic by-product from liver
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
cofactor NADPH, 80% of activity with NADH, rate of oxidation reaction: 1.5% of reduction reaction only with cofactor NADH
-
r
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
r
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
key enzyme of the serine cycle
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
key enzyme of the serine cycle
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glycerate to hydroxypyruvate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR1 prefers NADH over NADPH and hydroxypyruvate over glyoxylate. Isozyme AtHPR1 also converts glyoxylate to glycolate, albeit with much lower catalytic efficiency than for hydroxypyruvate
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
?
additional information
?
-
-
enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
-
-
?
additional information
?
-
-
the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2,3-diphospho-D-glycerate
-
1 mM, 83% and 91% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
2-oxoglutarate
-
5 mM, 80% of initial activity
2-phospho-DL-glycerate
-
1 mM, 93% and 81% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
3-phospho-D-glycerate
-
1 mM, 53% and 65% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
Ag+
-
0.1 mM, complete inhibition
alpha-D-fructose 1,6-diphosphate
-
0.1 mM, 28% and 74% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
Cl-
-
100 mM, 50% inhibition of D-glycerate oxidation
CTP
-
1 mM, 73% and 71% inhibition of liver and spinal cord enzyme respectively
glycolate
-
5 mM, 15% of NADPH linked reduction
glyoxylate
-
10 mM, 55% inhibition of NADH linked hydroxypyruvate reduction, 15% of NADPH linked reduction, 80% of NAD+ linked glycerate oxidation
GTP
-
1 mM, 94% and 93% inhibition of liver and spinal cord enzyme respectively
Hg2+
-
0.1 mM, complete inhibition
NaNO3
-
80 mM, 50% inhibition
NO3-
-
100 mM, 87% inhibition of D-glycerate oxidation
oxaloacetate
-
2.5 mM, 10% inhibition of NADH linked hydroxypyruvate reduction, 20% of NADPH linked reduction
p-chloromercuribenzoate
-
0.1 mM, complete inhibition
SO42-
-
100 mM, 55% inhibition of D-glycerate oxidation
Sodium bisulfite
-
0.01 mM, 16% inhibition, 0.1 mM, 67% inhibition
UTP
-
1 mM, 83% and 84% inhibition of liver and spinal cord enzyme respectively
additional information
-
not inhibited by 2 mM acetohydroxamate
-
acetyl-CoA
5 mM, 58% of initial activity
acetyl-CoA
-
5 mM, 58% of initial activity
ADP
5 mM, 94% of initial activity
ADP
-
5 mM, 78% of initial activity
ATP
-
1 mM, 62% and 64% inhibition of liver and spinal cord enzyme respectively, 73% and 89% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
ATP
5 mM, 78% of initial activity
ATP
-
5 mM, 57% of initial activity
bromide
-
100 mM, 70% inhibition of D-glycerate oxidation
bromide
-
33 mM, 38% inhibition
citrate
-
5 mM, 20% inhibition of NADH linked hydroxypyruvate reduction, 25% of NADPH linked reduction
citrate
-
competitive vs. hydroxypyruvate
D-glycerate
-
the enzyme shows product inhibition
D-glycerate
-
5 mM, 20% inhibition of NADH linked hydroxypyruvate reduction, 40% of NADPH linked reduction
glucose 6-phosphate
5 mM, 49% of initial activity
glucose 6-phosphate
-
5 mM, 91% of initial activity
Hydroxypyruvate
-
substrate inhibition at high concentrations
Hydroxypyruvate
-
2 mM, 79% inhibition of enzyme activity in LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase
Hydroxypyruvate
-
0.5 mM, 90% of NAD+ linked glycerate oxidation
Iodide
-
100 mM, 90% inhibition of D-glycerate oxidation
Iodide
-
33 mM, 39% inhibition
NAD+
1 mM, substrate NADH, 92% of initial activity; 1 mM, substrate NADPH, 54% of initial activity
NAD+
-
4 mM, 10% inhibition of NADH linked hydroxypyruvate reduction, 60% of NADPH linked reduction
NAD+
-
1 mM, substrate NADH, 86% of initial activity; 1 mM, substrate NADPH, 72% of initial activity
NAD+
-
1 mM, substrate NADPH, 64% of initial activity
NADP+
-
4 mM, 15% inhibition of NADH linked hydroxypyruvate reduction, 40% of NADPH linked reduction, 8% of NAD+ linked glycerate oxidation
NADP+
-
1 mM, substrate NADH, 81% of initial activity; 1 mM, substrate NADPH, 87% of initial activity
oxalate
strong inhibition of HPR2
oxalate
strong inhibition
oxalate
strong inhibition
oxalate
-
2 mM, 90% inhibition
phosphate
5 mM, 67% of initial activity
phosphate
-
5 mM, 67% of initial activity
phosphoenolpyruvate
5 mM, 41% of initial activity
phosphoenolpyruvate
-
5 mM, 41% of initial activity
phosphoenolpyruvate
-
5 mM, 41% of initial activity
phosphohydroxypyruvate
-
0.025 mM, 66% and 64% inhibition of liver and spinal cord enzyme respectively
phosphohydroxypyruvate
-
2 mM, 44-71% inhibition
pyruvate
-
1 mM, 73% and 89% inhibition of hydroxypyruvate reduction and D-glycerate oxidation respectively
pyruvate
5 mM, 78% of initial activity
pyruvate
-
10 mM, 40% inhibition of NADH linked hydroxypyruvate reduction
pyruvate
-
5 mM, 67% of initial activity
pyruvate
-
5 mM, 78% of initial activity
ribulose 5-phosphate
5 mM, 47% of initial activity
ribulose 5-phosphate
-
5 mM, 47% of initial activity
Tartronate
-
2 mM, 83% inhibition of enzyme activity in LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase
Tartronate
-
2 mM, 30-55% inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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11
2-dehydro-D-gluconate
pH 7.5, 25°C
0.057 - 9.35
3-hydroxypyruvate
0.8
4-hydroxyphenylpyruvate
pH 7.0, 30°C, recombinant enzyme
0.522
D-glycerate
-
D-glycerate oxidation, 50 mM, NaCl, pH 9
0.0038 - 40
Hydroxypyruvate
1.5 - 6.58
phenylpyruvate
9.69
pyruvate
pH 7.5, 25°C
0.057
3-hydroxypyruvate
cosubstrate NADH, pH 7, 37°C
0.14
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 30°C
0.17
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 37°C
0.5
3-hydroxypyruvate
cosubstrate NADPH, pH 7, 37°C
0.6
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 37°C
1.2
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 30°C
6.14
3-hydroxypyruvate
K0.5 value, Hill coefficient 1.74, pH 7.5, 25°C
9.35
3-hydroxypyruvate
pH 7.5, 25°C
3
glyoxylate
-
cosubstrate NADH, pH 7, 37°C
3.9
glyoxylate
cosubstrate NADH, pH 7, 37°C
11
glyoxylate
-
cosubstrate NADPH, pH 7, 37°C
12.3
glyoxylate
K0.5 value, Hill coefficient 1.83, pH 7.5, 25°C
18
glyoxylate
-
cosubstrate NADPH, pH 7, 30°C
22
glyoxylate
-
cosubstrate NADH, pH 7, 30°C
80
glyoxylate
K0.5 value, Hill coefficient 1.48, pH 7.5, 25°C
0.0038
Hydroxypyruvate
-
value increases with NaCl concentrations higher than 10 mM
0.004
Hydroxypyruvate
-
-
0.02
Hydroxypyruvate
-
with NADPH as cosubstrate, at pH 8.0 and 50°C
0.07
Hydroxypyruvate
-
with NADH as cosubstrate, at pH 8.0 and 50°C
0.08
Hydroxypyruvate
-
enzyme activity of wild-type in 40-60% precipitate fractions after ammonium sulfate fractionation
0.09
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50°C
0.1
Hydroxypyruvate
-
cofactor NADH
0.11
Hydroxypyruvate
-
ammonium sulfate fractionated leaf extracts, 45-60% fraction
0.13
Hydroxypyruvate
-
with 0.15 mM NADPH
0.14
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50°C
0.165
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50°C
0.175
Hydroxypyruvate
-
native enzyme
0.189
Hydroxypyruvate
-
purified recombinant enzyme
0.41
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50°C
0.71
Hydroxypyruvate
-
enzyme activity of LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase in 40-60% precipitate fractions after ammonium sulfate fractionation
0.8
Hydroxypyruvate
-
at pH 6.0
1.05
Hydroxypyruvate
pH 7, 30°C
1.05
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
1.25
Hydroxypyruvate
-
cofactor NADPH
2.1
Hydroxypyruvate
-
with 0.15 mM NADH
3.57
Hydroxypyruvate
pH 7, 30°C
6.1
Hydroxypyruvate
GLYR1, at pH 7.8 and 22°C
10
Hydroxypyruvate
-
enzyme in high-salt fraction of DEAE-cellulose chromatography
40
Hydroxypyruvate
-
enzyme in low-salt fraction of DEAE-cellulose chromatography
0.077
NAD+
-
-
0.22
NAD+
-
D-glycerate oxidation, 50 mM, NaCl, pH 9
0.0061
NADH
-
-
0.013
NADH
-
with hydroxypyruvate as substrate, pH 7.5
0.013
NADH
-
cosubsubstrate glyoxylate, 30°C, pH 7
0.015
NADH
-
with glyoxylate as substrate, pH 7.5
0.015
NADH
cosubsubstrate glyoxylate, 37°C, pH 7
0.028
NADH
-
cosubsubstrate 3-hydroxypyruvate, 30°C, pH 7
0.03
NADH
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
0.055
NADH
-
native enzyme
0.064
NADH
-
purified recombinant enzyme
0.07
NADH
-
cosubsubstrate glyoxylate, 37°C, pH 7
0.08
NADH
-
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
0.0105
NADPH
pH 7.5, 25°C
0.021
NADPH
-
with glyoxylate as substrate, pH 7.5
0.025
NADPH
-
with hydroxypyruvate as substrate, pH 7.5
0.028
NADPH
-
cosubsubstrate glyoxylate, 37°C, pH 7
0.055
NADPH
-
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
0.11
NADPH
-
cosubsubstrate 3-hydroxypyruvate, 30°C, pH 7
0.16
NADPH
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
0.22
NADPH
-
cosubsubstrate glyoxylate, 30°C, pH 7
1.5 - 2
phenylpyruvate
pH 7, 30°C
3.7
phenylpyruvate
pH 7, 30°C
3.7
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
5.59
phenylpyruvate
pH 7.5, 25°C
6.58
phenylpyruvate
pH 7.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30 - 687
3-hydroxypyruvate
0.122
4-hydroxyphenylpyruvate
pH 7.0, 30°C, recombinant enzyme
0.05 - 25
Hydroxypyruvate
0.033 - 0.61
phenylpyruvate
30
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 37°C
38
3-hydroxypyruvate
cosubstrate NADPH, pH 7, 37°C
42
3-hydroxypyruvate
cosubstrate NADH, pH 7, 37°C
48
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 37°C
288
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 30°C
687
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 30°C
19
glyoxylate
-
cosubstrate NADH, pH 7, 37°C
41
glyoxylate
cosubstrate NADH, pH 7, 37°C
52
glyoxylate
-
cosubstrate NADPH, pH 7, 30°C
88
glyoxylate
-
cosubstrate NADPH, pH 7, 37°C
166
glyoxylate
-
cosubstrate NADH, pH 7, 30°C
0.05
Hydroxypyruvate
pH 7, 30°C
0.6
Hydroxypyruvate
-
with NADPH as cosubstrate, at pH 8.0 and 50°C
0.927
Hydroxypyruvate
pH 7.0, 30°C, recombinant enzyme
0.93
Hydroxypyruvate
pH 7, 30°C
1.2
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50°C
4.5
Hydroxypyruvate
-
with NADH as cosubstrate, at pH 8.0 and 50°C
6.5
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50°C
10
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50°C
25
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50°C
4.1
NADH
-
with hydroxypyruvate as substrate, pH 7.5
11
NADH
-
with glyoxylate as substrate, pH 7.5
14
NADH
-
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
19
NADH
-
cosubsubstrate glyoxylate, 37°C, pH 7
41
NADH
cosubsubstrate glyoxylate, 37°C, pH 7
42
NADH
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
166
NADH
-
cosubsubstrate glyoxylate, 30°C, pH 7
687
NADH
-
cosubsubstrate 3-hydroxypyruvate, 30°C, pH 7
1.8
NADPH
-
with hydroxypyruvate as substrate, pH 7.5
2.4
NADPH
-
with glyoxylate as substrate, pH 7.5
23
NADPH
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
48
NADPH
-
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
52
NADPH
-
cosubsubstrate glyoxylate, 30°C, pH 7
88
NADPH
-
cosubsubstrate glyoxylate, 37°C, pH 7
284
NADPH
-
cosubsubstrate 3-hydroxypyruvate, 30°C, pH 7
0.033
phenylpyruvate
pH 7, 30°C
0.033
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
0.61
phenylpyruvate
pH 7, 30°C
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0.94
2-dehydro-D-gluconate
pH 7.5, 25°C
1.2 - 4907
3-hydroxypyruvate
0.153
4-hydroxyphenylpyruvate
pH 7.0, 30°C, recombinant enzyme
0.015 - 75
Hydroxypyruvate
0.009 - 0.4
phenylpyruvate
0.057
pyruvate
pH 7.5, 25°C
1.2
3-hydroxypyruvate
pH 7.5, 25°C
9.31
3-hydroxypyruvate
K0.5 value, Hill coefficient 1.74, pH 7.5, 25°C
10.56
3-hydroxypyruvate
cosubstrate NADPH, pH 7, 37°C
50
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 37°C
240
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 30°C
282
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 37°C
737
3-hydroxypyruvate
cosubstrate NADH, pH 7, 37°C
4907
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 30°C
0.81
glyoxylate
K0.5 value, Hill coefficient 1.48, pH 7.5, 25°C
1.72
glyoxylate
Hill coefficient 1.83, pH 7.5, 25°C
2.9
glyoxylate
-
cosubstrate NADPH, pH 7, 30°C
6
glyoxylate
-
cosubstrate NADH, pH 7, 37°C
6
glyoxylate
cosubstrate NADH, pH 7, 37°C
7.5
glyoxylate
-
cosubstrate NADH, pH 7, 30°C
8
glyoxylate
-
cosubstrate NADPH, pH 7, 37°C
0.015
Hydroxypyruvate
pH 7, 30°C
0.232
Hydroxypyruvate
GLYR1, at pH 7.8 and 22°C
0.95
Hydroxypyruvate
pH 7, 30°C
15
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50°C
30
Hydroxypyruvate
-
with NADPH as cosubstrate, at pH 8.0 and 50°C
40
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50°C
60
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50°C
65
Hydroxypyruvate
-
with NADH as cosubstrate, at pH 8.0 and 50°C
75
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50°C
175
NADH
-
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
271
NADH
-
cosubsubstrate glyoxylate, 37°C, pH 7
1400
NADH
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
2733
NADH
cosubsubstrate glyoxylate, 37°C, pH 7
12769
NADH
-
cosubsubstrate glyoxylate, 30°C, pH 7
24535
NADH
-
cosubsubstrate 3-hydroxypyruvate, 30°C, pH 7
143
NADPH
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
236
NADPH
-
cosubsubstrate glyoxylate, 30°C, pH 7
873
NADPH
-
cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7
2582
NADPH
-
cosubsubstrate 3-hydroxypyruvate, 30°C, pH 7
3142
NADPH
-
cosubsubstrate glyoxylate, 37°C, pH 7
0.009
phenylpyruvate
pH 7.0, 30°C, recombinant enzyme
0.009
phenylpyruvate
pH 7, 30°C
0.27
phenylpyruvate
pH 7.5, 25°C
0.37
phenylpyruvate
pH 7.5, 25°C
0.4
phenylpyruvate
pH 7, 30°C
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evolution
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs
evolution
HPR1 and HPR2 are the major hydroxypyruvate-reducing enzymes in leaves
evolution
no hydroxyphenylpyruvate reductase (HPPR) activity by isozyme HPPR4 from Arabidopsis thaliana. Isozyme HPPR2 mainly shows hydroxypyruvate reductase (HPR) activity, while isozyme HPPR3 mainly shows 4-hydroxyphenylpyruvate reductase (EC 1.1.1.237) activity. Enzyme HPPR2 belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, group II
evolution
-
HPR1 and HPR2 are the major hydroxypyruvate-reducing enzymes in leaves
-
malfunction
Arabidopsis thaliana mutants defective in either HPPR2 or HPPR3 isozyme contain lower amounts of pHPL and are impaired in conversion of tyrosine to pHPL. Furthermore, a loss-of-function mutation in tyrosine aminotransferase (TAT) also reduces the pHPL accumulation in plants
malfunction
deletion of HPR2 results in elevated levels of hydroxypyruvate and other metabolites in leaves. Photosynthetic gas exchange is slightly altered, especially under long-day conditions. Otherwise, the mutant closely resembles wild-type plants. The combined deletion of both HPR1 and HPR2 results in distinct air-sensitivity and a dramatic reduction in photosynthetic performance. Knockout of both HPR1 and HPR2 alters steady-state metabolite profiles. Knockout of either HPR1 or HPR2 alters photosynthetic gas exchange
malfunction
deletion of HPR3 results in slightly altered leaf concentrations of the photorespiratory intermediates HP, glycerate, and glycine, indicating a disrupted photorespiratory flux, but not in visible alteration of the phenotype. The combined deletion of HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1xhpr2 double mutant. HPR mutants show impaired growth and contain less chlorophyll, phenotypes, detailed overview
malfunction
deletion of photorespiratory enzymes typically leads to a strong air sensitivity of the respective mutants, which can be fully recovered by elevated-CO2 conditions. While this is a distinctive feature of most photorespiratory mutants, Arabidopsis thaliana HPR1 knockout mutants grow nearly normally in ambient air with moderate photoperiods and show only minor changes in photosynthetic and metabolic parameters under these conditions. The additional deletion of the cytosolic HPR2 distinctly elevates the oxygen sensitivity, but this hpr1xhpr2 double mutant can still survive long-term exposure to ambient air
malfunction
-
Arabidopsis thaliana mutants defective in either HPPR2 or HPPR3 isozyme contain lower amounts of pHPL and are impaired in conversion of tyrosine to pHPL. Furthermore, a loss-of-function mutation in tyrosine aminotransferase (TAT) also reduces the pHPL accumulation in plants
-
malfunction
-
deletion of HPR2 results in elevated levels of hydroxypyruvate and other metabolites in leaves. Photosynthetic gas exchange is slightly altered, especially under long-day conditions. Otherwise, the mutant closely resembles wild-type plants. The combined deletion of both HPR1 and HPR2 results in distinct air-sensitivity and a dramatic reduction in photosynthetic performance. Knockout of both HPR1 and HPR2 alters steady-state metabolite profiles. Knockout of either HPR1 or HPR2 alters photosynthetic gas exchange
-
malfunction
-
deletion of photorespiratory enzymes typically leads to a strong air sensitivity of the respective mutants, which can be fully recovered by elevated-CO2 conditions. While this is a distinctive feature of most photorespiratory mutants, Arabidopsis thaliana HPR1 knockout mutants grow nearly normally in ambient air with moderate photoperiods and show only minor changes in photosynthetic and metabolic parameters under these conditions. The additional deletion of the cytosolic HPR2 distinctly elevates the oxygen sensitivity, but this hpr1xhpr2 double mutant can still survive long-term exposure to ambient air
-
malfunction
-
deletion of HPR3 results in slightly altered leaf concentrations of the photorespiratory intermediates HP, glycerate, and glycine, indicating a disrupted photorespiratory flux, but not in visible alteration of the phenotype. The combined deletion of HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1xhpr2 double mutant. HPR mutants show impaired growth and contain less chlorophyll, phenotypes, detailed overview
-
metabolism
-
NADH-HPR is extensively involved in carbon metabolism
metabolism
in vitro characterization of the recombinant proteins reveals that HPPR2 has both hydroxypyruvate reductase (HPR EC 1.1.1.81, main activity) and hydroxyphenylpyruvate reductase (HPPR, EC 1.1.1.237) activities, whereas HPPR3 has a strong preference for pHPP, and both enzymes are localized in the cytosol. In Arabidopsis thaliana, HPPR2 and HPPR3, together with tyrosine aminotransferase 1 (TAT1), constitute to a probably conserved biosynthetic pathway from tyrosine to 4-hydroxyphenyllactic acid (pHPL), from which some specialized metabolites, such as rosmarinic acid (RA), can be generated in specific groups of plants. Role of HPPR in the tyrosine conversion pathway, overview
metabolism
-
in vitro characterization of the recombinant proteins reveals that HPPR2 has both hydroxypyruvate reductase (HPR EC 1.1.1.81, main activity) and hydroxyphenylpyruvate reductase (HPPR, EC 1.1.1.237) activities, whereas HPPR3 has a strong preference for pHPP, and both enzymes are localized in the cytosol. In Arabidopsis thaliana, HPPR2 and HPPR3, together with tyrosine aminotransferase 1 (TAT1), constitute to a probably conserved biosynthetic pathway from tyrosine to 4-hydroxyphenyllactic acid (pHPL), from which some specialized metabolites, such as rosmarinic acid (RA), can be generated in specific groups of plants. Role of HPPR in the tyrosine conversion pathway, overview
-
physiological function
deletion of any of the core enzymes of the photorespiratory cycle, one of the major pathways of plant primary metabolism, results in severe air-sensitivity of the respective mutants with the exception of the peroxisomal enzyme hydroxypyruvate reductase, HPR1, due to the existence of a second hydroxypyruvate reductase, HPR2, in the cytosol, overview. The enzyme provides a cytosolic bypass to the photorespiratory core cycle in Arabidopsis thaliana
physiological function
-
in the dark, cytokinins mimic the regulatory effect of light upon algal cell division, metabolite content and stimulate carbon recycling for Calvin cycle reactions by enhancing of light-dependent NADH-HPR activity, regulation, overview
physiological function
deletion of isoform HPR3 results in slightly altered leaf concentrations of the photorespiratory intermediates HP, glycerate, and glycine, indicating a disrupted photorespiratory flux, but not in visible alteration of the phenotype.The combined deletion of of isoforms HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1hpr2 double mutant. Isoform HPR3 could provide a compensatory bypass for the reduction of hydroxypyruvate and glyoxylate within the chloroplast
physiological function
upregulation of glyoxylate reductase/hydroxypyruvate reductase is associated with intestinal epithelial cells apoptosis in trinitrobenzenesulfonic acid-induced colitis
physiological function
hydroxypyruvate reductase activity is important in the recycling of metabolites derived during photorespiration
physiological function
Arabidopsis mutants defective in either isoform HPPR2 or HPPR3 contain lower amounts of 4-hydroxyphenyllactic acid and are impaired in conversion of tyrosine to 4-hydroxyphenyllactic acid
physiological function
HPR3 is the third enzyme in Arabidopsis (Arabidopsis thaliana), which also reduces 4-hydroxypyruvate (HP) to glycerate and shows even more activity with glyoxylate, a more upstream intermediate of the photorespiratory cycle. In silico analysis and proteomic studies target HPR3 to the chloroplast, the enzyme might provide a compensatory bypass for the reduction of HP and glyoxylate within this compartment
physiological function
hydroxyphenylpyruvate reductase (HPPR), which catalyzes the reduction of 4-hydroxyphenylpyruvic acid (pHPP) to 4-hydroxyphenyllactic acid (pHPL), is the key enzyme in the biosynthesis of rosmarinic acid (RA) from tyrosine and, so far, HPPR activity is reported only from the RA-accumulating plants
physiological function
the enzyme activity shows that photorespiratory metabolism is not confined to chloroplasts, peroxisomes, and mitochondria but also extends to the cytosol. The extent to which cytosolic reactions contribute to the operation of the photorespiratory cycle in varying natural environments might be dynamically regulated by the availability of NADH in the context of peroxisomal redox homeostasis. But isozyme HPR1 plays the dominant role in photorespiration
physiological function
-
Arabidopsis mutants defective in either isoform HPPR2 or HPPR3 contain lower amounts of 4-hydroxyphenyllactic acid and are impaired in conversion of tyrosine to 4-hydroxyphenyllactic acid
-
physiological function
-
hydroxyphenylpyruvate reductase (HPPR), which catalyzes the reduction of 4-hydroxyphenylpyruvic acid (pHPP) to 4-hydroxyphenyllactic acid (pHPL), is the key enzyme in the biosynthesis of rosmarinic acid (RA) from tyrosine and, so far, HPPR activity is reported only from the RA-accumulating plants
-
physiological function
-
the enzyme activity shows that photorespiratory metabolism is not confined to chloroplasts, peroxisomes, and mitochondria but also extends to the cytosol. The extent to which cytosolic reactions contribute to the operation of the photorespiratory cycle in varying natural environments might be dynamically regulated by the availability of NADH in the context of peroxisomal redox homeostasis. But isozyme HPR1 plays the dominant role in photorespiration
-
physiological function
-
HPR3 is the third enzyme in Arabidopsis (Arabidopsis thaliana), which also reduces 4-hydroxypyruvate (HP) to glycerate and shows even more activity with glyoxylate, a more upstream intermediate of the photorespiratory cycle. In silico analysis and proteomic studies target HPR3 to the chloroplast, the enzyme might provide a compensatory bypass for the reduction of HP and glyoxylate within this compartment
-
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G160R
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G165D
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
M322R
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
R302C
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G160R
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G165D
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
M322R
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
R302C
-
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
additional information
construction of hpr1 knockout and hpr2 knockout. Deletion of HPR2 results in elevated levels of hydroxypyruvate and other metabolites in leaves, photosynthetic gas exchange is slightly altered, especially under long-day conditions. Deletion of HPR1 does not show a severe phenotype, overview. The combined deletion of HPR1 and HPR2 is detrimental to air-grown mutants and alters steady state metabolite profiles, phenotypes, overview. The most prominent naturally occuring mutation causes the decrease in Ala content coupled with enhanced levels of Arg, Asn, and Asp in the hpr1 mutant and the double knockout plant
additional information
construction of hpr1 knockout and hpr2 knockout. Deletion of HPR2 results in elevated levels of hydroxypyruvate and other metabolites in leaves, photosynthetic gas exchange is slightly altered, especially under long-day conditions. Deletion of HPR1 does not show a severe phenotype, overview. The combined deletion of HPR1 and HPR2 is detrimental to air-grown mutants and alters steady state metabolite profiles, phenotypes, overview. The most prominent naturally occuring mutation causes the decrease in Ala content coupled with enhanced levels of Arg, Asn, and Asp in the hpr1 mutant and the double knockout plant
additional information
-
construction of hpr1 knockout and hpr2 knockout. Deletion of HPR2 results in elevated levels of hydroxypyruvate and other metabolites in leaves, photosynthetic gas exchange is slightly altered, especially under long-day conditions. Deletion of HPR1 does not show a severe phenotype, overview. The combined deletion of HPR1 and HPR2 is detrimental to air-grown mutants and alters steady state metabolite profiles, phenotypes, overview. The most prominent naturally occuring mutation causes the decrease in Ala content coupled with enhanced levels of Arg, Asn, and Asp in the hpr1 mutant and the double knockout plant
additional information
HPR1 knockout plants show slight visually noticeable impairments in air. Under shorter daylengths of 8 h, somewhat slower growth of the hpr1 mutants than of the wild-type, in combination with an approximately 4-week delay in bolting. Combined deletion of both HPR1 and HPR2 (EC 1.1.1.81) results in distinct air-sensitivity and a dramatic reduction in photosynthetic performance
additional information
HPR1 knockout plants show slight visually noticeable impairments in air. Under shorter daylengths of 8 h, somewhat slower growth of the hpr1 mutants than of the wild-type, in combination with an approximately 4-week delay in bolting. Combined deletion of both HPR1 and HPR2 (EC 1.1.1.81) results in distinct air-sensitivity and a dramatic reduction in photosynthetic performance
additional information
-
HPR1 knockout plants show slight visually noticeable impairments in air. Under shorter daylengths of 8 h, somewhat slower growth of the hpr1 mutants than of the wild-type, in combination with an approximately 4-week delay in bolting. Combined deletion of both HPR1 and HPR2 (EC 1.1.1.81) results in distinct air-sensitivity and a dramatic reduction in photosynthetic performance
additional information
deletion of HPR2 by T-DNA insertion, HPR2 knockout plants do not show visually noticeable impairments in air, but combined deletion of HPR1 and HPR2 is detrimental to air-grown mutants. Crossing of hpr1-1 and hpr2-1 leads to functional inactivation of both genes. Knockout of both HPR1 and HPR2 alters steady-state metabolite profiles and photorespiratory 13C fluxes. The leaf glycerate content remains essentially unaltered in the hpr2 mutant and is increased in hpr1 and the double knockout plant. Knockout of either HPR1 or HPR2 alters photosynthetic gas exchange
additional information
-
deletion of HPR2 by T-DNA insertion, HPR2 knockout plants do not show visually noticeable impairments in air, but combined deletion of HPR1 and HPR2 is detrimental to air-grown mutants. Crossing of hpr1-1 and hpr2-1 leads to functional inactivation of both genes. Knockout of both HPR1 and HPR2 alters steady-state metabolite profiles and photorespiratory 13C fluxes. The leaf glycerate content remains essentially unaltered in the hpr2 mutant and is increased in hpr1 and the double knockout plant. Knockout of either HPR1 or HPR2 alters photosynthetic gas exchange
additional information
deletion of HPR3 by T-DNA insertion mutagenesis resulting in slightly altered leaf concentrations of the photorespiratory intermediates HP, glycerate, and glycine, indicating a disrupted photorespiratory flux, but not in visible alteration of the phenotype. The combined deletion of HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1xhpr2 double mutant. Generation of two independent T-DNA insertion lines for the gene At1g12550, i.e. hpr3-1 and hpr3-2
additional information
deletion of HPR3 by T-DNA insertion mutagenesis resulting in slightly altered leaf concentrations of the photorespiratory intermediates HP, glycerate, and glycine, indicating a disrupted photorespiratory flux, but not in visible alteration of the phenotype. The combined deletion of HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1xhpr2 double mutant. Generation of two independent T-DNA insertion lines for the gene At1g12550, i.e. hpr3-1 and hpr3-2
additional information
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR2 mutant phenotype, overview
additional information
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR2 mutant phenotype, overview
additional information
-
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR2 mutant phenotype, overview
additional information
generation of Arabidopsis thaliana HPR1 knockout mutants, which grow nearly normally in ambient air with moderate photoperiods and show only minor changes in photosynthetic and metabolic parameters under these conditions. The additional deletion of the cytosolic HPR2 distinctly elevates the oxygen sensitivity, but this hpr1xhpr2 double mutant can still survive long-term exposure to ambient air
additional information
generation of Arabidopsis thaliana HPR1 knockout mutants, which grow nearly normally in ambient air with moderate photoperiods and show only minor changes in photosynthetic and metabolic parameters under these conditions. The additional deletion of the cytosolic HPR2 distinctly elevates the oxygen sensitivity, but this hpr1xhpr2 double mutant can still survive long-term exposure to ambient air
additional information
-
expression analysis of HPPR2, HPPR3, and other pathway-related enzymes in mutant strains, HPPR2 mutant phenotype, overview
-
additional information
-
deletion of HPR2 by T-DNA insertion, HPR2 knockout plants do not show visually noticeable impairments in air, but combined deletion of HPR1 and HPR2 is detrimental to air-grown mutants. Crossing of hpr1-1 and hpr2-1 leads to functional inactivation of both genes. Knockout of both HPR1 and HPR2 alters steady-state metabolite profiles and photorespiratory 13C fluxes. The leaf glycerate content remains essentially unaltered in the hpr2 mutant and is increased in hpr1 and the double knockout plant. Knockout of either HPR1 or HPR2 alters photosynthetic gas exchange
-
additional information
-
generation of Arabidopsis thaliana HPR1 knockout mutants, which grow nearly normally in ambient air with moderate photoperiods and show only minor changes in photosynthetic and metabolic parameters under these conditions. The additional deletion of the cytosolic HPR2 distinctly elevates the oxygen sensitivity, but this hpr1xhpr2 double mutant can still survive long-term exposure to ambient air
-
additional information
-
deletion of HPR3 by T-DNA insertion mutagenesis resulting in slightly altered leaf concentrations of the photorespiratory intermediates HP, glycerate, and glycine, indicating a disrupted photorespiratory flux, but not in visible alteration of the phenotype. The combined deletion of HPR1, HPR2, and HPR3 causes increased growth retardation, decreased photochemical efficiency, and reduced oxygen-dependent gas exchange in comparison with the hpr1xhpr2 double mutant. Generation of two independent T-DNA insertion lines for the gene At1g12550, i.e. hpr3-1 and hpr3-2
-
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Kleczkowski, L.A.; Randall, D.D.; Edwards, G.E.
Oxalate as a potent and selective inhibitor of spinach (Spinacia oleracea) leaf NADPH-dependent hydroxypyruvate reductase
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-
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1295-1303
2017
Methylosinus trichosporium, Methylotuvimicrobium alcaliphilum, Methylococcus capsulatus (Q608T2), Methylococcus capsulatus Bath (Q608T2), Methylotuvimicrobium alcaliphilum 20Z
brenda
Kutner, J.; Shabalin, I.G.; Matelska, D.; Handing, K.B.; Gasiorowska, O.; Sroka, P.; Gorna, M.W.; Ginalski, K.; Wozniak, K.; Minor, W.
Structural, biochemical, and evolutionary characterizations of glyoxylate/hydroxypyruvate reductases show their division into two distinct subfamilies
Biochemistry
57
963-977
2018
Sinorhizobium meliloti (Q92LZ4), Sinorhizobium meliloti (Q92T34)
brenda
Xu, J.; Fang, X.; Li, C.; Zhao, Q.; Martin, C.; Chen, X.; Yang, L.
Characterization of Arabidopsis thaliana hydroxyphenylpyruvate reductases in the tyrosine conversion pathway
Front. Plant Sci.
9
1305
2018
Arabidopsis thaliana (A0A178WMD4), Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9CA90)
brenda
Timm, S.; Nunes-Nesi, A.; Paernik, T.; Morgenthal, K.; Wienkoop, S.; Keerberg, O.; Weckwerth, W.; Kleczkowski, L.A.; Fernie, A.R.; Bauwe, H.
A cytosolic pathway for the conversion of hydroxypyruvate to glycerate during photorespiration in Arabidopsis
Plant Cell
20
2848-2859
2008
Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9CA90)
brenda
Timm, S.; Florian, A.; Jahnke, K.; Nunes-Nesi, A.; Fernie, A.R.; Bauwe, H.
The hydroxypyruvate-reducing system in Arabidopsis multiple enzymes for the same end
Plant Physiol.
155
694-705
2011
Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana (Q9LE33), Arabidopsis thaliana Col-0 (Q9CA90), Arabidopsis thaliana Col-0 (Q9LE33)
brenda