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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+
reaction of EC 1.1.1.237
-
-
?
4-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
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-hydroxypyruvate + NADH + H+

D-glycerate + NAD+
-
-
-
-
r
4-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
r
4-hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
-
-
-
r
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+
-
60% 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+
-
24% 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+
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+
-
-
-
-
?
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+
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+
-
-
-
-
?
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+
-
-
-
?
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 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.
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+
-
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
-
1 mM, substrate NADPH, 64% 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
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
-
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
-
5 mM, 78% of initial activity
pyruvate
-
10 mM, 40% inhibition of NADH linked hydroxypyruvate reduction
pyruvate
-
5 mM, 67% 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.
2-oxoglutarate
-
5 mM, 231% of initial activity
acetyl-CoA
-
5 mM, 120% of initial activity
ADP
-
5 mM, 298% of initial activity
ATP
-
5 mM, 305% of initial activity
citrate
-
5 mM, 399% of initial activity
CsCl
-
80 mM, 3fold increase in hydroxypyruvate reductase activity
F-
-
100 mM, 67% activation of hydroxypyruvate reduction
fructose 1,6-diphosphate
-
5 mM, 244% of initial activity
glycerate
5 mM, 244% of initial activity
KCl
-
80 mM, 9fold increase in hydroxypyruvate reductase activity
NaCl
-
80 mM, 8fold increase in hydroxypyruvate reductase activity, reaction rate increases with an increase in NaCl concentration up to 200 mM, but diminishes if the salt concentration is greater
NAD+
-
1 mM, substrate NADH, 157% of initial activity
ribulose 5-phosphate
-
5 mM, 109% of initial activity
serine
-
5 mM, 180% of initial activity
additional information
-
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 by up to 62%, overview
-
Br-

-
100 mM, 10fold activation of hydroxypyruvate reduction
Cl-

-
100 mM, 9fold activation of hydroxypyruvate reduction
diphosphate

-
5 mM, 362% of initial activity
diphosphate
-
5 mM, 152% of initial activity
glucose 6-phosphate

-
5 mM, 163% of initial activity
glucose 6-phosphate
-
5 mM, 134% of initial activity
I-

-
100 mM, 9fold activation of hydroxypyruvate reduction
NADP+

1 mM, substrate NADH, 104% of initial activity
NADP+
1 mM, substrate NADPH, 200% of initial activity
NADP+
-
1 mM, substrate NADH, 114% of initial activity
NADP+
-
1 mM, substrate NADPH, 199% of initial activity
NO3-

-
100 mM, 8fold activation of hydroxypyruvate reduction
oxaloacetate

-
5 mM, 231% of initial activity
oxaloacetate
-
5 mM, 119% of initial activity
Ribulose 1,5-diphosphate

-
5 mM, 325% of initial activity
Ribulose 1,5-diphosphate
-
5 mM, 170% of initial activity
SO42-

-
100 mM, 3fold activation of hydroxypyruvate reduction
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, 25ưC
0.057 - 9.35
3-hydroxypyruvate
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, 25ưC
0.057
3-hydroxypyruvate

cosubstrate NADH, pH 7, 37ưC
0.14
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 30ưC
0.17
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 37ưC
0.5
3-hydroxypyruvate
cosubstrate NADPH, pH 7, 37ưC
0.6
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 37ưC
1.2
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 30ưC
6.14
3-hydroxypyruvate
K0.5 value, Hill coefficient 1.74, pH 7.5, 25ưC
9.35
3-hydroxypyruvate
pH 7.5, 25ưC
3
glyoxylate

-
cosubstrate NADH, pH 7, 37ưC
3.9
glyoxylate
cosubstrate NADH, pH 7, 37ưC
11
glyoxylate
-
cosubstrate NADPH, pH 7, 37ưC
12.3
glyoxylate
K0.5 value, Hill coefficient 1.83, pH 7.5, 25ưC
18
glyoxylate
-
cosubstrate NADPH, pH 7, 30ưC
22
glyoxylate
-
cosubstrate NADH, pH 7, 30ưC
80
glyoxylate
K0.5 value, Hill coefficient 1.48, pH 7.5, 25ưC
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 50ưC
0.07
Hydroxypyruvate
-
with NADH as cosubstrate, at pH 8.0 and 50ưC
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 50ưC
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 50ưC
0.165
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50ưC
0.175
Hydroxypyruvate
-
native enzyme
0.189
Hydroxypyruvate
-
purified recombinant enzyme
0.41
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50ưC
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, 30ưC
1.25
Hydroxypyruvate
-
cofactor NADPH
2.1
Hydroxypyruvate
-
with 0.15 mM NADH
3.57
Hydroxypyruvate
pH 7, 30ưC
6.1
Hydroxypyruvate
GLYR1, at pH 7.8 and 22ưC
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, 30ưC, pH 7
0.015
NADH
-
with glyoxylate as substrate, pH 7.5
0.015
NADH
cosubsubstrate glyoxylate, 37ưC, pH 7
0.028
NADH
-
cosubsubstrate 3-hydroxypyruvate, 30ưC, pH 7
0.03
NADH
cosubsubstrate 3-hydroxypyruvate, 37ưC, pH 7
0.055
NADH
-
native enzyme
0.064
NADH
-
purified recombinant enzyme
0.07
NADH
-
cosubsubstate glyoxylate, 37ưC, pH 7
0.08
NADH
-
cosubsubstate 3-hydroxypyruvate, 37ưC, pH 7
0.0105
NADPH

pH 7.5, 25ưC
0.021
NADPH
-
with glyoxylate as substrate, pH 7.5
0.025
NADPH
-
with hydroxypyruvate as substrate, pH 7.5
0.028
NADPH
-
cosubsubstate glyoxylate, 37ưC, pH 7
0.055
NADPH
-
cosubsubstate 3-hydroxypyruvate, 37ưC, pH 7
0.059
NADPH
pH 7.5, 25ưC
0.11
NADPH
-
cosubsubstrate 3-hydroxypyruvate, 30ưC, pH 7
0.16
NADPH
cosubsubstrate 3-hydroxypyruvate, 37ưC, pH 7
0.22
NADPH
-
cosubsubstrate glyoxylate, 30ưC, pH 7
1.5 - 2
phenylpyruvate

pH 7, 30ưC
3.7
phenylpyruvate
pH 7, 30ưC
5.59
phenylpyruvate
pH 7.5, 25ưC
6.58
phenylpyruvate
pH 7.5, 25ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30 - 687
3-hydroxypyruvate
0.05 - 25
Hydroxypyruvate
0.033 - 0.61
phenylpyruvate
30
3-hydroxypyruvate

-
cosubstrate NADH, pH 7, 37ưC
38
3-hydroxypyruvate
cosubstrate NADPH, pH 7, 37ưC
42
3-hydroxypyruvate
cosubstrate NADH, pH 7, 37ưC
48
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 37ưC
288
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 30ưC
687
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 30ưC
19
glyoxylate

-
cosubstrate NADH, pH 7, 37ưC
41
glyoxylate
cosubstrate NADH, pH 7, 37ưC
52
glyoxylate
-
cosubstrate NADPH, pH 7, 30ưC
88
glyoxylate
-
cosubstrate NADPH, pH 7, 37ưC
166
glyoxylate
-
cosubstrate NADH, pH 7, 30ưC
0.05
Hydroxypyruvate

pH 7, 30ưC
0.6
Hydroxypyruvate
-
with NADPH as cosubstrate, at pH 8.0 and 50ưC
0.93
Hydroxypyruvate
pH 7, 30ưC
1.2
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50ưC
4.5
Hydroxypyruvate
-
with NADH as cosubstrate, at pH 8.0 and 50ưC
6.5
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50ưC
10
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50ưC
25
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50ưC
4.1
NADH

-
with hydroxypyruvate as substrate, pH 7.5
11
NADH
-
with glyoxylate as substrate, pH 7.5
14
NADH
-
cosubsubstate 3-hydroxypyruvate, 37ưC, pH 7
19
NADH
-
cosubsubstate glyoxylate, 37ưC, pH 7
41
NADH
cosubsubstrate glyoxylate, 37ưC, pH 7
42
NADH
cosubsubstrate 3-hydroxypyruvate, 37ưC, pH 7
166
NADH
-
cosubsubstrate glyoxylate, 30ưC, pH 7
687
NADH
-
cosubsubstrate 3-hydroxypyruvate, 30ưC, 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, 37ưC, pH 7
48
NADPH
-
cosubsubstate 3-hydroxypyruvate, 37ưC, pH 7
52
NADPH
-
cosubsubstrate glyoxylate, 30ưC, pH 7
88
NADPH
-
cosubsubstate glyoxylate, 37ưC, pH 7
284
NADPH
-
cosubsubstrate 3-hydroxypyruvate, 30ưC, pH 7
0.033
phenylpyruvate

pH 7, 30ưC
0.61
phenylpyruvate
pH 7, 30ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.94
2-dehydro-D-gluconate
pH 7.5, 25ưC
1.2 - 4907
3-hydroxypyruvate
0.015 - 75
Hydroxypyruvate
0.009 - 0.4
phenylpyruvate
0.057
pyruvate
pH 7.5, 25ưC
1.2
3-hydroxypyruvate

pH 7.5, 25ưC
9.31
3-hydroxypyruvate
K0.5 value, Hill coefficient 1.74, pH 7.5, 25ưC
10.56
3-hydroxypyruvate
cosubstrate NADPH, pH 7, 37ưC
50
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 37ưC
240
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 30ưC
282
3-hydroxypyruvate
-
cosubstrate NADPH, pH 7, 37ưC
737
3-hydroxypyruvate
cosubstrate NADH, pH 7, 37ưC
4907
3-hydroxypyruvate
-
cosubstrate NADH, pH 7, 30ưC
0.81
glyoxylate

K0.5 value, Hill coefficient 1.48, pH 7.5, 25ưC
1.72
glyoxylate
Hill coefficient 1.83, pH 7.5, 25ưC
2.9
glyoxylate
-
cosubstrate NADPH, pH 7, 30ưC
6
glyoxylate
-
cosubstrate NADH, pH 7, 37ưC
6
glyoxylate
cosubstrate NADH, pH 7, 37ưC
7.5
glyoxylate
-
cosubstrate NADH, pH 7, 30ưC
8
glyoxylate
-
cosubstrate NADPH, pH 7, 37ưC
0.015
Hydroxypyruvate

pH 7, 30ưC
0.232
Hydroxypyruvate
GLYR1, at pH 7.8 and 22ưC
0.95
Hydroxypyruvate
pH 7, 30ưC
15
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50ưC
30
Hydroxypyruvate
-
with NADPH as cosubstrate, at pH 8.0 and 50ưC
40
Hydroxypyruvate
with NADPH as cosubstrate, at pH 8.0 and 50ưC
60
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50ưC
65
Hydroxypyruvate
-
with NADH as cosubstrate, at pH 8.0 and 50ưC
75
Hydroxypyruvate
with NADH as cosubstrate, at pH 8.0 and 50ưC
175
NADH

-
cosubsubstate 3-hydroxypyruvate, 37ưC, pH 7
271
NADH
-
cosubsubstate glyoxylate, 37ưC, pH 7
1400
NADH
cosubsubstrate 3-hydroxypyruvate, 37ưC, pH 7
2733
NADH
cosubsubstrate glyoxylate, 37ưC, pH 7
12769
NADH
-
cosubsubstrate glyoxylate, 30ưC, pH 7
24535
NADH
-
cosubsubstrate 3-hydroxypyruvate, 30ưC, pH 7
143
NADPH

cosubsubstrate 3-hydroxypyruvate, 37ưC, pH 7
236
NADPH
-
cosubsubstrate glyoxylate, 30ưC, pH 7
371
NADPH
pH 7.5, 25ưC
773
NADPH
pH 7.5, 25ưC
873
NADPH
-
cosubsubstate 3-hydroxypyruvate, 37ưC, pH 7
2582
NADPH
-
cosubsubstrate 3-hydroxypyruvate, 30ưC, pH 7
3142
NADPH
-
cosubsubstate glyoxylate, 37ưC, pH 7
0.009
phenylpyruvate

pH 7, 30ưC
0.27
phenylpyruvate
pH 7.5, 25ưC
0.37
phenylpyruvate
pH 7.5, 25ưC
0.4
phenylpyruvate
pH 7, 30ưC
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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
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
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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
Biochem. J.
276
125-127
1991
Spinacia oleracea
brenda
Chistoserdova, L.V.; Lidstrom, M.E.
Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1
J. Bacteriol.
173
7228-7232
1991
Methylorubrum extorquens AM1
brenda
Hagishita, T.; Yoshida, T.; Izumi, Y.; Mitsunaga, T.
Immunological characterization of serine-glyoxylate aminotransferase and hydroxypyruvate reductase from a methylotrophic bacterium, Hyphomicrobium methylovorum GM2
FEMS Microbiol. Lett.
142
49-52
1996
Cucumis sativus, Hyphomicrobium methylovorum GM2, Methylorubrum extorquens AM1, Methylobacterium organophilum, Spinacia oleracea
brenda
Yoshida, T.; Yamaguchi, K.; Hagishata, T.; Miyata, T.; Tanabe, T.; Toh, H.; Oshiro, T.; Shimao, M.; Itumi, Y.
Cloning and expression of the gene for hydroxypyruvate reductase (D-glycerate dehydrogenase) from an obligate methylotroph Hyphomicrobium methyovorum GM2
Eur. J. Biochem.
223
727-732
1994
Hyphomicrobium methylovorum GM2
brenda
Oliver, M.J.; Ferguson, D.L.; Burke, J.J.; Velten, J.
Inhibition of tobacco NADH-hydroxypyruvate reductase by expression of a heterologous antisense RNA derived from a cucumber cDNA: implications for the mechanism of action of antisense RNAs
Mol. Gen. Genet.
239
425-434
1993
Nicotiana tabacum cv. SR1
brenda
Kleczkowski, L.A.; Edwards, G.E.; Blackwell, R.D.; Lea, P.J.; Givan, C.V.
Enzymology of the reduction of hydroxypyruvate and glyoxylate in a mutant of barley lacking peroxisomal hydroxypyruvate reductase
Plant Physiol.
94
819-825
1990
Hordeum vulgare
brenda
Krema, C.; Lidstrom, M.E.
Hydroxypyruvate reductase from Methylobacterium extorquens AM1
Methods Enzymol.
188
373-378
1990
Methylorubrum extorquens AM1
-
brenda
Kleczkowski, L.A.; Edwards, G.E.
Identification of hydroxypyruvate and glyoxylate reductase in maize leaves
Plant Physiol.
91
278-288
1989
Zea mays
brenda
Murray, A.J.S.; Blackwell, R.D.; Lea, P.J.
Metabolism of hydroxypyruvate in a mutant of barley lacking NADH-dependent hydroxypyruvate reductase, an important photorespiratory enzyme activity
Plant Physiol.
91
395-400
1989
Hordeum vulgare
brenda
Sautter, C.; Sautter, E.; Hock, B.
Import of peroxisomal hydroxypyruvate reductase into glyoxysomes
Planta
176
149-158
1988
Citrullus lanatus subsp. vulgaris, Cucurbita pepo, Spinacia oleracea
brenda
Kleczkowski, L.A.; Givan, C.V.; Hodgson, J.M.; Randall, D.D.
Subcellular location of NADPH-dependent hydroxypyruvate reductase activity in leaf protoplasts of Pisum sativum L. and its role in photorespiratory metabolism
Plant Physiol.
88
1182-1185
1988
Pisum sativum, Spinacia oleracea
brenda
Kleczkowski, L.A.; Randall, D.D.
Purification and characterization of a novel NADPH(NADH)-dependent hydroxypyruvate reductase from spinach leaves. Comparison of immunological properties of leaf hydroxypyruvate reductases
Biochem. J.
250
145-152
1988
Spinacia oleracea
brenda
Bamforth, C.W.; Quayle, J.R.
Hydroxypyruvate reductase activity in Paracoccus denitrificans
J. Gen. Microbiol.
101
259-267
1977
Paracoccus denitrificans
-
brenda
Feld, R.D.; Sallach, H.J.
Comparison of D-glycerate dehydrogenases from beef liver, beef spinal cord and hog spinal cord
Arch. Biochem. Biophys.
166
417-425
1975
Bos taurus, Sus scrofa
brenda
Feld, R.D.; Sallach, H.J.
D-Glycerate dehydrogenase from hog spinal cord
Methods Enzymol.
41B
289-293
1975
Sus scrofa
brenda
Sugimoto, E.; Kitagawa, Y.; Hirose, M.; Chiba, H.
Mechanisms of inhibition and activation of beef liver D-glycerate dehydrogenase by inorganic anions
J. Biochem.
72
1317-1325
1972
Bos taurus
brenda
Sugimoto, E.; Kitagawa, Y.; Nakanishi, K.; Chiba, H.
Purification and properties of beef liver D-glycerate dehydrogenase
J. Biochem.
72
1307-1315
1972
Bos taurus
brenda
Uhr, M.L.; Sneddon, M.K.
Glycine and serine inhibition of D-glycerate dehydrogenase and 3-phosphoglycerate dehydrogenase of rat brain
FEBS Lett.
17
137-140
1971
Rattus norvegicus
brenda
Kohn, L.D.; Jakoby, W.B.
Tartaric acid metabolism. VII. Crystalline hydroxypyruvate reductase (D-glycerate dehydrogenase)
J. Biol. Chem.
243
2494-2499
1968
Delftia acidovorans
brenda
Kohn, L.D.; Jakoby, W.B.
Hydroxypyruvate reductase (D-glycerate dehydrogenase; crystalline) Pseudomonas
Methods Enzymol.
9
229-232
1966
Delftia acidovorans
-
brenda
Coderch, R.; Lluis, C.; Bozal, J.
Effect of salts on D-glycerate dehydrogenase kinetic behavior
Biochim. Biophys. Acta
566
21-31
1979
Bos taurus
brenda
Booth, M.P.; Conners, R.; Rumsby, G.; Brady, R.L.
Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase
J. Mol. Biol.
360
178-189
2006
Homo sapiens, Mus musculus
brenda
Yoshikawa, S.; Arai, R.; Kinoshita, Y.; Uchikubo-Kamo, T.; Wakamatsu, T.; Akasaka, R.; Masui, R.; Terada, T.; Kuramitsu, S.; Shirouzu, M.; Yokoyama, S.
Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate
Acta Crystallogr. Sect. D
63
357-365
2007
Pyrococcus horikoshii OT3
brenda
Shen, P.H.; Wu, B.
Over-expression of a hydroxypyruvate reductase in Methylobacterium sp. MB200 enhances glyoxylate accumulation
J. Ind. Microbiol. Biotechnol.
34
657-663
2007
Methylobacterium sp., Methylobacterium sp. MB200
brenda
Piotrowska, A.; Czerpak, R.
Cellular response of light/dark-grown green alga Chlorella vulgaris Beijerinck (Chlorophyceae) to exogenous adenine- and phenylurea-type cytokinins
Acta Physiol. Plant.
31
573-585
2009
Chlorella vulgaris
-
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 (Q9C9W5), Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana
brenda
Wang, Y.; Beaith, M.; Chalifoux, M.; Ying, J.; Uchacz, T.; Sarvas, C.; Griffiths, R.; Kuzma, M.; Wan, J.; Huang, Y.
Shoot-specific down-regulation of protein farnesyltransferase (alpha-subunit) for yield protection against drought in canola
Mol. Plant
2
191-200
2009
Brassica napus
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 (Q9LE33)
brenda
Hoover, G.J.; Jorgensen, R.; Rochon, A.; Bajwa, V.S.; Merrill, A.R.; Shelp, B.J.
Identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants
Biochim. Biophys. Acta
1834
2663-2671
2013
Arabidopsis thaliana (A0A178WMD4), Arabidopsis thaliana (A0A1I9LPQ6), Arabidopsis thaliana (Q9C9W5), Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana (Q9LE33)
brenda
Zong, C.; Nie, X.; Zhang, D.; Ji, Q.; Qin, Y.; Wang, L.; Jiang, D.; Gong, C.; Liu, Y.; Zhou, G.
Up regulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is associated with intestinal epithelial cells apoptosis in TNBS-induced experimental colitis
Pathol. Res. Pract.
212
365-371
2016
Homo sapiens (Q9UBQ7)
brenda
Lassalle, L.; Engilberge, S.; Madern, D.; Vauclare, P.; Franzetti, B.; Girard, E.
New insights into the mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductases
Sci. Rep.
6
20629
2016
Pyrococcus horikoshii, Pyrococcus yayanosii (F8AEA4), Pyrococcus furiosus (Q8U3Y2), Pyrococcus yayanosii CH1 (F8AEA4)
brenda
But, S.Y.; Egorova, S.V.; Khmelenina, V.N.; Trotsenko, Y.A.
Biochemical properties and phylogeny of hydroxypyruvate reductases from methanotrophic bacteria with different C1-assimilation pathways
Biochemistry (Moscow)
82
1295-1303
2017
Methylosinus trichosporium, Methylomicrobium alcaliphilum, Methylococcus capsulatus (Q608T2), Methylococcus capsulatus Bath (Q608T2), Methylomicrobium 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
brenda