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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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,3-butandione + NAD(P)H
butan-2-ol-3-one + NAD(P)+
-
33 mM, 12% of activity with hydroxypyruvate
-
?
acetoin + NAD(P)H + H+
2,3-butanediol + NAD(P)+
-
33 mM, 14% of activity with hydroxypyruvate
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
D-glycerate + NADP+
hydroxypyruvate + NADPH + H+
-
-
-
r
glyoxylate + NAD(P)H
glycolate + NAD(P)+
glyoxylate + NAD(P)H + H+
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NADH
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
-
?
additional information
?
-
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)+
-
-
-
?
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+
-
-
-
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+
-
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+
Nicotiana tabacum cv. SR1
-
-
-
?
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+
-
-
-
?, 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+
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
?
-
-
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
?
-
-
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+
Nicotiana tabacum cv. SR1
-
-
-
?
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-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
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
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
NAD+
-
4 mM, 10% inhibition of NADH linked hydroxypyruvate reduction, 60% of NADPH linked reduction
NADP+
-
4 mM, 15% inhibition of NADH linked hydroxypyruvate reduction, 40% of NADPH linked reduction, 8% of NAD+ linked glycerate oxidation
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
-
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
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
oxalate

; strong inhibition of HPR2
oxalate
-
2 mM, 90% inhibition
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
-
10 mM, 40% inhibition of NADH linked hydroxypyruvate reduction
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
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purified detagged recombinant enzyme in ternary complex with product D-glycerate and cofactor NADPH, sitting drop vapour diffusion method, 5.5 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 1 mM 2-mercaptoethanol, 0.2 mM NADPH, and 0.5 mm di-sodium oxalate, mixed with mother liquor, containing 15% w/v PEG 8000, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate, pH 6.5, to 0.002 ml drops, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl
sitting drop vapor diffusion method in the presence of NAD, crystal structure analysis reveals tightly bound NADP(H) at the enzyme originating from Escherichia coli expression, which is not replaceable by NAD
-
in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl
purified detagged recombinant enzyme in ternary complex with product D-glycerate and cofactor NADPH, sitting drop vapour diffusion method, 5.5 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 1 mM 2-mercaptoethanol, 0.2 mM NADPH, and 0.5 mm di-sodium oxalate, mixed with mother liquor, containing 15% w/v PEG 8000, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate, pH 6.5, to 0.002 ml drops, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution

-
purified detagged recombinant enzyme in ternary complex with product D-glycerate and cofactor NADPH, sitting drop vapour diffusion method, 5.5 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 1 mM 2-mercaptoethanol, 0.2 mM NADPH, and 0.5 mm di-sodium oxalate, mixed with mother liquor, containing 15% w/v PEG 8000, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate, pH 6.5, to 0.002 ml drops, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl

in complex with D-glycerate and NADPH, hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 5.2, 15% (w/v) polyethylene glycol 400 and 100 mM NaCl
-
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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; 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
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; 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
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; 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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-
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-
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-
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-
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