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2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
13.9% of glyoxylate activity
-
?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
acetaldehyde + NADPH + H+
ethanol + NADP+
-
10.4% of glyoxylate activity
-
?
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
-
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
glycolate + NADP+
glyoxylate + NADPH + H+
glycolate + NADP+
glyoxylate + NAPDH + H+
glyoxal + NADPH
glycol + NADP+
-
isoenzyme 1, 16% activity of glyxoxylate
-
?
glyoxylate + NAD(P)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+
glycerate + NAD(P)+
hydroxypyruvate + NADH
D-glycerate + NAD+
-
affinity for NADPH is lower than affinity for NADH
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
hydroxypyruvate + NADPH
D-glycerate + NADP+
-
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
oxalate + NADPH + H+
?
-
-
-
-
?
oxaloacetate + NADPH
malate + NADP+
phenylpyruvate + NAD(P)H
phenyllactate + NAD(P)+
-
isoenzyme 2, 6% activity of glyoxylate
-
?
pyruvate + NADPH + H+
?
-
low efficiency
-
-
?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
NADH much less effective than NADPH
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
additional information
?
-
2-oxoisocaproate + NADPH + H+

2-hydroxy-4-methylpentanoate + NADP+
-
low activity
-
-
?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
-
low activity
-
-
?
glycolate + NAD+

glyoxylate + NADH + H+
-
the reaction occurs only at pH 9.0
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
-
the reaction occurs only at pH 9.0
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
-
-
-
r
glycolate + NAD+
glyoxylate + NADH + H+
-
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
-
-
-
?
glycolate + NADP+

glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+

glyoxylate + NAPDH + H+
-
the reaction occurs only at pH 9.0
-
-
?
glycolate + NADP+
glyoxylate + NAPDH + H+
-
the reaction occurs only at pH 9.0
-
-
?
glyoxylate + NAD(P)H

glycolate + NAD(P)+
-
enzyme prefers NADPH
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
specific for NADPH
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
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)+
-
the enzyme plays a protective role in detoxification of glyoxylate
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
isoenzyme 2, 16% activity with NADH
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
Populus gelrica
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?, ir
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
7% of activity with glyoxylate
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NADH

glycolate + NAD+
NADH much less effective than NADPH
-
-
ir
glyoxylate + NADH
glycolate + NAD+
-
affinity for NADPH is lower than affinity for NADH
-
-
?
glyoxylate + NADH + H+

glycolate + NAD+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
NADH much less effective than NADPH
-
-
ir
glyoxylate + NADH + H+
glycolate + NAD+
-
-
-
-
r
glyoxylate + NADH + H+
glycolate + NAD+
-
NADPH-dependent activity is much higher than the NADH-dependent activity
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
-
-
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
-
-
-
-
r
glyoxylate + NADH + H+
glycolate + NAD+
-
-
-
-
r
glyoxylate + NADH + H+
glycolate + NAD+
-
-
-
-
r
glyoxylate + NADH + H+
glycolate + NAD+
-
-
-
-
ir
glyoxylate + NADH + H+
glycolate + NAD+
-
-
-
-
r
glyoxylate + NADPH

glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH
glycolate + NADP+
-
key enzyme in glyoxylate pathway
-
-
?
glyoxylate + NADPH
glycolate + NADP+
-
key enzyme in glyoxylate pathway. The regulation of the GHPR expression by peroxisome proliferator-activated receptor alpha may contribute to energy homeostasis by modulating the carbon supply for gluconeogenesis
-
-
?
glyoxylate + NADPH + H+

glycolate + NADP+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
preferred substrate
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
glyoxylate highly preferred over succinic semialdehyde as substrate
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
glyoxylate reductase 2 has a 350fold higher preference for glyoxylate than for succinic semialdehyde
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
the affinity for glyoxylate is 10fold lower for isoform GLYR2 than that for isoform GLYR1
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
NADPH-dependent activity is much higher than the NADH-dependent activity
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
-
highest activity
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
-
enzyme GhrA shows highest catalytic efficiency for glyoxylate
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
ir
hydroxypyruvate + NAD(P)H

D-glycerate + NAD(P)+ + H+
-
-
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
preferred substrate
-
-
?
hydroxypyruvate + NAD(P)H + H+

glycerate + NAD(P)+
-
25 mM hydroxypyruvate, 68% of the activity with glyoxylate, 2.5 mM hydroxypyruvate, isoenzyme 2, 332% of the activity of glyoxylate
-
?
hydroxypyruvate + NAD(P)H + H+
glycerate + NAD(P)+
-
-
-
?
hydroxypyruvate + NAD(P)H + H+
glycerate + NAD(P)+
-
isoenzyme 1, hydroxypyruvate shows 15% of the activity of glyoxylate
-
?
hydroxypyruvate + NADH + H+

D-glycerate + NAD+
-
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
with hydroxypyruvate as a substrate at a saturating concentration (66.7 mM), the enzyme GhrA exhibits 2-3% activity with 0.4 mM NADH as compared to 0.4 mM NADPH
-
-
?
hydroxypyruvate + NADPH + H+

D-glycerate + NADP+
-
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
15% activity compared to glyoxylate
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
15% activity compared to glyoxylate
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
?
oxaloacetate + NADPH

malate + NADP+
-
28.6% of glyoxylate activity
-
?
oxaloacetate + NADPH
malate + NADP+
-
isoenzyme 1, 12% activity of glyoxylate
-
?
succinic semialdehyde + NADPH + H+

4-hydroxybutyrate + NADP+
-
-
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
at least under oxygen deficient and high light conditions
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
detoxification of succinic semialdehyde during stress
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
reverse reaction less efficient than forward reaction
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
glyoxylate reductase 2 has a 350fold higher preference for glyoxylate than for succinic semialdehyde
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
the affinity for succinic semialdehyde is 10fold lower for isoform GLYR2 than that for isoform GLYR1
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
additional information

?
-
-
the enzyme exhibits no activity against succinic semialdehyde, hydroxypyruvate, formate, acetate, oxalate, 3-hydroxypropionate, DL-glycerate, pyruvate, and phenylpyruvate, formaldehyde, acetaldehyde, glutaraldehyde, glyoxal, methylglyoxal, and phenylglyoxal. The enzyme does not catalyze NAD(P)+-dependent glycolate oxidation at pH 4.0 and 7.0. DL-lactate, L-malate, (S)-hydroxyisobutyrate, and (R)-hydroxyisobutyrate, D-serine, L-serine, D-threonine, and L-threonine are inert as substrates of the enzyme when examined at pH of 4.0, 6.0, and 9.0
-
-
-
additional information
?
-
-
the enzyme exhibits no activity against succinic semialdehyde, hydroxypyruvate, formate, acetate, oxalate, 3-hydroxypropionate, DL-glycerate, pyruvate, and phenylpyruvate, formaldehyde, acetaldehyde, glutaraldehyde, glyoxal, methylglyoxal, and phenylglyoxal. The enzyme does not catalyze NAD(P)+-dependent glycolate oxidation at pH 4.0 and 7.0. DL-lactate, L-malate, (S)-hydroxyisobutyrate, and (R)-hydroxyisobutyrate, D-serine, L-serine, D-threonine, and L-threonine are inert as substrates of the enzyme when examined at pH of 4.0, 6.0, and 9.0
-
-
-
additional information
?
-
-
involved in stress response, enhanced transcript levels of GR1 at salinity, drought, submergence, and heat and GR2 at cold and heat
-
-
?
additional information
?
-
glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
-
-
?
additional information
?
-
glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
-
-
?
additional information
?
-
-
glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
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 highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate
-
-
?
additional information
?
-
-
the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate
-
-
?
additional information
?
-
the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate
-
-
?
additional information
?
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
?
additional information
?
-
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
?
additional information
?
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
?
additional information
?
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
?
additional information
?
-
-
no activity with glycolate, pyruvate, L-alanine, and glycine
-
-
-
additional information
?
-
-
no activity with 2-oxo-D-gluconate
-
-
-
additional information
?
-
-
substrate specificity, several 2-oxo compounds including phenylpyruvate, pyruvate, methylglyoxal, and oxaloacetate act as inert electron acceptors, as do glycolate and malate, overview
-
-
?
additional information
?
-
-
phenylpyruvate, pyruvate, methylglyoxal, malate, and oxaloacetate not suitable as substrate
-
-
?
additional information
?
-
-
substrate specificity, several 2-oxo compounds including phenylpyruvate, pyruvate, methylglyoxal, and oxaloacetate act as inert electron acceptors, as do glycolate and malate, 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+
-
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
glyoxylate + NAD(P)H
glycolate + NAD(P)+
glyoxylate + NADH + H+
glycolate + NAD+
glyoxylate + NADPH
glycolate + NADP+
glyoxylate + NADPH + H+
glycolate + NADP+
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
-
-
-
?
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
-
with hydroxypyruvate as a substrate at a saturating concentration (66.7 mM), the enzyme GhrA exhibits 2-3% activity with 0.4 mM NADH as compared to 0.4 mM NADPH
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
-
-
-
?
oxalate + NADPH + H+
?
-
-
-
-
?
pyruvate + NADPH + H+
?
-
low efficiency
-
-
?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
additional information
?
-
glycolate + NADP+

glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glyoxylate + NAD(P)H

glycolate + NAD(P)+
-
enzyme prefers NADPH
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
specific for NADPH
-
?
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)+
-
the enzyme plays a protective role in detoxification of glyoxylate
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
Populus gelrica
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
-
-
?
glyoxylate + NADH + H+

glycolate + NAD+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADPH

glycolate + NADP+
-
key enzyme in glyoxylate pathway
-
-
?
glyoxylate + NADPH
glycolate + NADP+
-
key enzyme in glyoxylate pathway. The regulation of the GHPR expression by peroxisome proliferator-activated receptor alpha may contribute to energy homeostasis by modulating the carbon supply for gluconeogenesis
-
-
?
glyoxylate + NADPH + H+

glycolate + NADP+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
-
enzyme GhrA shows highest catalytic efficiency for glyoxylate
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
-
-
-
-
ir
succinic semialdehyde + NADPH + H+

4-hydroxybutyrate + NADP+
-
at least under oxygen deficient and high light conditions
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
detoxification of succinic semialdehyde during stress
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
-
ir
additional information

?
-
-
involved in stress response, enhanced transcript levels of GR1 at salinity, drought, submergence, and heat and GR2 at cold and heat
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
the recombinant AtGLYR1 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR1 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR1 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
additional information
?
-
-
the recombinant AtGLYR2 prefers NADPH over NADH and converts glyoxylate to glycolate, AtGLYR2 has negligible hydroxypyruvate-dependent activity. Isozyme AtGLYR2 also converts succinic semialdehyde to gamma-hydroxybutyrate, albeit with much lower catalytic efficiency than for glyoxylate
-
-
?
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
?
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
?
additional information
?
-
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
?
additional information
?
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
?
additional information
?
-
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
?
additional information
?
-
-
no activity with 2-oxo-D-gluconate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NAD(P)H

-
-
NAD(P)H
-
specific for NADPH
NAD(P)H
-
specific for NADPH
NAD(P)H
Populus gelrica
-
specific for NADPH
NAD(P)H
-
highly specific for NADPH
NAD(P)H
-
NADPH is preferred
NAD(P)H
-
NADPH is preferred
NAD+

-
NADH

-
-
NADH
-
less active than NADPH
NADH
-
higher affinity for NADPH
NADH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADH
much less effective than NADPH
NADH
-
yields higher Km but similar turnover than NADPH
NADP+

-
-
NADP+
the wild-type enzyme is specific for NADPH/NADP+
NADPH

-
-
NADPH
-
preferred cofactor
NADPH
-
specific for NADPH
NADPH
-
specific for NADPH
NADPH
Populus gelrica
-
specific for NADPH
NADPH
-
highly specific for NADPH
NADPH
-
NADPH is preferred
NADPH
-
NADPH is preferred
NADPH
-
binding structure
NADPH
-
lower affinity for NADH
NADPH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADPH
-
is the preferred cofactor
NADPH
-
preferred cofactor, NADH gives only 4% of the activity with NADPH
NADPH
-
preferred cofactor, yields lower Km but similar turnover than NADH
NADPH
glyoxylate reductase 2 uses either NADPH or NADH as a cofactor, however, much greater activity is found with NADPH
NADPH
the wild-type enzyme is specific for NADPH/NADP+
NADPH
-
the enzyme prefers NADPH to NADH as cofactor
NADPH
-
the highest catalytic efficiency is observed for NADPH
NADPH
the highest catalytic efficiency is observed for NADPH
NADPH
the highest catalytic efficiency is observed for NADPH
additional information

-
comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview
-
additional information
comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview
-
additional information
comparison of cofactor specificities of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR) using glyoxylate or hydroxypyruvate as substrates and NADH or NADPH as cofactors, crystal structures analysis, overview
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
-
recombinant AtGLYR1 prefers NADPH over NADH
-
additional information
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
-
recombinant AtGLYR2 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
recombinant HPR3 prefers NADPH over NADH
-
additional information
-
recombinant HPR3 prefers NADPH over NADH
-
additional information
the enzyme utilize either NADPH or NADH as the coenzyme with glyoxylate, but prefers NADPH rather than NADH as an electron donor. The coenzyme specificity is provided by a cationic cluster consisting of N184, R185, and N186. Cofactor binding structure, overview
-
additional information
-
the enzyme utilize either NADPH or NADH as the coenzyme with glyoxylate, but prefers NADPH rather than NADH as an electron donor. The coenzyme specificity is provided by a cationic cluster consisting of N184, R185, and N186. Cofactor binding structure, overview
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
-
the recombinant AtHPR2 prefers NADPH over NADH
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-hydroxybutyrate
mixed type inhibition with NADPH; mixed type inhibition with succinic semialdehyde
adenine
-
0.01 mM, 70% inhibition after preincubation for 5 min
alpha-ketoglutarate
-
5 mM, 57% inhibition
Carbonate
-
20 mM, 7-16% inhibition
chloride
-
20 mM, 7-16% inhibition
cyanide
-
2 mM, 46% inhibition, 20 mM, 92% inhibition
cysteine
-
isoenzyme 1, 1 mM, 29% inhibition
D-glycerate
-
the enzyme shows product inhibition
diethyldicarbonate
-
1 mM, 33% inhibition, incubation for 1 min
ethanol
-
enzyme activity is decreased to 20% by incubation with 60% (v/v) ethanol
Fe3+
-
15% inhibition at 1 mM
glutathione
-
isoenzyme 1, 1 mM, 12% inhibition
glycidate
-
10 mM, 35% inhibition after 15 min
Hg2+
-
30% inhibition at 1 mM
iodoacetate
-
isoenzyme 2, 1 mM, 97% inhibition, isoenzyme 1, 1 mM, 18% inhibition
NaCl
-
complete inhibition at 0.5 M
nitrite
-
20 mM, 7-16% inhibition
oxalate
-
when using NADPH as cofactor, the Ki value of oxalate for isoform GR1 is 21.2 mM and that for isoform GR2 is 290.8 mM. When using NADH as cofactor, the Ki values of oxalate are much lower, 3.6mM for isoform GR1, and 8.2mM for isoform GR2
PMSF
-
1 mM, 30% inhibition, incubation for 1 min
pyruvate
-
5 mM, 33% inhibition
Sodium fluoride
-
isoenzyme 1, 10 mM, 32% inhibition
sodium iodide
-
isoenzyme 1, 50 mM, 37% inhibition of glyoxylate reduction
Sodium phosphate
-
50% inhibition at 900 mM
2-mercaptoethanol

-
isoenzyme 1, 1 mM, 19% inhibition
2-mercaptoethanol
-
5 mM, 37% inhibition, incubation for 1 min
ATP

-
10 mM, 20% inhibition
ATP
-
5 mM, 28% inhibition
dithiothreitol

-
isoenzyme 1, 1 mM, 41% inhibition, 10 mM, 87% inhibition
dithiothreitol
-
5 mM, 51% inhibition, incubation for 1 min
glycolate

mixed type inhibition with glyoxylate; uncompetitive with NADPH
glycolate
-
5 mM, 42% inhibition
iodoacetamide

-
isoenzyme 2, 1 mM, 87% inhibition, isoenzyme 1, 1 mM, 17% inhibition
iodoacetamide
-
1 mM, 28% inhibition, incubation for 1 min
N-ethylmaleimide

-
10.0 mM, 75% inhibition after preincubation for 5 min
N-ethylmaleimide
-
1 mM, 58% inhibition
NADP+

competitive with NADPH; competitive with NADPH when glyoxylate is the fixed substrate; uncompetitive with glyoxylate; uncompetitive with succinic semialdehyde
NADP+
-
NADP+ is a competitive inhibitor with respect to NADPH
NADP+
-
competitive product inhibition
nitrate

-
25 mM, competitive vs. glyoxylate
nitrate
-
isoenzyme 1, 50 mM, 50% inhibition
nitrate
-
20 mM, 7-16% inhibition
p-chloromercuribenzoate

-
0.1 mM, 55% inhibition after preincubation for 5 min
p-chloromercuribenzoate
-
1 mM, 70% inhibition
p-chloromercuribenzoate
-
isoenzyme 2, 1 mM, complete inhibition, 0.1 mM, 88% inhibition, 29% inhibition in the presence of 1 mM dithiothreitol, 21% inhibition in the presence of 1 mM L-cysteine, isoenzyme 1, 1 mM, 59% inhibition
additional information

-
no inhibition by 4-hydroxybutyrate
-
additional information
-
no activity at more than 500 mM NaCl, 50% activity in the presence of 900 mM sodium phosphate
-
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.
0.058 - 1.4
Hydroxypyruvate
9.7
pyruvate
-
at pH 7.5 and 25ưC
0.87 - 8.96
Succinic semialdehyde
additional information
additional information
-
309
glycolate

-
with NAD+ as cosubstrate, at pH 9.0 and 45ưC
334
glycolate
-
with NADP+ as cosubstrate, at pH 9.0 and 45ưC
0.0045
glyoxylate

recombinant protein from Escherichia coli
0.0045
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a double beam spectrophotometer
0.0141
glyoxylate
isoform GLYR1, at pH 7.5 and 25ưC
0.016
glyoxylate
pH 7.8, temperature not specified in the publication, recombinant truncated enzyme
0.018
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
0.0191
glyoxylate
-
isoform GLYR2, at pH 7.1 and 25ưC
0.0193
glyoxylate
isoform GLYR2, at pH 7.8 and 25ưC
0.0232
glyoxylate
isoform GLYR1, at pH 7.8 and 25ưC
0.0239
glyoxylate
isoform GLYR2, at pH 7.3 and 25ưC
0.0304
glyoxylate
-
isoform GR1, with NADPH as cosubstrate, at pH 7.4 and 30ưC
0.033
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E
0.034
glyoxylate
with as NADPH as cofactor, pH 7.6, 30ưC
0.034
glyoxylate
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30ưC
0.0532
glyoxylate
-
isoform GLYR1, at pH 6.5 and 25ưC
0.059
glyoxylate
-
cofactor NADPH
0.061
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
0.0721
glyoxylate
-
isoform GR2, with NADPH as cosubstrate, at pH 7.4 and 30ưC
0.085
glyoxylate
-
cofactor NADPH
0.088
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
0.11
glyoxylate
Populus gelrica
-
-
0.1446
glyoxylate
-
isoform GR2, with NADH as cosubstrate, at pH 7.4 and 30ưC
0.181
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
0.24
glyoxylate
-
37ưC, cofactor: NADPH
0.24
glyoxylate
-
pH 7.5, 37ưC, recombinant enzyme, with NADPH
0.2677
glyoxylate
-
isoform GR1, with NADH as cosubstrate, at pH 7.4 and 30ưC
0.38
glyoxylate
-
with NADPH as cosubstrate, at pH 4.0 and 45ưC
0.5
glyoxylate
-
pH 6.7, 45ưC, cofactor NADPH, purified recombinant enzyme
0.5
glyoxylate
-
with as NADPH as cofactor, pH 6.7, 45ưC
0.58
glyoxylate
-
with NADH as cosubstrate, at pH 4.0 and 45ưC
1
glyoxylate
-
37ưC, cofactor: NADH
1
glyoxylate
-
pH 7.5, 37ưC, recombinant enzyme, with NADH
1.1
glyoxylate
-
cofactor NADH
1.2
glyoxylate
-
pH 6.7, 45ưC, cofactor NADH, purified recombinant enzyme
1.2
glyoxylate
-
with as NADH as cofactor, pH 6.7, 45ưC
3
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
4.1
glyoxylate
pH 7.5, 50ưC, recombinant enzyme, with NADPH
4.6
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
12.4
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
13
glyoxylate
-
isoenzyme 1
0.058
Hydroxypyruvate

-
37ưC, cofactor: NAPDH
0.058
Hydroxypyruvate
-
pH 7.5, 37ưC, recombinant enzyme, with NADPH
0.085
Hydroxypyruvate
-
-
0.19
Hydroxypyruvate
-
37ưC, cofactor: NADH
0.19
Hydroxypyruvate
-
pH 7.5, 37ưC, recombinant enzyme, with NADH
0.013
NADH

-
with hydroxypyruvate as substrate, pH 7.5
0.015
NADH
-
with glyoxylate as substrate, pH 7.5
0.076
NADH
-
pH 6.7, 45ưC, substrate glyoxylate, purified recombinant enzyme
0.076
NADH
-
with glyoxylate as substrate, pH 6.7, 45ưC
0.4039
NADH
-
isoform GR2, at pH 7.4 and 30ưC
0.4202
NADH
-
isoform GR1, at pH 7.4 and 30ưC
2.42
NADH
-
pH 7.5, 37ưC, recombinant enzyme
0.0009
NADPH

pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
0.0012
NADPH
with succinic semialdehyde as substrate, pH 7.6, 30ưC
0.0012
NADPH
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30ưC
0.0012
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25ưC
0.0014
NADPH
with glyoxylate as substrate, pH 7.6, 30ưC
0.0014
NADPH
recombinant enzyme, using glyoxylate as fixed substrate, in 50 mM HEPES (pH 7.6), at 30ưC
0.0014
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25ưC
0.0018
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
0.0018
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.3 and 25ưC
0.002
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
0.0022
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a double beam spectrophotometer
0.0022
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.8 and 25ưC
0.0026
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25ưC
0.0027
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
0.0033
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.5 and 25ưC
0.0034
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
0.004
NADPH
-
isoenzyme 1
0.004
NADPH
-
pH 6.7, 45ưC, substrate glyoxylate, purified recombinant enzyme
0.0074
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.5 and 25ưC
0.0084
NADPH
-
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25ưC
0.0088
NADPH
-
isoform GLYR1, with glyoxylate as cosubstrate, at pH 6.5 and 25ưC
0.011
NADPH
-
pH 7.5, 37ưC, recombinant enzyme
0.0117
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25ưC
0.0125
NADPH
-
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25ưC
0.0176
NADPH
-
isoform GR1, at pH 7.4 and 30ưC
0.021
NADPH
-
with glyoxylate as substrate, pH 7.5
0.025
NADPH
-
with hydroxypyruvate as substrate, pH 7.5
0.0362
NADPH
-
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 6.5 and 25ưC
0.04
NADPH
-
with glyoxylate as substrate, pH 6.7, 45ưC
0.053
NADPH
-
isoform GR2, at pH 7.4 and 30ưC
0.0648
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
0.87
Succinic semialdehyde

recombinant protein from Escherichia coli
0.87
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25ưC
1.133
Succinic semialdehyde
isoform GLYR1, at pH 7.5 and 25ưC
1.457
Succinic semialdehyde
-
isoform GLYR2, at pH 7.1 and 25ưC
4.003
Succinic semialdehyde
-
isoform GLYR1, at pH 6.5 and 25ưC
6.5
Succinic semialdehyde
isoform GLYR2, at pH 7.3 and 25ưC
8.96
Succinic semialdehyde
with as NADPH as cofactor, pH 7.6, 30ưC
8.96
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30ưC
8.96
Succinic semialdehyde
isoform GLYR2, at pH 7.8 and 25ưC
additional information
additional information

-
kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics, altered cofactor kinetics of the mutant enzyme R31L/T32K/K35D/C68R compared to the wild-type
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0052 - 760000
glyoxylate
4.6 - 21.9
Succinic semialdehyde
4.8
glycolate

-
with NAD+ as cosubstrate, at pH 9.0 and 45ưC
10
glycolate
-
with NADP+ as cosubstrate, at pH 9.0 and 45ưC
0.0052
glyoxylate

pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E
0.051
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
6.06
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
10.8
glyoxylate
-
isoform GLYR2, at pH 7.1 and 25ưC
11
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
18.4
glyoxylate
isoform GLYR2, at pH 7.8 and 25ưC
19.1
glyoxylate
isoform GLYR2, at pH 7.3 and 25ưC
22
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
22.5
glyoxylate
with as NADPH as cofactor, pH 7.6, 30ưC
22.5
glyoxylate
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30ưC
27
glyoxylate
-
37ưC, cofactor: NADPH
27
glyoxylate
-
pH 7.5, 37ưC, recombinant enzyme, with NADPH
28.4
glyoxylate
isoform GLYR1, at pH 7.8 and 25ưC
30.9
glyoxylate
isoform GLYR1, at pH 7.5 and 25ưC
33.7
glyoxylate
-
isoform GLYR1, at pH 6.5 and 25ưC
54.6
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
67
glyoxylate
-
37ưC, cofactor: NADH
67
glyoxylate
-
pH 7.5, 37ưC, recombinant enzyme, with NADH
67.8
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
86.4
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
530
glyoxylate
-
with NADH as cosubstrate, at pH 4.0 and 45ưC
570
glyoxylate
-
with NADPH as cosubstrate, at pH 4.0 and 45ưC
3407
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enyzme
65000
glyoxylate
-
pH 6.7, 45ưC, cofactor NADPH, purified recombinant enzyme
76000
glyoxylate
-
pH 6.7, 45ưC, cofactor NADH, purified recombinant enzyme
650000
glyoxylate
-
with as NADPH as cofactor, pH 6.7, 45ưC
760000
glyoxylate
-
with as NADH as cofactor, pH 6.7, 45ưC
38
Hydroxypyruvate

-
37ưC, cofactor: NAPDH
38
Hydroxypyruvate
-
pH 7.5, 37ưC, recombinant enzyme, with NADPH
65
Hydroxypyruvate
-
37ưC, cofactor: NADH
65
Hydroxypyruvate
-
pH 7.5, 37ưC, recombinant enzyme, with NADH
4.1
NADH

-
with hydroxypyruvate as substrate, pH 7.5
11
NADH
-
with glyoxylate as substrate, pH 7.5
22000
NADH
-
pH 6.7, 45ưC, substrate glyoxylate, purified recombinant enzyme
220000
NADH
-
with glyoxylate as substrate, pH 6.7, 45ưC
1.8
NADPH

-
with hydroxypyruvate as substrate, pH 7.5
2.4
NADPH
-
with glyoxylate as substrate, pH 7.5
5.5
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.5 and 25ưC
6.5
NADPH
-
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25ưC
8.1
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25ưC
8.6
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25ưC
8.9
NADPH
-
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25ưC
9.09
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
9.3
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.8 and 25ưC
9.56
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
10.7
NADPH
with succinic semialdehyde as substrate, pH 7.6, 30ưC
10.7
NADPH
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30ưC
10.7
NADPH
-
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 6.5 and 25ưC
10.7
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25ưC
12
NADPH
with glyoxylate as substrate, pH 7.6, 30ưC
12
NADPH
recombinant enzyme, using glyoxylate as fixed substrate, in 50 mM HEPES (pH 7.6), at 30ưC
12
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25ưC
14.2
NADPH
-
isoform GLYR1, with glyoxylate as cosubstrate, at pH 6.5 and 25ưC
15.7
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.3 and 25ưC
22.3
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.5 and 25ưC
25.4
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
51.1
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
84.1
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
93.7
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
30000
NADPH
-
pH 6.7, 45ưC, substrate glyoxylate, purified recombinant enzyme
300000
NADPH
-
with glyoxylate as substrate, pH 6.7, 45ưC
4.6
Succinic semialdehyde

isoform GLYR1, at pH 7.5 and 25ưC
7.2
Succinic semialdehyde
-
isoform GLYR2, at pH 7.1 and 25ưC
10.1
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25ưC
10.3
Succinic semialdehyde
isoform GLYR2, at pH 7.3 and 25ưC
17
Succinic semialdehyde
with as NADPH as cofactor, pH 7.6, 30ưC
17
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30ưC
17
Succinic semialdehyde
isoform GLYR2, at pH 7.8 and 25ưC
21.9
Succinic semialdehyde
-
isoform GLYR1, at pH 6.5 and 25ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.6 - 11.6
Succinic semialdehyde
0.048
glycolate

-
with NAD+ as cosubstrate, at pH 9.0 and 45ưC
0.1
glycolate
-
with NADP+ as cosubstrate, at pH 9.0 and 45ưC
0.19
glyoxylate

pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E
0.86
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
0.87
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
7.45
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
14.6
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
72.8
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
349
glyoxylate
-
isoform GLYR2, at pH 7.1 and 25ưC
480
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
636
glyoxylate
-
isoform GLYR1, at pH 6.5 and 25ưC
796
glyoxylate
isoform GLYR2, at pH 7.3 and 25ưC
906
glyoxylate
isoform GLYR2, at pH 7.8 and 25ưC
910
glyoxylate
-
with NADH as cosubstrate, at pH 4.0 and 45ưC
1259
glyoxylate
isoform GLYR1, at pH 7.8 and 25ưC
1500
glyoxylate
-
with NADPH as cosubstrate, at pH 4.0 and 45ưC
2230
glyoxylate
isoform GLYR1, at pH 7.5 and 25ưC
2870
glyoxylate
pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer
3407
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enyzme
290
NADPH

-
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 6.5 and 25ưC
525
NADPH
-
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25ưC
660
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25ưC
779
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
832
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.5 and 25ưC
833
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25ưC
1040
NADPH
-
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25ưC
1729
NADPH
-
isoform GLYR1, with glyoxylate as cosubstrate, at pH 6.5 and 25ưC
2870
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.8 and 25ưC
3500
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25ưC
4340
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
6803
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.5 and 25ưC
9180
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25ưC
10070
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.3 and 25ưC
10400
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
10900
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
24450
NADPH
pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a microplate reader
51700
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
1.6
Succinic semialdehyde

isoform GLYR2, at pH 7.3 and 25ưC
1.9
Succinic semialdehyde
isoform GLYR2, at pH 7.8 and 25ưC
5.1
Succinic semialdehyde
isoform GLYR1, at pH 7.5 and 25ưC
5.1
Succinic semialdehyde
-
isoform GLYR2, at pH 7.1 and 25ưC
5.4
Succinic semialdehyde
-
isoform GLYR1, at pH 6.5 and 25ưC
11.6
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25ưC
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evolution

-
role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview
evolution
role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview
evolution
role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview
evolution
the deduced amino acid sequence of the enzyme from Paecilomyes thermophila has low similarities to the reported glyoxylate reductases
evolution
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family
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
the enzyme belongs to the group of enzymes with the most common NAD(P)-binding fold, the Rossmann fold, as well as other, less common cofactor binding folds (TIM barrel and dihydroquinoate synthase-like folds)
evolution
the primary sequence of cytosolic AtGLYR1 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR1 and beta-HAD family members, overview. 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
the primary sequence of plastidial AtGLYR2 reveals several sequence elements that are consistent with the beta-HAD (beta-hydroxyacid dehydrogenase) protein family, sequence alignment of AtGLYR2 and beta-HAD family members, overview. 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
-
the deduced amino acid sequence of the enzyme from Paecilomyes thermophila has low similarities to the reported glyoxylate reductases
-
evolution
-
role in the substrate binding mode and role of Leu53 and Trp138 in substrate trafficking is conserved between human and archeal enzymes, modelling, overview
-
malfunction

enzyme deficiency causes primary hyperoxaluria type 2
malfunction
enzyme deficiency is the underlying cause of primary hyperoxaluria type 2 (PH2) and leads to increased urinary oxalate levels, formation of kidney stones and renal failure. Upregulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is associated with intestinal epithelial cells apoptosis in TNBS-induced experimental colitis, the phenomenon also occurs in patients with Crohn's disease. Overexpression of GRHPR is accompanied by active caspase-3 and cleaved poly ADP-ribose polymerase (PARP) accumulation. Knockdown of GRHPR inhibits the accumulation of active caspase-3 and cleaved PARP in TNF-alpha treated HT-29 cells
metabolism

glyoxylate reductase is an important enzyme involved in theglyoxylate metabolism in organism
metabolism
glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is a key enzyme in the glyoxylate cycle
metabolism
-
glyoxylate reductase is an important enzyme involved in theglyoxylate metabolism in organism
-
physiological function

GLYR1 scavenges succinic semialdehyde and glyoxylate that escape from mitochondria and peroxisomes, respectively
physiological function
upregulation of glyoxylate reductase/hydroxypyruvate reductase is associated with intestinal epithelial cells apoptosis in trinitrobenzenesulfonic acid-induced colitis
physiological function
human glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is a D-2 hydroxy-acid dehydrogenase that plays a critical role in the removal of the metabolic by-product glyoxylate from the liver
physiological function
the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulate the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH
physiological function
-
the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulates the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH
physiological function
the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulates the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH
physiological function
-
isoforms GR1 and GR2 function redundantly in detoxifying glyoxylate in rice plants under normal growth conditions, whereas both are simultaneously required under high photorespiration conditions
physiological function
-
the NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases (GRHPR) regulates the glyoxylate content within cells, highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. The enzyme from the hyperthermophilic archaeon, displays a higher preference for glyoxylate than hydroxypyruvate in presence of NADH, whereas no activity is detected in presence of NADPH
-
additional information

due to the glutamate at the -1 position, GLYR1 C-terminal tripeptide, -SRE, does not function as a type 1 peroxisomal targeting signal, PTS1. GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
additional information
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
additional information
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
additional information
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
additional information
identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
additional information
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identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants by bifunctional enzyme glyoxylate/succinic semialdehyde reductase 1, that converts both glyoxylate and succinic semialdehyde into their corresponding hydroxyacid equivalents. Residue Lys170 is essential for catalysis, Phe231, Asp239, Ser121 and Thr95 are more important in substrate binding than in catalysis, and Asn174 is more important in catalysis. Residues Thr95, Phe231 and Asp239 serve a more important role in substrate orientation and docking than in catalysis
additional information
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residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
-
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
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