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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 25°C
0.87 - 8.96
Succinic semialdehyde
additional information
additional information
-
309
glycolate
-
with NAD+ as cosubstrate, at pH 9.0 and 45°C
334
glycolate
-
with NADP+ as cosubstrate, at pH 9.0 and 45°C
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 25°C
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 25°C
0.0193
glyoxylate
isoform GLYR2, at pH 7.8 and 25°C
0.0232
glyoxylate
isoform GLYR1, at pH 7.8 and 25°C
0.0239
glyoxylate
isoform GLYR2, at pH 7.3 and 25°C
0.0304
glyoxylate
-
isoform GR1, with NADPH as cosubstrate, at pH 7.4 and 30°C
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, 30°C
0.034
glyoxylate
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
0.0532
glyoxylate
-
isoform GLYR1, at pH 6.5 and 25°C
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 30°C
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 30°C
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
-
37°C, cofactor: NADPH
0.24
glyoxylate
-
pH 7.5, 37°C, recombinant enzyme, with NADPH
0.2677
glyoxylate
-
isoform GR1, with NADH as cosubstrate, at pH 7.4 and 30°C
0.38
glyoxylate
-
with NADPH as cosubstrate, at pH 4.0 and 45°C
0.5
glyoxylate
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
0.5
glyoxylate
-
with as NADPH as cofactor, pH 6.7, 45°C
0.58
glyoxylate
-
with NADH as cosubstrate, at pH 4.0 and 45°C
1
glyoxylate
-
37°C, cofactor: NADH
1
glyoxylate
-
pH 7.5, 37°C, recombinant enzyme, with NADH
1.1
glyoxylate
-
cofactor NADH
1.2
glyoxylate
-
pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme
1.2
glyoxylate
-
with as NADH as cofactor, pH 6.7, 45°C
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, 50°C, 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
-
37°C, cofactor: NAPDH
0.058
Hydroxypyruvate
-
pH 7.5, 37°C, recombinant enzyme, with NADPH
0.085
Hydroxypyruvate
-
-
0.19
Hydroxypyruvate
-
37°C, cofactor: NADH
0.19
Hydroxypyruvate
-
pH 7.5, 37°C, 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, 45°C, substrate glyoxylate, purified recombinant enzyme
0.076
NADH
-
with glyoxylate as substrate, pH 6.7, 45°C
0.4039
NADH
-
isoform GR2, at pH 7.4 and 30°C
0.4202
NADH
-
isoform GR1, at pH 7.4 and 30°C
2.42
NADH
-
pH 7.5, 37°C, 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, 30°C
0.0012
NADPH
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C
0.0012
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
0.0014
NADPH
with glyoxylate as substrate, pH 7.6, 30°C
0.0014
NADPH
recombinant enzyme, using glyoxylate as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C
0.0014
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
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 25°C
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 25°C
0.0026
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
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 25°C
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, 45°C, substrate glyoxylate, purified recombinant enzyme
0.0074
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.5 and 25°C
0.0084
NADPH
-
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25°C
0.0088
NADPH
-
isoform GLYR1, with glyoxylate as cosubstrate, at pH 6.5 and 25°C
0.011
NADPH
-
pH 7.5, 37°C, recombinant enzyme
0.0117
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25°C
0.0125
NADPH
-
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25°C
0.0176
NADPH
-
isoform GR1, at pH 7.4 and 30°C
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 25°C
0.04
NADPH
-
with glyoxylate as substrate, pH 6.7, 45°C
0.053
NADPH
-
isoform GR2, at pH 7.4 and 30°C
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 25°C
1.133
Succinic semialdehyde
isoform GLYR1, at pH 7.5 and 25°C
1.457
Succinic semialdehyde
-
isoform GLYR2, at pH 7.1 and 25°C
4.003
Succinic semialdehyde
-
isoform GLYR1, at pH 6.5 and 25°C
6.5
Succinic semialdehyde
isoform GLYR2, at pH 7.3 and 25°C
8.96
Succinic semialdehyde
with as NADPH as cofactor, pH 7.6, 30°C
8.96
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
8.96
Succinic semialdehyde
isoform GLYR2, at pH 7.8 and 25°C
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 45°C
10
glycolate
-
with NADP+ as cosubstrate, at pH 9.0 and 45°C
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 25°C
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 25°C
19.1
glyoxylate
isoform GLYR2, at pH 7.3 and 25°C
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, 30°C
22.5
glyoxylate
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
27
glyoxylate
-
37°C, cofactor: NADPH
27
glyoxylate
-
pH 7.5, 37°C, recombinant enzyme, with NADPH
28.4
glyoxylate
isoform GLYR1, at pH 7.8 and 25°C
30.9
glyoxylate
isoform GLYR1, at pH 7.5 and 25°C
33.7
glyoxylate
-
isoform GLYR1, at pH 6.5 and 25°C
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
-
37°C, cofactor: NADH
67
glyoxylate
-
pH 7.5, 37°C, 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 45°C
570
glyoxylate
-
with NADPH as cosubstrate, at pH 4.0 and 45°C
3407
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
65000
glyoxylate
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
76000
glyoxylate
-
pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme
650000
glyoxylate
-
with as NADPH as cofactor, pH 6.7, 45°C
760000
glyoxylate
-
with as NADH as cofactor, pH 6.7, 45°C
38
Hydroxypyruvate
-
37°C, cofactor: NAPDH
38
Hydroxypyruvate
-
pH 7.5, 37°C, recombinant enzyme, with NADPH
65
Hydroxypyruvate
-
37°C, cofactor: NADH
65
Hydroxypyruvate
-
pH 7.5, 37°C, 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, 45°C, substrate glyoxylate, purified recombinant enzyme
220000
NADH
-
with glyoxylate as substrate, pH 6.7, 45°C
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 25°C
6.5
NADPH
-
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25°C
8.1
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
8.6
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25°C
8.9
NADPH
-
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25°C
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 25°C
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, 30°C
10.7
NADPH
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C
10.7
NADPH
-
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 6.5 and 25°C
10.7
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
12
NADPH
with glyoxylate as substrate, pH 7.6, 30°C
12
NADPH
recombinant enzyme, using glyoxylate as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C
12
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
14.2
NADPH
-
isoform GLYR1, with glyoxylate as cosubstrate, at pH 6.5 and 25°C
15.7
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.3 and 25°C
22.3
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.5 and 25°C
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, 45°C, substrate glyoxylate, purified recombinant enzyme
300000
NADPH
-
with glyoxylate as substrate, pH 6.7, 45°C
4.6
Succinic semialdehyde
isoform GLYR1, at pH 7.5 and 25°C
7.2
Succinic semialdehyde
-
isoform GLYR2, at pH 7.1 and 25°C
10.1
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25°C
10.3
Succinic semialdehyde
isoform GLYR2, at pH 7.3 and 25°C
17
Succinic semialdehyde
with as NADPH as cofactor, pH 7.6, 30°C
17
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
17
Succinic semialdehyde
isoform GLYR2, at pH 7.8 and 25°C
21.9
Succinic semialdehyde
-
isoform GLYR1, at pH 6.5 and 25°C
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1.6 - 11.6
Succinic semialdehyde
0.048
glycolate
-
with NAD+ as cosubstrate, at pH 9.0 and 45°C
0.1
glycolate
-
with NADP+ as cosubstrate, at pH 9.0 and 45°C
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 25°C
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 25°C
796
glyoxylate
isoform GLYR2, at pH 7.3 and 25°C
906
glyoxylate
isoform GLYR2, at pH 7.8 and 25°C
910
glyoxylate
-
with NADH as cosubstrate, at pH 4.0 and 45°C
1259
glyoxylate
isoform GLYR1, at pH 7.8 and 25°C
1500
glyoxylate
-
with NADPH as cosubstrate, at pH 4.0 and 45°C
2230
glyoxylate
isoform GLYR1, at pH 7.5 and 25°C
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 enzyme
290
NADPH
-
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 6.5 and 25°C
525
NADPH
-
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25°C
660
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
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 25°C
833
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25°C
1040
NADPH
-
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25°C
1729
NADPH
-
isoform GLYR1, with glyoxylate as cosubstrate, at pH 6.5 and 25°C
2870
NADPH
isoform GLYR1, with glyoxylate as cosubstrate, at pH 7.8 and 25°C
3500
NADPH
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
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 25°C
9180
NADPH
isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C
10070
NADPH
isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.3 and 25°C
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 25°C
1.9
Succinic semialdehyde
isoform GLYR2, at pH 7.8 and 25°C
5.1
Succinic semialdehyde
isoform GLYR1, at pH 7.5 and 25°C
5.1
Succinic semialdehyde
-
isoform GLYR2, at pH 7.1 and 25°C
5.4
Succinic semialdehyde
-
isoform GLYR1, at pH 6.5 and 25°C
11.6
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25°C
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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
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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
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tetramer
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4 * 33000, SDS-PAGE
?
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x * 328000, calculated from amino acid sequence
?
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x * 328000, calculated from amino acid sequence
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?
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x * 330000, SDS-PAGE
-
?
x * 35900, truncated enzyme from Escherichia coli including His-tag
?
x * 36287, calculated from the deduced amino acid sequence
?
x * 30700, isoform GLYR1, calculated from amino acid sequence
?
x * 33200, isoform GLYR2, calculated from amino acid sequence
?
x * 31800, isoform GLYR1, calculated from amino acid sequence
?
x * 33100, isoform GLYR2, calculated from amino acid sequence
?
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x * 30500, isoform GLYR1, calculated from amino acid sequence
?
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x * 31400, isoform GLYR2, calculated from amino acid sequence
?
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x * 30000, isoform GR1, SDS-PAGE
?
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x * 37000, isoform GR2, SDS-PAGE
dimer
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x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation
dimer
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2 * 36000, SDS-PAGE, native mass by gel filtration (native mass not given in the reference)
homodimer
2 * 35898, sequence calculation, 2 * 42000, SDS-PAGE, recombinant enzyme
homodimer
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2 * 35898, sequence calculation, 2 * 42000, SDS-PAGE, recombinant enzyme
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homodimer
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x-ray crystallography
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
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domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
the overall structure of the apo-enzyme monomer adopts the typical D-2-hydroxy-aciddehydrogenase fold with a closed conformation, which comprises two alpha/beta/alpha domains, structure analysis, overview
additional information
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the overall structure of the apo-enzyme monomer adopts the typical D-2-hydroxy-aciddehydrogenase fold with a closed conformation, which comprises two alpha/beta/alpha domains, structure analysis, overview
additional information
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the overall structure of the apo-enzyme monomer adopts the typical D-2-hydroxy-aciddehydrogenase fold with a closed conformation, which comprises two alpha/beta/alpha domains, structure analysis, overview
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purified apo-enzyme, sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution containing 0.2 M calcium acetate hydrate, 20% PEG 3350, pH 6.5, 20°C, 6 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using a previously unrecognized member of the beta-HAD family, cytokine-like nuclear factor, structure
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
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sitting-drop vapour-diffusipon method. Crystal structure at 2.2 Å resolution. There are four copies of GRHPR in the crystallographic asymmetric unit: in each homodimer, one subunit forms a ternary (enzyme/NADPH/reduced substrate) complex, and the other a binary (enzyme/NADPH) form. The spatial arrangement of the two enzyme domains is the same in binary and ternary forms
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purified recombinant enzyme, sitting drop vapour diffusion method, the reservoir solution contains 0.1 M MES buffer, pH 6.5, 0.01 M cobalt (II) chloride, and 1.8 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis at 1.75 A resolution
purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, hanging drop vapour diffusion method, from a mother liquor containing 100 mM sodium acetate, pH 5.2, 15% PEG 400, and 100 mM NaCl, 20°C, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution
analysis of the three-dimensional crystal structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR
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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
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purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, sitting drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein solution with 0.0015 ml of mother liquor containing 1.7 malonate, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 1.4 A-2.0 A resolution, molecular replacement using the three-dimensional structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR
enzyme with NADP+ plus sulfate, sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 5.5, 25% (w/v) PEG 3350, 0.2 M ammonium sulfate. Enzyme with NADPH plus oxalate, sitting drop vapor diffusion method, using 0.2 M ammonium citrate tribasic pH 7.0, 20% (w/v) PEG 3350. Apo enzyme form, sitting drop vapor diffusion method, using 0.1 M sodium citrate, pH 5.6, 20% (v/v) 2-propanol, 20% (w/v) PEG 4000
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ammonium sulfate, affinity chromatography, Sephadex G-75SF, AgdApP-4
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centrifugation at 10500g, isoelectric focusing
Populus gelrica
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ethanol precipitation, DEAE-cellulose, CM-cellulose, affinity chromatography
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His-tag affinity Ni-IDA resin column chromatography
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isoenzyme 1, protamine sulfate, DEAE-cellulose, hydroxylapatite, Sephadex G-150, DEAE-cellulose, hydroxylapatite
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isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxyapatite, Sephadex G-150, phosphocellulose
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isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxylapatite, Sephadex G-150, DEAE-cellulose, phospho-cellulose
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Ni-NTA column chromatography
Ni-NTA resin column chromatography and Superdex 200 pg gel filtration
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Ni-NTA Sepharose column chromatography
nickel affinity column chromatography
recombinant C-terminally His9-tagged enzyme from Escherichia coli by nickel affinity chromatography to homogeneity
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recombinant His-tagged enzyme 2.7fold from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography, the His-tag is cleaved by thrombin followed by gel filtration, over 95% purity
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recombinant His6-tagged truncated mutant enzyme from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography
recombinant protein from Escherichia coli
recombinant protein from Escherichia coli using His-tag
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recombinant truncated protein using His-tag
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
Ni-NTA column chromatography
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Ni-NTA column chromatography
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nickel affinity column chromatography
-
nickel affinity column chromatography
nickel affinity column chromatography
nickel affinity column chromatography
recombinant protein from Escherichia coli
-
recombinant protein from Escherichia coli
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
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Yokota, A.; Kitaoka, S.
Occurrence and subcellular distribution of enzymes involved in the glycolate pathway and their physiological function in a bleached mutant of Euglena gracilis Z
Agric. Biol. Chem.
45
15-22
1981
Euglena gracilis
-
brenda
Kleczkowski, L.A.
Kinetics and regulation of the NAD(P)H-dependent glyoxylate-specific reductase from spinach leaves
Z. Naturforsch. C
50
21-28
1995
Spinacia oleracea
-
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Husic, D.W.; Tolbert, N.E.
NADH:hydroxypyruvate reductase and NADPH:glyoxylate reductase in algae: partial purification and characterization from Chlamydomonas reinhardtii
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252
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1987
Chlamydomonas reinhardtii
brenda
Kleczkowski, L.A.; Randall, D.D.; Blevins, D.G.
Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase
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Glycine max, Spinacia oleracea, Triticum aestivum
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Purification and some properties of glyoxylate reductase (NADP+) and its functional location in mitochondria in Euglena gracilis Z
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Euglena gracilis
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Effects of glyoxylate on photosynthesis by intact chloroplasts
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72
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1983
Spinacia oleracea
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Fukuda, H.; Moriguchi, M.; Kimura, A.; Tochikura, T.
Purification and properties of glyoxylate reductase from Neurospora crassa
Agric. Biol. Chem.
45
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Neurospora crassa
-
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Fukuda, H.; Moriguchi, M.; Tochikura, T.
Purification and enzymatic properties of glyoxylate reductase II from baker's yeast
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87
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Saccharomyces cerevisiae
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Occurrence of nicotinamide adenine dinucleotide phosphate-linked glyoxylate reductase in nonphotosynthetic xylem tissue of perennials
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65
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1980
Populus gelrica
brenda
Yokota, A.; Kitaoka, S.
Occurrence and properties of the glycollate-glyoxylate shuttle in mitochondria of Euglena gracilis z
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184
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Euglena gracilis
brenda
Tochikura, T.; Fukuda, H.; Moriguchi, M.
Purification and properties of glyoxylate reductase I from baker's yeast
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86
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1979
Saccharomyces cerevisiae
brenda
Zeltich, I.
Effect of glycidate, an inhibitor of glycolate synthesis in leaves, on the activity of some enzymes of the glycolate pathway
Plant Physiol.
61
236-241
1978
Nicotiana tabacum
brenda
Mdluli, K.; Booth, M.P.; Brady, R.L.; Rumsby, G.
A preliminary account of the properties of recombinant human glyoxylate reductase (GRHPR), LDHA and LDHB with glyoxylate, and their potential roles in its metabolism
Biochim. Biophys. Acta
1753
209-216
2005
Homo sapiens
brenda
Genolet, R.; Kersten, S.; Braissant, O.; Mandard, S.; Tan, N.S.; Bucher, P.; Desvergne, B.; Michalik, L.; Wahli, W.
Promoter rearrangements cause species-specific hepatic regulation of the glyoxylate reductase/hydroxypyruvate reductase gene by the peroxisome proliferator-activated receptor alpha
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280
24143-24152
2005
Homo sapiens, Mus musculus
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Booth, M.P.; Conners, R.; Rumsby, G.; Brady, R.L.
Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase
J. Mol. Biol.
360
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2006
Homo sapiens
brenda
Yoshikawa, S.; Arai, R.; Kinoshita, Y.; Uchikubo-Kamo, T.; Wakamatsu, T.; Akasaka, R.; Masui, R.; Terada, T.; Kuramitsu, S.; Shirouzu, M.; Yokoyama, S.
Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate
Acta Crystallogr. Sect. D
63
357-365
2007
Pyrococcus horikoshii OT3
brenda
Ogino, H.; Nakayama, H.; China, H.; Kawata, T.; Doukyu, N.; Yasuda, M.
Characterization of recombinant glyoxylate reductase from thermophile Thermus thermophilus HB27
Biotechnol. Prog.
24
321-325
2008
Thermus thermophilus, Thermus thermophilus HB27, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
brenda
Hoover, G.J.; Prentice, G.A.; Merrill, A.R.; Shelp, B.J.
Kinetic mechanism of a recombinant Arabidopsis glyoxylate reductase: studies of initial velocity, dead-end inhibition and product inhibition
Can. J. Bot.
85
896-902
2007
Arabidopsis thaliana (Q9LSV0)
brenda
Simpson, J.P.; Di Leo, R.; Dhanoa, P.K.; Allan, W.L.; Makhmoudova, A.; Clark, S.M.; Hoover, G.J.; Mullen, R.T.; Shelp, B.J.
Identification and characterization of a plastid-localized Arabidopsis glyoxylate reductase isoform: comparison with a cytosolic isoform and implications for cellular redox homeostasis and aldehyde detoxification
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59
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2008
Arabidopsis thaliana (F4I907), Arabidopsis thaliana (Q9LSV0), Arabidopsis thaliana
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Gamma-hydroxybutyrate accumulation in Arabidopsis and tobacco plants is a general response to abiotic stress: putative regulation by redox balance and glyoxylate reductase isoforms
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59
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Arabidopsis thaliana, Nicotiana tabacum
brenda
Rintala, E.; Pitkanen, J.; Vehkomaki, M.; Penttila, M.; Ruohonen, L.
The ORF YNL274c (GOR1) codes for glyoxylate reductase in Saccharomyces cerevisiae
Yeast
24
129-136
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
brenda
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Role of plant glyoxylate reductases during stress: a hypothesis
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Arabidopsis thaliana
brenda
Ching, S.L.; Gidda, S.K.; Rochon, A.; van Cauwenberghe, O.R.; Shelp, B.J.; Mullen, R.T.
Glyoxylate reductase isoform 1 is localized in the cytosol and not peroxisomes in plant cells
J. Integr. Plant Biol.
54
152-168
2012
Arabidopsis thaliana (Q9LSV0)
brenda
Hoover, G.J.; Jorgensen, R.; Rochon, A.; Bajwa, V.S.; Merrill, A.R.; Shelp, B.J.
Identification of catalytically important amino acid residues for enzymatic reduction of glyoxylate in plants
Biochim. Biophys. Acta
1834
2663-2671
2013
Arabidopsis thaliana (A0A178WMD4), Arabidopsis thaliana (F4I907), Arabidopsis thaliana (Q9CA90), Arabidopsis thaliana (Q9LSV0), Arabidopsis thaliana
brenda
Pan, Y.; Ni, R.; Deng, Q.; Huang, X.; Zhang, Y.; Lu, C.; Li, F.; Huang, D.; He, S.; Chen, B.
Glyoxylate reductase/hydroxypyruvate reductase: a novel prognostic marker for hepatocellular carcinoma patients after curative resection
Pathobiology
80
155-162
2013
Homo sapiens (Q9UBQ7)
brenda
Zong, C.; Nie, X.; Zhang, D.; Ji, Q.; Qin, Y.; Wang, L.; Jiang, D.; Gong, C.; Liu, Y.; Zhou, G.
Up regulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is associated with intestinal epithelial cells apoptosis in TNBS-induced experimental colitis
Pathol. Res. Pract.
212
365-371
2016
Homo sapiens (Q9UBQ7), Homo sapiens
brenda
Lassalle, L.; Engilberge, S.; Madern, D.; Vauclare, P.; Franzetti, B.; Girard, E.
New insights into the mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductases
Sci. Rep.
6
20629
2016
Pyrococcus horikoshii, Pyrococcus yayanosii (F8AEA4), Pyrococcus furiosus (Q8U3Y2), Pyrococcus yayanosii CH1 (F8AEA4)
brenda
Cahn, J.K.; Werlang, C.A.; Baumschlager, A.; Brinkmann-Chen, S.; Mayo, S.L.; Arnold, F.H.
A general tool for engineering the NAD/NADP cofactor preference of oxidoreductases
ACS Synth. Biol.
6
326-333
2016
Arabidopsis thaliana (Q9LSV0)
brenda
Duan, X.; Hu, S.; Zhou, P.; Zhou, Y.; Liu, Y.; Jiang, Z.
Characterization and crystal structure of a first fungal glyoxylate reductase from Paecilomyes thermophila
Enzyme Microb. Technol.
60
72-79
2014
Paecilomyces sp. 'thermophila' (A0A0H3U0Y7), Paecilomyces sp. 'thermophila', Paecilomyces sp. 'thermophila' J18 (A0A0H3U0Y7)
brenda
Cahn, J.K.; Werlang, C.A.; Baumschlager, A.; Brinkmann-Chen, S.; Mayo, S.L.; Arnold, F.H.
A general tool for engineering the NAD/NADP cofactor preference of oxidoreductases
ACS Synth. Biol.
6
326-333
2017
Arabidopsis thaliana (Q9LSV0)
brenda
Kutner, J.; Shabalin, I.G.; Matelska, D.; Handing, K.B.; Gasiorowska, O.; Sroka, P.; Gorna, M.W.; Ginalski, K.; Wozniak, K.; Minor, W.
Structural, biochemical, and evolutionary characterizations of glyoxylate/hydroxypyruvate reductases show their division into two distinct subfamilies
Biochemistry
57
963-977
2018
Sinorhizobium meliloti
brenda
Kumsab, J.; Tobe, R.; Kurihara, T.; Hirose, Y.; Omori, T.; Mihara, H.
Characterization of a novel class of glyoxylate reductase belonging to the beta-hydroxyacid dehydrogenase family in Acetobacter aceti
Biosci. Biotechnol. Biochem.
84
2303-2310
2020
Acetobacter aceti, Acetobacter aceti JCM20276
brenda
Zhang, Z.; Liang, X.; Lu, L.; Xu, Z.; Huang, J.; He, H.; Peng, X.
Two glyoxylate reductase isoforms are functionally redundant but required under high photorespiration conditions in rice
BMC Plant Biol.
20
357
2020
Oryza sativa Japonica Group
brenda
Zarei, A.; Brikis, C.J.; Bajwa, V.S.; Chiu, G.Z.; Simpson, J.P.; DeEll, J.R.; Bozzo, G.G.; Shelp, B.J.
Plant glyoxylate/succinic semialdehyde reductases comparative biochemical properties, function during chilling stress, and subcellular localization
Front. Plant Sci.
8
1399
2017
Oryza sativa, Malus domestica (A0A1C8M582), Malus domestica (A0A1C8M593), Arabidopsis thaliana (F4I907), Arabidopsis thaliana (Q9LSV0)
brenda
Yadav, S.; Mody, T.A.; Sharma, A.; Bachhawat, A.K.
A genetic screen to identify genes influencing the secondary redox couple NADPH/NADP+ in the yeast Saccharomyces cerevisiae
G3 (Bethesda)
10
371-378
2020
Saccharomyces cerevisiae
brenda