1.1.1.79: glyoxylate reductase (NADP+)
This is an abbreviated version!
For detailed information about glyoxylate reductase (NADP+), go to the full flat file.
Reaction
Synonyms
aac4036, At3g25530, AtGLYR1, AtGLYR2, AtGR1, AtGR2, D-2-hydroxy-acid dehydrogenase, GhrA, glycerate dehydrogenase, glyoxylate reductase, glyoxylate reductase 1, glyoxylate reductase 2, glyoxylate reductase isoform 1, glyoxylate reductase/hydroxypyruvate reductase, glyoxylate/succinic semialdehyde reductase, GLYR1, GLYR2, GOR1, Gor1p, GR/HPR, GR1, GR2, GRHPR, GRHRP, HPR2, HPR3, More, NAD(P)H-dependent GR, NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases, PfuGRHPR, PhoGRHPR, PtGR, PyaGRHPR, TthGR1
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Substrates Products
Substrates Products on EC 1.1.1.79 - glyoxylate reductase (NADP+)
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REACTION DIAGRAM
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
13.9% of glyoxylate activity
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
10.4% of glyoxylate activity
-
?
glyoxal + NADPH
glycol + NADP+
-
isoenzyme 1, 16% activity of glyxoxylate
-
?
hydroxypyruvate + NADH
D-glycerate + NAD+
-
affinity for NADPH is lower than affinity for NADH
-
-
?
phenylpyruvate + NAD(P)H
phenyllactate + NAD(P)+
-
isoenzyme 2, 6% activity of glyoxylate
-
?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
NADH much less effective than NADPH
-
-
?
2-hydroxy-4-methylpentanoate + NADP+
-
low activity
-
-
?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
-
low activity
-
-
?
glyoxylate + NADH + H+
-
the reaction occurs only at pH 9.0
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
Acetobacter aceti JCM20276
-
the reaction occurs only at pH 9.0
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glyoxylate + NAPDH + H+
-
the reaction occurs only at pH 9.0
-
-
?
glycolate + NADP+
glyoxylate + NAPDH + H+
Acetobacter aceti JCM20276
-
the reaction occurs only at pH 9.0
-
-
?
glycolate + NAD(P)+
-
enzyme prefers NADPH
-
?
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)+
-
isoenzyme 2, 16% activity with NADH
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
7% of activity with glyoxylate
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
-
?
glycolate + NAD+
NADH much less effective than NADPH
-
-
ir
glyoxylate + NADH
glycolate + NAD+
-
affinity for NADPH is lower than affinity for NADH
-
-
?
glycolate + NAD+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
Acetobacter aceti JCM20276
-
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+
-
NADPH-dependent activity is much higher than the NADH-dependent activity
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
-
r
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
-
-
?
glycolate + NADP+
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
Acetobacter aceti JCM20276
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
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+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
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+
-
enzyme GhrA shows highest catalytic efficiency for glyoxylate
-
-
?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
-
preferred substrate
-
-
?
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)+
-
isoenzyme 1, hydroxypyruvate shows 15% of the activity of glyoxylate
-
?
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+
-
15% activity compared to glyoxylate
-
-
?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
-
15% activity compared to glyoxylate
-
-
?
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+
-
-
-
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+
-
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
?
-
-
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
?
-
Acetobacter aceti JCM20276
-
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
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-
-
additional information
?
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involved in stress response, enhanced transcript levels of GR1 at salinity, drought, submergence, and heat and GR2 at cold and heat
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-
?
additional information
?
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glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
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-
?
additional information
?
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glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
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?
additional information
?
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glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
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-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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-
?
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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-
?
additional information
?
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-
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
?
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the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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-
?
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
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-
?
additional information
?
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enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
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?
additional information
?
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structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview
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-
?
additional information
?
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the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate
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-
?
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
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-
?
additional information
?
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-
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
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-
-
additional information
?
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substrate specificity, several 2-oxo compounds including phenylpyruvate, pyruvate, methylglyoxal, and oxaloacetate act as inert electron acceptors, as do glycolate and malate, overview
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-
?
additional information
?
-
-
phenylpyruvate, pyruvate, methylglyoxal, malate, and oxaloacetate not suitable as substrate
-
-
?
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
substrate specificity, several 2-oxo compounds including phenylpyruvate, pyruvate, methylglyoxal, and oxaloacetate act as inert electron acceptors, as do glycolate and malate, overview
-
-
?