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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Natural Substrates Products
Natural Substrates Products on EC 1.1.1.79 - glyoxylate reductase (NADP+)
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REACTION DIAGRAM
hydroxypyruvate + NADH + H+
D-glycerate + NAD+
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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
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glycolate + NADP+
glyoxylate + NADPH + H+
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r
glycolate + NADP+
glyoxylate + NADPH + H+
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?
glycolate + NAD(P)+
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enzyme prefers NADPH
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glyoxylate + NAD(P)H
glycolate + NAD(P)+
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the enzyme is involved in removal of the metabolic by-product from liver
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glyoxylate + NAD(P)H
glycolate + NAD(P)+
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the enzyme plays a protective role in detoxification of glyoxylate
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glyoxylate + NAD(P)H
glycolate + NAD(P)+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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glycolate + NAD+
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the specific activity with NADPH is slightly higher as that with NADH
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glyoxylate + NADH + H+
glycolate + NAD+
Acetobacter aceti JCM20276
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the specific activity with NADPH is slightly higher as that with NADH
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?
glyoxylate + NADPH
glycolate + NADP+
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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
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glycolate + NADP+
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the specific activity with NADPH is slightly higher as that with NADH
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glyoxylate + NADPH + H+
glycolate + NADP+
Acetobacter aceti JCM20276
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the specific activity with NADPH is slightly higher as that with NADH
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?
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
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ir
glyoxylate + NADPH + H+
glycolate + NADP+
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enzyme GhrA shows highest catalytic efficiency for glyoxylate
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?
4-hydroxybutyrate + NADP+
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at least under oxygen deficient and high light conditions
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ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
detoxification of succinic semialdehyde during stress
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r
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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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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
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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
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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
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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
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additional information
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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
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?
additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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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
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the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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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
?
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the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
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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
?
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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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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
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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
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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
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?