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Information on EC 1.1.1.79 - glyoxylate reductase (NADP+)
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1.1.1.79 glyoxylate reductase (NADP+)IUBMB Comments
Also reduces hydroxypyruvate to glycerate; has some affinity for NAD+.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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Synonyms
aac4036, At3g25530, AtGLYR1, AtGLYR2, AtGR1, AtGR2, D-2-hydroxy-acid dehydrogenase, GhrA, glycerate dehydrogenase, glyoxylate reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aac4036
AtGR1
AtGR2
glyoxylate reductase
glyoxylate reductase/hydroxypyruvate reductase
glyoxylate/succinic semialdehyde reductase
GLYR1
GLYR2
GOR1
GR1
GR2
GRHPR
GRHRP
NAD(P)H-dependent GR
NADPH/NADH-dependent glyoxylate/hydroxypyruvate reductases
PtGR
PyaGRHPR
TthGR1
-
belongs to the D-2-hydroxyacid dehydrogenase family, enzyme used NADPH and NADH (EC 1.1.1.26 activity) as cofactor
additional information
GRHPR
bifunctional enzyme with glyoxylate reductase and hydroxypyruvate reductase activities
additional information
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency
additional information
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency
additional information
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency
additional information
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the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81
additional information
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the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81
additional information
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enzyme shows NADH- and NADPH-dependent glyoxylate reductase (EC 1.1.1.26 or 1.1.1.79) activity with higher efficiency with NADH but higher affinity for NADPH when enzyme is incubated without substrate, enzyme displays also hydroxypyruvate reductase (EC 1.1.1.81) activity, closely related to D-glycerate dehydrogense (EC 1.1.1.29)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glycerate + NAD(P)+ = glyoxylate + NADPH + H+
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glycolate + NADP+ = glyoxylate + NADPH + H+
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glycolate + NADP+ = glyoxylate + NADPH + H+
ordered Bi Bi mechanism, complexation of NADPH to the enzyme before glyoxylate or succinic semialdehyde, and release of NADP+ before glycolate or 4-hydroxybutyrate
glycolate + NADP+ = glyoxylate + NADPH + H+
the enzyme performs an acid/base catalytic mechanism involving Lys170 as the general acid and a conserved active-site water molecule
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
glycolate:NADP+ oxidoreductase
Also reduces hydroxypyruvate to glycerate; has some affinity for NAD+.
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CAS REGISTRY NUMBER
COMMENTARY
37250-17-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
13.9% of glyoxylate activity
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
10.4% of glyoxylate activity
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?
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-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
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low activity
-
-
?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
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low activity
-
-
?
glycolate + NAD+
glyoxylate + NADH + H+
-
the reaction occurs only at pH 9.0
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-
?
glycolate + NAD+
glyoxylate + NADH + H+
Acetobacter aceti JCM20276
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the reaction occurs only at pH 9.0
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-
?
glycolate + NAD+
glyoxylate + NADH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
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-
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r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glycolate + NADP+
glyoxylate + NAPDH + H+
-
the reaction occurs only at pH 9.0
-
-
?
glycolate + NADP+
glyoxylate + NAPDH + H+
Acetobacter aceti JCM20276
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the reaction occurs only at pH 9.0
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-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
enzyme prefers NADPH
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
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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)+
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7% of activity with glyoxylate
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?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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-
-
-
?
glyoxylate + NADH
glycolate + NAD+
NADH much less effective than NADPH
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-
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+
Acetobacter aceti JCM20276
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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+
NADH much less effective than NADPH
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ir
glyoxylate + NADH + H+
glycolate + NAD+
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NADPH-dependent activity is much higher than the NADH-dependent activity
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-
?
glyoxylate + NADH + H+
glycolate + NAD+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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-
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r
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
-
-
?
glyoxylate + NADPH + H+
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
-
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?
glyoxylate + NADPH + H+
glycolate + NADP+
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-
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r
glyoxylate + NADPH + H+
glycolate + NADP+
preferred substrate
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ir
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
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ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
glyoxylate highly preferred over succinic semialdehyde as substrate
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-
?
glyoxylate + NADPH + H+
glycolate + NADP+
glyoxylate reductase 2 has a 350fold higher preference for glyoxylate than for succinic semialdehyde
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ir
glyoxylate + NADPH + H+
glycolate + NADP+
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the affinity for glyoxylate is 10fold lower for isoform GLYR2 than that for isoform GLYR1
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ir
glyoxylate + NADPH + H+
glycolate + NADP+
the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
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?
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+
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the enzyme prefers glyoxylate over succinic semialdehyde, and has a high affinity for their co-substrate NADPH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
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NADPH-dependent activity is much higher than the NADH-dependent activity
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?
glyoxylate + NADPH + H+
glycolate + NADP+
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enzyme GhrA shows highest catalytic efficiency for glyoxylate
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
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preferred substrate
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?
hydroxypyruvate + NAD(P)H + H+
glycerate + NAD(P)+
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25 mM hydroxypyruvate, 68% of the activity with glyoxylate, 2.5 mM hydroxypyruvate, isoenzyme 2, 332% of the activity of glyoxylate
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?
hydroxypyruvate + NAD(P)H + H+
glycerate + NAD(P)+
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isoenzyme 1, hydroxypyruvate shows 15% of the activity of glyoxylate
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?
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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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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15% activity compared to glyoxylate
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?
hydroxypyruvate + NADPH + H+
D-glycerate + NADP+
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15% activity compared to glyoxylate
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?
oxaloacetate + NADPH
malate + NADP+
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28.6% of glyoxylate activity
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?
oxaloacetate + NADPH
malate + NADP+
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isoenzyme 1, 12% activity of glyoxylate
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?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
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ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
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r
succinic semialdehyde + NADPH + H+
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
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
reverse reaction less efficient than forward reaction
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r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
glyoxylate reductase 2 has a 350fold higher preference for glyoxylate than for succinic semialdehyde
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ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
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the affinity for succinic semialdehyde is 10fold lower for isoform GLYR2 than that for isoform GLYR1
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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
-
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?
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
-
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?
additional information
?
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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
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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
-
-
?
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
-
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?
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
-
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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
-
-
?
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
?
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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
-
-
?
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
?
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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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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
?
-
-
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
?
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
?
glyoxylate + NAD(P)H
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)+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
-
?
glyoxylate + NADH + H+
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 + 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+
Acetobacter aceti JCM20276
-
the specific activity with NADPH is slightly higher as that with NADH
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
enzyme GhrA shows highest catalytic efficiency for glyoxylate
-
-
?
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
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADPH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
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 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 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
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.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxybutyrate
mixed type inhibition with NADPH; mixed type inhibition with succinic semialdehyde
ethanol
-
enzyme activity is decreased to 20% by incubation with 60% (v/v) ethanol
iodoacetate
-
isoenzyme 2, 1 mM, 97% inhibition, isoenzyme 1, 1 mM, 18% 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
sodium iodide
-
isoenzyme 1, 50 mM, 37% inhibition of glyoxylate reduction
dithiothreitol
-
isoenzyme 1, 1 mM, 41% inhibition, 10 mM, 87% inhibition
glycolate
mixed type inhibition with glyoxylate; uncompetitive with NADPH
iodoacetamide
-
isoenzyme 2, 1 mM, 87% inhibition, isoenzyme 1, 1 mM, 17% inhibition
NADP+
competitive with NADPH; competitive with NADPH when glyoxylate is the fixed substrate; uncompetitive with glyoxylate; uncompetitive with succinic semialdehyde
p-chloromercuribenzoate
-
0.1 mM, 55% inhibition after preincubation for 5 min
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 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.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hyperoxaluria, Primary
Up regulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is associated with intestinal epithelial cells apoptosis in TNBS-induced experimental colitis.
Liver Cirrhosis
Association between angiotensin II type 1 receptor polymorphisms and the occurrence of nonalcoholic fatty liver disease.
Neoplasms
Identification of NPAC as a novel biomarker and regulator for hepatocellular carcinoma.
Non-alcoholic Fatty Liver Disease
Association between angiotensin II type 1 receptor polymorphisms and the occurrence of nonalcoholic fatty liver disease.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0045
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a double beam spectrophotometer
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
0.0304
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
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C
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
0.088
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
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
0.2677
glyoxylate
-
isoform GR1, with NADH as cosubstrate, at pH 7.4 and 30°C
0.5
glyoxylate
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
1.2
glyoxylate
-
pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme
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
0.076
NADH
-
pH 6.7, 45°C, substrate glyoxylate, purified 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
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
-
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
0.0117
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
0.0362
NADPH
-
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 6.5 and 25°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
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
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.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
11
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
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
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°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
67.8
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
3407
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enyzme
65000
glyoxylate
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
76000
glyoxylate
-
pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme
22000
NADH
-
pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme
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
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
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
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
4.6
Succinic semialdehyde
isoform GLYR1, at pH 7.5 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
480
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
2870
glyoxylate
pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer
3407
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enyzme
290
NADPH
-
isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 6.5 and 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
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
11.6
Succinic semialdehyde
isoform GLYR1, at pH 7.8 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
93.5
4-hydroxybutyrate
mixed type inhibition with succinic semialdehyde
0.0095
NADP+
competitive with NADPH when glyoxylate is the fixed substrate
3.6
oxalate
-
isoform GR1, with glyoxylate and NADH as substrates, at pH 7.4 and 30°C
8.2
oxalate
-
isoform GR2, with glyoxylate and NADH as substrates, at pH 7.4 and 30°C
212
oxalate
-
isoform GR1, with glyoxylate and NADPH as substrates, at pH 7.4 and 30°C
290.8
oxalate
-
isoform GR2, with glyoxylate and NADPH as substrates, at pH 7.4 and 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.45 - 0.7
1300
-
after 2.81fold purification, the reaction mixture contains 100 mM citrate buffer (pH 4.0), 1 mM glyoxylate, and 0.15 mM NADPH at 45°C
24.2
purified recombinant enzyme, pH 7.5, 50°C, with NADH
463
-
crude extract, the reaction mixture contains 100 mM citrate buffer (pH 4.0), 1 mM glyoxylate, and 0.15 mM NADPH at 45°C
70.1
purified recombinant enzyme, pH 7.5, 50°C, with NADPH
additional information
additional information
-
activities of wild-type and mutant strains, overview
additional information
-
3 micromol/min mg chlorophyll, chloroplast preparations
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.45
-
enzyme activity decreases by 40% and 50% at pH 5.5 and 8.0 respectively
6.7
6.8
6.8 - 7.8
7.5
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 8
-
approximately 50% of the activity is retained at a pH of 3.5 and 8.0, respectively
5.5 - 7
5.5 - 7
enzyme isoform GLYR1 retains at least half of maximal activity over the pH range of 5.5-7.0
5.5 - 7
-
enzyme isoform GLYR1 retains at least half of maximal activity over the pH range of 5.5-7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 45
-
the enzyme shows relatively high activity over a broad temperature range (30-45°C)
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency; (L.) Heynh
SwissProt
brenda
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency; L. Heynh
SwissProt
brenda
L. Heynh ecotype Columbia, plants exposed to the stress factors drought, salinity, submergence, cold, or heat
-
-
brenda
putative uncharacterized protein At1g17650; ecotype Columbia
UniProt
brenda
L., cv. Samsun NN, plants exposed to the stress factor submergence
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme GRHPR is lost in hepatocellular carcinoma (HCC) and proliferative HCC cells
brenda
additional information
immunohistochemic tissue expression analysis of GRHPR, overview. GRHPR shows a lower expression in tumor tissues than in nontumoral tissues. GRHPR is negatively correlated with Ki-67
brenda
-
the enzyme plays a critical role in the removal of the metabolic by-product glyoxylate from within the liver. Deficiency of this enzyme is the underlying cause of primary hyperoxaluria type 2 (PH2) and leads to increased urinary oxalate levels, formation of kidney stones and renal failure
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
-
brenda
glyoxylate reductase 2 is localized within the plastid, presumably in the stroma
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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 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
-
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
-
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
-
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35900
x * 35900, truncated enzyme from Escherichia coli including His-tag
36000
36287
x * 36287, calculated from the deduced amino acid sequence
38000
-
x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation
36000
-
2 * 36000, SDS-PAGE, native mass by gel filtration (native mass not given in the reference)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
?
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