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Information on EC 1.1.1.79 - glyoxylate reductase (NADP+)
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EC Tree
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
atgr1, atglyr1, atgr2, d-2-hydroxy-acid dehydrogenase, glyoxylate reductase (nadp+), glyoxylate reductase 1, atglyr2, 
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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
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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+
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13.9% of glyoxylate activity
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?
acetaldehyde + NADPH + H+
ethanol + NADP+
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10.4% of glyoxylate activity
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?
glyoxal + NADPH
glycol + NADP+
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isoenzyme 1, 16% activity of glyxoxylate
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?
hydroxypyruvate + NADH
D-glycerate + NAD+
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affinity for NADPH is lower than affinity for NADH
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?
phenylpyruvate + NAD(P)H
phenyllactate + NAD(P)+
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isoenzyme 2, 6% activity of glyoxylate
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?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
NADH much less effective than NADPH
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?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
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low activity
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?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
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low activity
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?
glycolate + NAD+
glyoxylate + NADH + H+
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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+
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?
glycolate + NADP+
glyoxylate + NADPH + H+
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r
glycolate + NADP+
glyoxylate + NADPH + H+
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?
glycolate + NADP+
glyoxylate + NAPDH + H+
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the reaction occurs only at pH 9.0
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?
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)+
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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)+
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isoenzyme 2, 16% activity with NADH
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?
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+
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affinity for NADPH is lower than affinity for NADH
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?
glyoxylate + NADH + H+
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 + 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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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
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?
glyoxylate + NADPH + H+
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+
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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+
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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
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?
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
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?
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
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?
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
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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
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additional information
?
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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
?
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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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