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Enzyme Nomenclature
Information on EC 1.1.1.79 - glyoxylate reductase (NADP+)
Word Map on EC 1.1.1.79
- 1.1.1.79
- hyperoxalurias
- ph2
- oxalate
- renal
- stone
- calcium
- nephrocalcinosis
-
nephrolithiasis
- l-glycerate
-
monogenic
-
alanine:glyoxylate
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.1.79
-
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RECOMMENDED NAME
GeneOntology No.
glyoxylate reductase (NADP+)
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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+
-
-
-
-
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
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia; putative uncharacterized protein At1g17650; ecotype Columbia
UniProt
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency; (L.) Heynh
SwissProt
enzyme also displays 4-hydroxybutyrate dehydrogenase (EC1.1.1.61) activity but with less efficiency; L. Heynh
SwissProt
L. Heynh ecotype Columbia, plants exposed to the stress factors drought, salinity, submergence, cold, or heat
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family; 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; 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; 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
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
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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
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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 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
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malfunction
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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
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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
-
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; upregulation of glyoxylate reductase/hydroxypyruvate reductase is associated with intestinal epithelial cells apoptosis in trinitrobenzenesulfonic acid-induced colitis
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
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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
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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
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additional information
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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
residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
additional information
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residues Leu53 and Trp138 act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Substrate optimum position within the catalytic pocket is raised thought interactions with catalytic residues His288, Arg241, Val76, and Gly77, catalytic mechanism modelling, overview
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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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
-
?
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
-
-
?
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+
-
low activity
-
-
?
2-oxoisocaproate + NADPH + H+
2-hydroxy-4-methylpentanoate + NADP+
-
low activity
-
-
?
glycolate + NADP+
glyoxylate + NADPH + H+
-
-
-
r
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)+
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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
-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
-
7% of activity with glyoxylate
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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
-
-
?
glyoxylate + NADH + H+
glycolate + NAD+
NADH much less effective than NADPH
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-
ir
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+
-
-
-
r
glyoxylate + NADPH + H+
glycolate + NADP+
preferred substrate
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
detoxification of glyoxylate during stress
-
-
ir
glyoxylate + NADPH + H+
glycolate + NADP+
-
glyoxylate highly preferred over succinic semialdehyde as substrate
-
-
?
glyoxylate + NADPH + H+
glycolate + NADP+
glyoxylate reductase 2 has a 350fold higher preference for glyoxylate than for succinic semialdehyde
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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
-
-
ir
hydroxypyruvate + NAD(P)H
glycerate + NAD(P)+
-
25 mM hydroxypyruvate, 68% of the activity with glyoxylate, 2.5 mM hydroxypyruvate, isoenzyme 2, 332% of the activity of glyoxylate
-
?
hydroxypyruvate + NAD(P)H
glycerate + NAD(P)+
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isoenzyme 1, hydroxypyruvate shows 15% of the activity of glyoxylate
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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+
-
28.6% of glyoxylate activity
-
?
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+
-
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
at least under oxygen deficient and high light conditions
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
detoxification of succinic semialdehyde during stress
-
-
r
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
reverse reaction less efficient than forward reaction
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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
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
the affinity for succinic semialdehyde is 10fold lower for isoform GLYR2 than that for isoform GLYR1
-
-
ir
additional information
?
-
-
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
?
-
glyoxylate reductase 2 is ineffective in catalysing the reverse reaction utilizing either glycolate or 6-phosphogluconate
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-
-
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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-
-
additional information
?
-
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
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-
-
additional information
?
-
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
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 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
?
-
-
enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
-
-
-
additional information
?
-
-
structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview
-
-
-
additional information
?
-
the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate
-
-
-
additional information
?
-
-
the enzyme is highly specific for glyoxylate, it shows no detectable activity with 4-methyl-2-oxopentanoate, phenylglyoxylate, pyruvate, oxaloacetate, and alpha-ketoglutarate
-
-
-
additional information
?
-
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
glycolate + NADP+
glyoxylate + NADPH + H+
A0A178WMD4, F4I907, Q9CA90
-
-
-
r
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 + 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+
F4I907, Q9LSV0
detoxification of glyoxylate during stress
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
-
at least under oxygen deficient and high light conditions
-
-
ir
succinic semialdehyde + NADPH + H+
4-hydroxybutyrate + NADP+
F4I907, Q9LSV0
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
?
-
A0A178WMD4
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
?
-
F4I907
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
Q9CA90
HPR3 prefers NADPH over NADH and converts glyoxylate to glycolate, the purified recombinant HPR3 shows similar activity with hydroxypyruvate and glyoxylate
-
-
-
additional information
?
-
A0A178WMD4
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
?
-
F4I907
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
?
-
Q9CA90
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
?
-
A0A178WMD4
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
?
-
F4I907
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
?
-
Q9CA90
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
?
-
A0A178WMD4
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
?
-
F4I907
the recombinant AtHPR2 prefers NADPH over NADH but utilizes hydroxypyruvate and glyoxylate similarly
-
-
-
additional information
?
-
Q9CA90
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
?
-
Q8U3Y2
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
?
-
F8AEA4
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
?
-
F8AEA4
a bifunctional enzyme, that also performs the reaction of hydroxypyruvate reductase, EC 1.1.1.81, mechanism of substrates trafficking in glyoxylate/hydroxypyruvate reductase, catalytic mechanism modelling, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
NADH
much less effective than NADPH; much less effective than NADPH
NADPH
-
enzyme has a higher affinity for NADPH than for NADH when incubated without substrate
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
-
preferred cofactor, NADH gives only 4% of the activity with NADPH
additional information
recombinant AtGLYR1 prefers NADPH over NADH; recombinant AtGLYR2 prefers NADPH over NADH; recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
-
recombinant AtGLYR1 prefers NADPH over NADH; recombinant AtGLYR2 prefers NADPH over NADH; recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH; recombinant AtGLYR2 prefers NADPH over NADH; recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
additional information
recombinant AtGLYR1 prefers NADPH over NADH; recombinant AtGLYR2 prefers NADPH over NADH; recombinant HPR3 prefers NADPH over NADH; the recombinant AtHPR2 prefers NADPH over NADH
-
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
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
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxybutyrate
mixed type inhibition with NADPH; mixed type inhibition with succinic semialdehyde
iodoacetate
-
isoenzyme 2, 1 mM, 97% inhibition, isoenzyme 1, 1 mM, 18% inhibition
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
-
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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.
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
0.033
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; with as NADPH as cofactor, pH 7.6, 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
0.088
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
0.181
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
0.24
glyoxylate
-
37°C, cofactor: NADPH; pH 7.5, 37°C, recombinant enzyme, with NADPH
0.5
glyoxylate
-
pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme
1
glyoxylate
-
37°C, cofactor: NADH; pH 7.5, 37°C, recombinant enzyme, with NADH
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
4.6
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
0.058
Hydroxypyruvate
-
37°C, cofactor: NAPDH; pH 7.5, 37°C, recombinant enzyme, with NADPH
0.19
Hydroxypyruvate
-
37°C, cofactor: NADH; pH 7.5, 37°C, recombinant enzyme, with NADH
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
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C; with succinic semialdehyde as substrate, pH 7.6, 30°C
0.0014
NADPH
recombinant enzyme, using glyoxylate as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C; with glyoxylate as substrate, pH 7.6, 30°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
0.002
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
0.0027
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A
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
0.0648
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
8.96
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C; with as NADPH as cofactor, pH 7.6, 30°C
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics; 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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
Succinic semialdehyde
recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C; with as NADPH as cofactor, pH 7.6, 30°C
0.0052
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E
0.051
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R
6.06
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
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; with as NADPH as cofactor, pH 7.6, 30°C
27
glyoxylate
-
37°C, cofactor: NADPH; pH 7.5, 37°C, recombinant enzyme, with NADPH
54.6
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme
67
glyoxylate
-
37°C, cofactor: NADH; pH 7.5, 37°C, recombinant enzyme, with NADH
67.8
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
86.4
glyoxylate
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A
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
38
Hydroxypyruvate
-
37°C, cofactor: NAPDH; pH 7.5, 37°C, recombinant enzyme, with NADPH
65
Hydroxypyruvate
-
37°C, cofactor: NADH; pH 7.5, 37°C, recombinant enzyme, with NADH
22000
NADH
-
pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme
9.09
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A
9.56
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
recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C; with succinic semialdehyde as substrate, pH 7.6, 30°C
12
NADPH
recombinant enzyme, using glyoxylate as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C; with glyoxylate as substrate, pH 7.6, 30°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
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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
779
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A
4340
NADPH
pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A
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
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.45 - 0.7
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
7.5
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
50
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme GRHPR is lost in hepatocellular carcinoma (HCC) and proliferative HCC cells
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
-
; 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
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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
-
glyoxylate reductase 2 is localized within the plastid, presumably in the stroma; stroma
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus yayanosii (strain CH1 / JCM 16557)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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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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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 35900, truncated enzyme from Escherichia coli including His-tag; x * 36287, calculated from the deduced amino acid sequence
dimer
homodimer
2 * 35898, sequence calculation, 2 * 42000, SDS-PAGE, recombinant enzyme
additional information
dimer
-
x * 38000, SDS-PAGE, native mass by analytical ultracentrifugation
dimer
-
2 * 36000, SDS-PAGE, native mass by gel filtration (native mass not given in the reference)
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
-
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
domain I, with the dinucleotide binding region, comprises residues 1-165 in the N-terminus. This typical Rossmann fold domain contains two alpha/beta units: a six-stranded parallel beta-sheet (beta1-beta6a) covered by four helices (alpha1-alpha5) and followed by a mixed three-stranded beta-sheet (beta6b-beta8) covered by two helices (alpha6 and alpha7). Domain II (residues 195-287) consists of only helices (alpha8-alpha13) from the C-terminal segment of the protein. The two domains are connected by a long alpha-helix, alpha8 (residues 166-194). Enzyme domain structure analysis, overview
additional information
the overall structure of the apo-enzyme monomer adopts the typical D-2-hydroxy-aciddehydrogenase fold with a closed conformation, which comprises two alpha/beta/alpha domains, structure analysis, overview
additional information
-
the overall structure of the apo-enzyme monomer adopts the typical D-2-hydroxy-aciddehydrogenase fold with a closed conformation, which comprises two alpha/beta/alpha domains, structure analysis, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified apo-enzyme, sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution containing 0.2 M calcium acetate hydrate, 20% PEG 3350, pH 6.5, 20°C, 6 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using a previously unrecognized member of the beta-HAD family, cytokine-like nuclear factor, structure
purified detagged recombinant enzyme in ternary complex with product D-glycerate and cofactor NADPH, sitting drop vapour diffusion method, 5.5 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 1 mM 2-mercaptoethanol, 0.2 mM NADPH, and 0.5 mm di-sodium oxalate, mixed with mother liquor, containing 15% w/v PEG 8000, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate, pH 6.5, to 0.002 ml drops, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution; sitting-drop vapour-diffusipon method. Crystal structure at 2.2 Å resolution. There are four copies of GRHPR in the crystallographic asymmetric unit: in each homodimer, one subunit forms a ternary (enzyme/NADPH/reduced substrate) complex, and the other a binary (enzyme/NADPH) form. The spatial arrangement of the two enzyme domains is the same in binary and ternary forms
-
purified recombinant enzyme, sitting drop vapour diffusion method, the reservoir solution contains 0.1 M MES buffer, pH 6.5, 0.01 M cobalt (II) chloride, and 1.8 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis at 1.75 A resolution
purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, hanging drop vapour diffusion method, from a mother liquor containing 100 mM sodium acetate, pH 5.2, 15% PEG 400, and 100 mM NaCl, 20°C, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution
analysis of the three-dimensional crystal structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR
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sitting drop vapor diffusion method in the presence of NAD, crystal structure analysis reveals tightly bound NADP(H) at the enzyme originating from Escherichia coli expression, which is not replaceable by NAD
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purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, sitting drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein solution with 0.0015 ml of mother liquor containing 1.7 malonate, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 1.4 A-2.0 A resolution, molecular replacement using the three-dimensional structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 10
recombinant enzyme, 30°C, 1 h, more than 80% of activity is retained
740392
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
70
80
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complete loss of activity within 10 min when incubates above 80°C
40
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isoenzyme 2, 90% loss of activity after 5 min, 20% glycerol protects from inactivation, enzyme retains 65% of its activity after 5 min at 40°C
40
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isoenzyme 1, 20% loss of activity after 5 min, complete inactivation above 50°C
50
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60% loss of activity after 10 min, activity is completely lost above 60°C
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diethylene glycol
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half-life in the presence of 25% diethylene glycol significantly longer than that in the absence of an organic solvent
dimethyl sulfoxide
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half-life in the presence of 25% dimethyl sulfoxide significantly longer than that in the absence of an organic solvent
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, concentrated protein eluate from the affinity column, for months, enzyme activity is reasonably stable
4°C, alkaline pH, no loss of activity after 1 week, at pH 7-11, 20% loss of activity
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4°C, concentrated protein eluate from the affinity column, for hours, enzyme activity is reasonably stable
4°C, diluted enzyme, storage during assays, activity starts to decrease within 30 min
isoenzyme 1, 4°C, 10 mM potassium phosphate, pH 7.0, 1 week, 20% loss of activity
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isoenzyme 2, 4°C, 10 mM, potassium phosphate, pH 7.0, 20% glycerol, 1 week, 10% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ethanol precipitation, DEAE-cellulose, CM-cellulose, affinity chromatography
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isoenzyme 1, protamine sulfate, DEAE-cellulose, hydroxylapatite, Sephadex G-150, DEAE-cellulose, hydroxylapatite
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isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxyapatite, Sephadex G-150, phosphocellulose
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isoenzyme 2, protamine sulfate, DEAE-cellulose, hydroxylapatite, Sephadex G-150, DEAE-cellulose, phospho-cellulose
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nickel affinity column chromatography; recombinant truncated protein using His-tag
recombinant C-terminally His9-tagged enzyme from Escherichia coli by nickel affinity chromatography to homogeneity
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recombinant enzyme; recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography, the His-tag is cleaved by thrombin followed by gel filtration, over 95% purity
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recombinant His-tagged enzyme 2.7fold from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His6-tagged truncated mutant enzyme from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography; recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 pLysS by precipitation with 10% PEG 8000, and nickel affinity chromatography
recombinant protein from Escherichia coli
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
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recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)-RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, ultrafiltration, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
exclusive localization in the cytosol of transgenic Arabidopsis plants co-expressing GFP-GLYR1 and and Cherry-PTS1, a fusion protein consisting of the Cherry fluorescent protein linked to the PTS1 of the peroxisomal enzyme hydroxypyruvate reductase. Expression of N-terminal GFP-tagged or Myc-tagged GLYR1 in tobacco BY-2 cell cytosol. GFP- or Myc-tagged GLYR1 is competent, at least partially, for import into peroxisomes, since replacement of the C-terminal glutamate in GLYR1 with leucine, which yields a canonical PTS1 (i.e., a C-terminal small-basic-hydrophobic tripeptide motif), results in the modified fusion protein (GFPGLYR1-E to L and Myc-GLYR1-E to L) being dual localized to the cytosol and peroxisomes in BY-2 cells
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expressed as GFP-fusion protein in tobacco BY-2 cells; expressed as GFP-fusion protein in tobacco BY-2 cells; expressed as His-tag fusion protein in E. coli BL-21(DE3) Rosetta (pLysS), full-length and truncated GR2 sequences introduced into Escherichia coli, only the recombinant truncated GR2 is soluble, expression markedly improved by co-expression of the GroES/GroEL chaperone; expressed in Escherichia coli BL-21(DE3) Rosetta (pLysS) cells and in Nicotiana tabacum BY-2 cells
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL and Escherichia coli B834(DE3)pRARE
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gene GLYR1, sequence comparisons of GLYR genes and HPR genes; gene GLYR1, sequence comparisons of GLYR genes and HPR genes, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 pLysS; gene GLYR2, sequence comparisons of GLYR genes and HPR genes, recombinant expression of a His6-tagged truncated AtGLYR2 cDNA sequence, lacking the N-terminal 58 amino acids, in Escherichia coli strain BL21 pLysS
gene PtGR, DNa and mino acid seuence determination and analysis, sequence comparisons, recombinant expresssion of His-tagged enzyme in Escherichia coli strain BL21
ORF YNL274c, DNA and amino acid sequence determination and analysis, expression in yeast strains, overview
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recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL
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recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)-RIL
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
upregulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) by trinitrobenzenesulphonic acid, which induces experimental colitis and intestinal epithelial cell apoptosis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA1-43
in contrast to the full length sequence yields a soluble protein when expressed in Escherichia coli
K170A
site-directed mutagenesis, catalytically inactive mutant
K170E
site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type
K170H
site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type
K170R
site-directed mutagenesis, the mutant shows highly reduced kcat for glyoxylate compared to the wild-type
R31L/T32K/K35D/C68R
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site-directed mutagenesis of Rosmann fold (c.2.1.6) residues leading to a switch of cofactor preference of the enzyme from NADP(H) to NAD(H), altered cofactor kinetics of the mutant enzyme R31L/T32K/ K35D/C68R compared to the wild-type, overview
G160R
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G165D
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
M322R
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
R302C
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site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
additional information
additional information
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invertion of the cofactor specificity of the NADP+-dependent enzyme glyoxylate reductase by a structure-guided, semirational strategy, overview. The heuristic-based approach leverages the diversity and sensitivity of catalytically productive cofactor binding geometries to limit the problem to an experimentally tractable scale. Experimental validation of the CSR-SALAD method for switching cofactor preference to NAD while retaining catalytic activity
additional information
constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR)
additional information
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constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR)
additional information
constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR)
additional information
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constructin of various recombinant GRHPR enzymes arising from Pyrococcus furiosus (PfuGRHPR), Pyrococcus horikoshii (PhoGRHPR), and Pyrococcus yayanosii (PyaGRHPR)
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additional information
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deletion of the glyoxylate reductase-encoding gene leads to higher biomass concentration after diauxic shift, overview
additional information
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deletion of the glyoxylate reductase-encoding gene leads to higher biomass concentration after diauxic shift, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
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enzyme glyoxylate reductase/hydroxypyruvate reductase is a prognostic marker for hepatocellular carcinoma patients after curative resection. Patients with negative GRHPR both in tumor tissues and nontumoral tissues have a significantly shorter survival time than those with positive GRHPR. Multivariate analysis establishes that GRHPR is detected in nontumoral tissues as an independent prognostic factor for patients with hepatocellular carcinoma, overview
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.79)
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