EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.79 | expression of His-tagged wild-type and mutant enzymes in Escherichia coli | Homo sapiens |
1.1.1.81 | expression of His-tagged wild-type and mutant enzymes in Escherichia coli | Homo sapiens |
1.1.1.81 | gene GRHPR, localization of chromosome 9q12, DNA and amino acid sequence determination and analysis, genetic structure and promoter analysis, expression analysis, expression as GFP-fusion protein in the cytosol of HEK293 cells, co-expression with PPARalpha in HepG2 cells and regulation, overview | Mus musculus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.79 | 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 | Homo sapiens |
1.1.1.79 | 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 | Homo sapiens |
1.1.1.81 | 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 | Mus musculus |
1.1.1.81 | 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 | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.79 | G160R | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Homo sapiens |
1.1.1.79 | G165D | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Homo sapiens |
1.1.1.79 | M322R | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Homo sapiens |
1.1.1.79 | R302C | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Homo sapiens |
1.1.1.81 | G160R | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Mus musculus |
1.1.1.81 | G160R | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Homo sapiens |
1.1.1.81 | G165D | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Mus musculus |
1.1.1.81 | G165D | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Homo sapiens |
1.1.1.81 | M322R | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Mus musculus |
1.1.1.81 | M322R | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Homo sapiens |
1.1.1.81 | R302C | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Mus musculus |
1.1.1.81 | R302C | site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.79 | D-glycerate | the enzyme shows product inhibition | Homo sapiens | |
1.1.1.81 | D-glycerate | the enzyme shows product inhibition | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.1.81 | cytosol | - |
Mus musculus | 5829 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.79 | glyoxylate + NAD(P)H | Homo sapiens | the enzyme is involved in removal of the metabolic by-product from liver | glycolate + NAD(P)+ | - |
? | |
1.1.1.79 | hydroxypyruvate + NAD(P)H | Homo sapiens | - |
D-glycerate + NAD(P)+ + H+ | - |
? | |
1.1.1.79 | additional information | Homo sapiens | enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure | ? | - |
? | |
1.1.1.81 | glyoxylate + NAD(P)H | Mus musculus | - |
glycolate + NAD(P)+ | - |
? | |
1.1.1.81 | glyoxylate + NAD(P)H | Homo sapiens | the enzyme is involved in removal of the metabolic by-product from liver | glycolate + NAD(P)+ | - |
? | |
1.1.1.81 | hydroxypyruvate + NAD(P)H | Mus musculus | - |
D-glycerate + NAD(P)+ + H+ | - |
? | |
1.1.1.81 | hydroxypyruvate + NAD(P)H | Homo sapiens | - |
D-glycerate + NAD(P)+ + H+ | - |
? | |
1.1.1.81 | additional information | Homo sapiens | enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure | ? | - |
? | |
1.1.1.81 | additional information | Mus musculus | the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.79 | Homo sapiens | - |
- |
- |
1.1.1.81 | Homo sapiens | - |
- |
- |
1.1.1.81 | Mus musculus | - |
gene GRHPR | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.79 | recombinant enzyme | Homo sapiens |
1.1.1.79 | 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 | Homo sapiens |
1.1.1.81 | 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 | Mus musculus |
1.1.1.81 | 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 | Homo sapiens |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.1.1.79 | liver | - |
Homo sapiens | - |
1.1.1.79 | liver | 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 | Homo sapiens | - |
1.1.1.81 | kidney | - |
Mus musculus | - |
1.1.1.81 | liver | - |
Mus musculus | - |
1.1.1.81 | liver | - |
Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.79 | glyoxylate + NAD(P)H | - |
Homo sapiens | glycolate + NAD(P)+ | - |
? | |
1.1.1.79 | glyoxylate + NAD(P)H | the enzyme is involved in removal of the metabolic by-product from liver | Homo sapiens | glycolate + NAD(P)+ | - |
? | |
1.1.1.79 | hydroxypyruvate + NAD(P)H | - |
Homo sapiens | D-glycerate + NAD(P)+ + H+ | - |
? | |
1.1.1.79 | additional information | enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure | Homo sapiens | ? | - |
? | |
1.1.1.79 | additional information | structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview | Homo sapiens | ? | - |
? | |
1.1.1.81 | glyoxylate + NAD(P)H | - |
Mus musculus | glycolate + NAD(P)+ | - |
? | |
1.1.1.81 | glyoxylate + NAD(P)H | - |
Homo sapiens | glycolate + NAD(P)+ | - |
? | |
1.1.1.81 | glyoxylate + NAD(P)H | the enzyme is involved in removal of the metabolic by-product from liver | Homo sapiens | glycolate + NAD(P)+ | - |
? | |
1.1.1.81 | hydroxypyruvate + NAD(P)H | - |
Mus musculus | D-glycerate + NAD(P)+ + H+ | - |
? | |
1.1.1.81 | hydroxypyruvate + NAD(P)H | - |
Homo sapiens | D-glycerate + NAD(P)+ + H+ | - |
? | |
1.1.1.81 | additional information | enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure | Homo sapiens | ? | - |
? | |
1.1.1.81 | additional information | the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview | Mus musculus | ? | - |
? | |
1.1.1.81 | additional information | structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.79 | D-2-hydroxy-acid dehydrogenase | - |
Homo sapiens |
1.1.1.79 | glyoxylate reductase/hydroxypyruvate reductase | - |
Homo sapiens |
1.1.1.79 | GRHPR | - |
Homo sapiens |
1.1.1.79 | More | the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81 | Homo sapiens |
1.1.1.81 | D-2-hydroxy-acid dehydrogenase | - |
Homo sapiens |
1.1.1.81 | glyoxylate reductase/hydroxypyruvate reductase | - |
Mus musculus |
1.1.1.81 | glyoxylate reductase/hydroxypyruvate reductase | - |
Homo sapiens |
1.1.1.81 | GRHPR | - |
Mus musculus |
1.1.1.81 | GRHPR | - |
Homo sapiens |
1.1.1.81 | More | the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81 | Mus musculus |
1.1.1.81 | More | the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81 | Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.79 | 7.5 | - |
assay at | Homo sapiens |
1.1.1.81 | 7.5 | - |
assay at | Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.79 | NADH | - |
Homo sapiens | |
1.1.1.79 | NADPH | - |
Homo sapiens | |
1.1.1.79 | NADPH | binding structure | Homo sapiens | |
1.1.1.81 | NADH | - |
Mus musculus | |
1.1.1.81 | NADH | - |
Homo sapiens | |
1.1.1.81 | NADPH | - |
Mus musculus | |
1.1.1.81 | NADPH | binding structure | Homo sapiens |