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Literature summary extracted from

  • Booth, M.P.; Conners, R.; Rumsby, G.; Brady, R.L.
    Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase (2006), J. Mol. Biol., 360, 178-189.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

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

Inhibitors

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.81 cytosol
-
Mus musculus 5829
-

Natural Substrates/ Products (Substrates)

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 ?
-
?

Organism

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
-

Purification (Commentary)

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

Source Tissue

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
-

Substrates and Products (Substrate)

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 ?
-
?

Synonyms

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

pH Optimum

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

Cofactor

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