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Literature summary for 1.1.1.81 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)

Cloned (Comment) Organism
expression of His-tagged wild-type and mutant enzymes in Escherichia coli Homo sapiens
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)

Crystallization (Comment) Organism
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
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

Protein Variants Comment Organism
G160R site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Mus musculus
G160R site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Homo sapiens
G165D site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Mus musculus
G165D site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Homo sapiens
M322R site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Mus musculus
M322R site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Homo sapiens
R302C site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Mus musculus
R302C site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
D-glycerate the enzyme shows product inhibition Homo sapiens

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glyoxylate + NAD(P)H Mus musculus
-
glycolate + NAD(P)+
-
?
glyoxylate + NAD(P)H Homo sapiens the enzyme is involved in removal of the metabolic by-product from liver glycolate + NAD(P)+
-
?
hydroxypyruvate + NAD(P)H Mus musculus
-
D-glycerate + NAD(P)+ + H+
-
?
hydroxypyruvate + NAD(P)H Homo sapiens
-
D-glycerate + NAD(P)+ + H+
-
?
additional information Homo sapiens enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure ?
-
?
additional information Mus musculus the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
gene GRHPR
-

Purification (Commentary)

Purification (Comment) Organism
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
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

Source Tissue Comment Organism Textmining
kidney
-
Mus musculus
-
liver
-
Mus musculus
-
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glyoxylate + NAD(P)H
-
Mus musculus glycolate + NAD(P)+
-
?
glyoxylate + NAD(P)H
-
Homo sapiens glycolate + NAD(P)+
-
?
glyoxylate + NAD(P)H the enzyme is involved in removal of the metabolic by-product from liver Homo sapiens glycolate + NAD(P)+
-
?
hydroxypyruvate + NAD(P)H
-
Mus musculus D-glycerate + NAD(P)+ + H+
-
?
hydroxypyruvate + NAD(P)H
-
Homo sapiens D-glycerate + NAD(P)+ + H+
-
?
additional information enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure Homo sapiens ?
-
?
additional information the enzyme is transcriptionally regulated by the peroxisome proliferator-activated receptor alpha, PPARalpha, in liver, overview Mus musculus ?
-
?
additional information structural basis of enzyme substrate specificity, active site structure and substrate binding, no activity with pyruvate, overview Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
D-2-hydroxy-acid dehydrogenase
-
Homo sapiens
glyoxylate reductase/hydroxypyruvate reductase
-
Mus musculus
glyoxylate reductase/hydroxypyruvate reductase
-
Homo sapiens
GRHPR
-
Mus musculus
GRHPR
-
Homo sapiens
More the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81 Mus musculus
More the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADH
-
Mus musculus
NADH
-
Homo sapiens
NADPH
-
Mus musculus
NADPH binding structure Homo sapiens