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Information on EC 1.1.1.81 - hydroxypyruvate reductase and Organism(s) Homo sapiens

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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hydroxypyruvate reductase, nadh-hpr, athpr1, nadph-dependent hydroxypyruvate reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-hydroxypyruvate reductase
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D-2-hydroxy-acid dehydrogenase
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D-glycerate dehydrogenase
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glyoxylate reductase/hydroxypyruvate reductase
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GRHPR
NADH:hydroxypyruvate reductase
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additional information
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the enzyme shows bifunctionality also performing the reaction of hydroxypyruvate reductase, EC 1.1.1.81
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
D-glycerate:NADP+ 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9059-44-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
show the reaction diagram
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-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glycerate + NAD+
hydroxypyruvate + NADH + H+
show the reaction diagram
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-
?
glyoxylate + NAD(P)H
glycolate + NAD(P)+
show the reaction diagram
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the enzyme is involved in removal of the metabolic by-product from liver
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?
hydroxypyruvate + NAD(P)H
D-glycerate + NAD(P)+ + H+
show the reaction diagram
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?
additional information
?
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enzyme deficiency leads to primary hyperoxaluria type 2 with increased urinary oxalate levels, formation of kidney stones, and renal failure
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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NADPH
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binding structure
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glycerate
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the enzyme shows product inhibition
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
upregulation of glyoxylate reductase/hydroxypyruvate reductase is associated with intestinal epithelial cells apoptosis in trinitrobenzenesulfonic acid-induced colitis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GRHPR_HUMAN
328
0
35668
Swiss-Prot
Mitochondrion (Reliability: 3)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Booth, M.P.; Conners, R.; Rumsby, G.; Brady, R.L.
Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase
J. Mol. Biol.
360
178-189
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Zong, C.; Nie, X.; Zhang, D.; Ji, Q.; Qin, Y.; Wang, L.; Jiang, D.; Gong, C.; Liu, Y.; Zhou, G.
Up regulation of glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is associated with intestinal epithelial cells apoptosis in TNBS-induced experimental colitis
Pathol. Res. Pract.
212
365-371
2016
Homo sapiens (Q9UBQ7)
Manually annotated by BRENDA team