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Information on EC 1.1.1.26 - glyoxylate reductase and Organism(s) Homo sapiens
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1.1.1.26 glyoxylate reductaseIUBMB Comments
Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
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Word Map
- 1.1.1.26
- hyperoxalurias
- oxalate
- ph2
- stone
- nephrolithiasis
- nephrocalcinosis
- l-glycerate
-
photorespiratory
-
alanine:glyoxylate
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urolithiasis
- 4-hydroxy-2-oxoglutarate
- glyrs
- diagnostics
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
grhpr, glyoxylate reductase, glyr1, glyoxylate reductase/hydroxypyruvate reductase, glyr2, glyoxylate/hydroxypyruvate reductase, nadh-dependent glyoxylate reductase, nadh-glyoxylate reductase, glyoxylic acid reductase, succinic semialdehyde/glyoxylate reductase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycolate oxidase
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-
-
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glyoxylic acid reductase
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-
-
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NADH-dependent glyoxylate reductase
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-
-
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NADH-glyoxylate reductase
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-
-
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reductase, glyoxylate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -
SYSTEMATIC NAME
IUBMB Comments
glycolate:NAD+ oxidoreductase
Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
CAS REGISTRY NUMBER
COMMENTARY
9028-32-4
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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
NATURAL SUBSTRATE
NATURAL 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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme GRHPR is lost in hepatocellular carcinoma (HCC) and proliferative HCC cells
additional information
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
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is a key enzyme in the glyoxylate cycle
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
malfunction
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G165D
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mutation identified in patient with primary hyperoxaluria type 2, about 1.5% residual enzymic activity, enzyme is unstable upon purification
R302C
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mutation identified in patient with primary hyperoxaluria type 2, about 5.6% residual enzymic activity, enzyme is unstable upon purification
additional information
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identification of point mutations and minor deletions resulting in primary hyperoxaluria type 2
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Epicurean coli BL21 (DE3) as fusion protein from a His-tag plasmid
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
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
medicine
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identification of point mutations and minor deletions resulting in primary hyperoxaluria type 2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Giafi, C.F.; Rumsby, G.
Kinetic analysis and tissue distribution of human D-glycerate dehydrogenase/glyoxylate reductase and its relevance to the diagnosis of primary hyperoxaluria type 2
Ann. Clin. Biochem.
35
104-109
1998
Homo sapiens
Rumsby, G.; Cregeen, D.P.
Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase
Biochim. Biophys. Acta
1446
383-388
1999
Homo sapiens
Cregeen, D.P.; Williams, E.L.; Hulton, S.; Rumsby, G.
Molecular analysis of the glyoxylate reductase (GRHPR) gene and description of mutations underlying primary hyperoxaluria type 2
Hum. Mutat.
22
497
2003
Homo sapiens
Pan, Y.; Ni, R.; Deng, Q.; Huang, X.; Zhang, Y.; Lu, C.; Li, F.; Huang, D.; He, S.; Chen, B.
Glyoxylate reductase/hydroxypyruvate reductase: a novel prognostic marker for hepatocellular carcinoma patients after curative resection
Pathobiology
80
155-162
2013
Homo sapiens (Q9UBQ7), Homo sapiens
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), Homo sapiens
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