1.1.1.26: glyoxylate reductase
This is an abbreviated version!
For detailed information about glyoxylate reductase, go to the full flat file.
Word Map on EC 1.1.1.26
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1.1.1.26
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hyperoxalurias
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oxalate
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ph2
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stone
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nephrolithiasis
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nephrocalcinosis
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l-glycerate
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photorespiratory
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alanine:glyoxylate
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urolithiasis
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4-hydroxy-2-oxoglutarate
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glyrs
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diagnostics
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medicine
- 1.1.1.26
- hyperoxalurias
- oxalate
- ph2
- stone
- nephrolithiasis
- nephrocalcinosis
- l-glycerate
-
photorespiratory
-
alanine:glyoxylate
-
urolithiasis
- 4-hydroxy-2-oxoglutarate
- glyrs
- diagnostics
- medicine
Reaction
Synonyms
GHPR, glycerate dehydrogenase, glycolate oxidase, glyoxylate reductase isoform 1, glyoxylate reductase/hydroxypyruvate reductase, glyoxylate/hydroxypyruvate reductase, glyoxylic acid reductase, GLYR1, GLYR2, GRHPR, GxrA, HPR1, NADH-dependent glyoxylate reductase, NADH-glyoxylate reductase, reductase, glyoxylate, SSO3187, succinic semialdehyde/glyoxylate reductase
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General Information on EC 1.1.1.26 - glyoxylate reductase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
the enzyme belongs to the beta-HAD (beta-hydroxyacid dehydrogenase) protein family. AtHPR2 and AtHPR3 are 45% identical to each other at the amino acid level, but only 19-25% identical to AtHPR1, the NADH-dependent form, and 8-9% identical to the AtGLYRs. None of the AtHPRs contains the active-site residues conserved in AtGLYR1 and AtGLYR2, indicating that the sites responsible for reducing glyoxylate differ greatly between the AtGLYRs and AtHPRs
malfunction
metabolism
physiological function
additional information
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
metabolism
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the enzyme is involved in the glycolate metabolism, as well as the 4-hydroxybutyrate production and the GABA shunt pathway, overview
metabolism
glyoxylate reductase/hydroxypyruvate reductase (GRHPR) is a key enzyme in the glyoxylate cycle
metabolism
HPR1 phosphomimetic variant T335D exhibits reduced NADH-dependent hydroxypyruvate reductase activity but improved NADPH-dependent activity. Complementation of the Arabidopsis HPR1 mutant by either wild-type HPR1 or HPR1 nonphosphorylatable mutant T335A fully complements the photorespiratory growth phenotype of the HPR1 mutant in ambient air, whereas HPR1 T335D-containing HPR1 mutant plants remain smaller and have lower photosynthetic CO2 assimilation rates. These phenotypes were associated with subtle perturbations in the photorespiratory cycle of HPR1 T335D-complemented HPR1 mutant rosettes compared to all other HPR1-containing lines
physiological function
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succinic semialdehyde and glyoxylate are typically generated in leaves via two distinct metabolic pathways, 4-aminobutyrate and glycolate respectively. GLYR isozymes function in the detoxification of both aldehydes during stress and contribute to redox balance, overview
physiological function
GLYR1 scavenges succinic semialdehyde and glyoxylate that escape from mitochondria and peroxisomes, respectively
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
additional information
due to the glutamate at the -1 position, GLYR1 C-terminal tripeptide, -SRE, does not function as a type 1 peroxisomal targeting signal, PTS1. GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
additional information
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due to the glutamate at the -1 position, GLYR1 C-terminal tripeptide, -SRE, does not function as a type 1 peroxisomal targeting signal, PTS1. GLYR1 is not relocalized from the cytosol to peroxisomes in response to abiotic stress
