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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Engineering
Engineering on EC 1.1.1.26 - glyoxylate reductase
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T335D
phosphomimetic variant, exhibits reduced NADH-dependent hydroxypyruvate reductase activity while showing improved NADPH-dependent activity
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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complementation of SSADH-deficient yeast with Arabidopsis thaliana GLYR1, the yeast then grows on 20 mM GABA as the sole nitrogen source and contains elevated levels of 4-hydroxybutyrate
additional information
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identification of point mutations and minor deletions resulting in primary hyperoxaluria type 2
additional information
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mutant lacking cytosolic hydroxypyruvate-metabolizing activity (HPR-1)
additional information
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construction of a E141N/Q313E mutant formate dehydrogenase which gains glyoxylate reductase activity improved through enhancement of the hydrogen transfer step in the catalytic process, while the replacement induces no marked activity toward other 2-koxoacid substrates, and diminishes the enzyme's activity as to formate oxidation, substrate specificity and kinetic switch of the mutant, overview