EC Number   |
General Information |
Reference |
|---|
    1.8.1.7 | drug target |
the enzymed is an important target of phenothiazinium dyes in Neospora caninum proliferation inhibition |
-, 764886 |
| 1.8.1.7 | evolution |
phylogenetic analysis demonstrated the closest evolutionary relationship between mitochondrial isoform of Liza haematocheila glutathione reductase and other fish mitochondrial isoforms of glutathione reductase |
764549 |
| 1.8.1.7 | malfunction |
cells lacking the enzyme show decreased resistance to oxidative stress (H2O2) and 2fold higher levels of reactive oxygen species and catalase activity than the wild type strain |
-, 726543 |
| 1.8.1.7 | malfunction |
deletion of isoform GR1 prevents survival due to a pollen lethal phenotype |
701018 |
| 1.8.1.7 | malfunction |
enzyme-deficient mice exhibit increased morbidity and mortality but do not exhibit a greater sensitivity to lipopolysaccharide than do wild type mice. Neutrophils of enzyme-deficient mice reveal impaired phagocytosis |
725067 |
| 1.8.1.7 | malfunction |
glutathione reductase inhibition significantly enhances cancer sensitivity to X-ray irradiation through glutathione disulfide increase |
712066 |
| 1.8.1.7 | malfunction |
in addition to a decrease in GSH and increase in GSSG, inhibition of glutathione reductase increases the ratios of NADH/NAD+ and NADPH/NADP+. Significant protein glutathionylation is observed. However, the inhibition does not affect the formation of reactive oxygen species or expression of antioxidant defense enzyme systems (glutathione reductase, glutathione peroxidase, catalase, and superoxide dismutase) |
711000 |
| 1.8.1.7 | metabolism |
gene GLR1 uses alternative start codons to generate two forms of enzyme. Translation from the first AUG codon generates the mitochondrial form incorporating a presequence necessary for import, while translation from the second AUG codon yields the cytosolic counterpart. The N-terminus of cytosolic GLR1 normally is N-acetylserine. In a GLR1-overproducing strain, unprocessed mitochondrial GLR1 with N-terminal acetylmethionine also accumulates in the cytosol. The processed mitochondrial GLR1 has three alternative N-termini, none of them acetylated. Mitochondrial GLR1 is turned over faster than the cytosolic form by a factor of about 2. The second AUG appears to be responsible for most of the cellular GLR1 |
-, 743172 |
| 1.8.1.7 | metabolism |
the enzyme is involved in glucose metabolism |
-, 726543 |
| 1.8.1.7 | physiological function |
a GLR1-deficient strain is not viable. During filamentation, nongrowing hyphal GLR1-overexpressing cells exhibit resistance against oxidants and cellular methylglyoxal is significantly decreased, which concomitantly increases expression of genes encoding energy-generating enzymes, including fructose-1,6-bisphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, and alcohol dehydrogenase (ADH1), with remarkable repression of Efg1-signaling cascades |
741997 |
