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Literature summary for 1.11.1.5 extracted from
- Cytochrome c peroxidase regulates intracellular reactive oxygen species and methylglyoxal via enzyme activities of erythroascorbate peroxidase and glutathione-related enzymes in Candida albicans (2017), Int. J. Biochem. Cell Biol., 92, 183-201 .
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Candida albicans | 5739 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Candida albicans | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CCP1 | - |
Candida albicans |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | CCP1 does not affect cell respiration under cyanide treatment, but predominantly detoxifies H2O2 by glutathione. CCP1 deficiency stimulates superoxide dismutase and alcohol dehydrogenase Adh1 activity and enhances catalase-peroxidase KatG, erythroascorbate peroxidase EAPX1, and glutathione reductase GLR1 transcription by decreasing glutathione and D-erythroascorbic acid and increasing pyruvate. The CCP1-deficient mutant maintains steady-state levels of methylglyoxal. CCP1/EAPX1 double disruptants show severe growth defects due to the D-erythroascorbic acid and glutathione depletion because of pyruvate overaccumulation. CCP1-deficient and CCP1/EAPX1 double-knockout mutants show more hyphal growth than the wild-type | Candida albicans |
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