EC Number   |
General Information |
Reference |
|---|
   1.11.1.5 | more |
structural features that are important for accelerating cyanide binding are also important for accelerating the rate of hydrogen peroxide binding to the heme iron |
724463 |
| 1.11.1.5 | more |
the catalytic mechanism of H2O2 reduction involves formation of CcP Compound I (CpdI), an intermediate oxidized 2 equiv above the CcP Fe(III) resting state and containing Fe(IV)=O heme oxyferryl and W191 cation radical. Subsequent CpdI reduction occurs in two one-electron steps, involving complex formation with ferrous Cc, intermolecular electron transfer (ET), and product dissociation |
724372 |
| 1.11.1.5 | physiological function |
bacterial di-heme cytochrome c peroxidases (CcpAs) protect the cell from reactive oxygen species by reducing hydrogen peroxide to water |
705165 |
| 1.11.1.5 | physiological function |
CcP catalyzes reduction of hydroperoxides using the electrons provided by its physiological binding partner cytochrome c |
724372 |
| 1.11.1.5 | 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 |
742669 |
| 1.11.1.5 | physiological function |
cytochrome c peroxidase is a mitochondrial heme-based H2O2 sensor that modulates antioxidant defense. The enzyme in intermembrane space functions primarily as a mitochondrial H2O2 sensing and signaling protein in yeast cells. Ccp1 H2O2 sensing and signaling regulate Sod2 activity to control superoxide levels. Respiration-derived H2O2 is removed principally by mitochondrial catalase Cta1, which is regulated in a H2O2-dependent manner by Ccp1, overview |
-, 725070 |
| 1.11.1.5 | physiological function |
disruption of the cytochrome c peroxidase gene causes a decrease of the membrane NADH peroxidase activity, impairs the resistance of growing culture to exogenous hydrogen peroxide and hampers aerobic growth. The mutation does not affect the activity or oxygen affinity of the respiratory chain, or the kinetics of cytochrome d reduction. Cytochrome c peroxidase does not terminate the cytochrome bc1 branch of Zymomonas mobilis |
-, 743248 |
| 1.11.1.5 | physiological function |
electron transfer |
702250 |
| 1.11.1.5 | physiological function |
increased copy number of CCP1 on chromosome XI activates respiratory metabolism and decreases pyruvate levels in an aneuploid sake yeast |
-, 765121 |
| 1.11.1.5 | physiological function |
involvement of ZmCytC in the aerobic respiratory chain via the cytochrome bc1 complex in addition to the previously proposed direct interaction with ubiquinol and its contribution to protection against oxidative stress |
725756 |
