Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of enzyme disruption mutant DELTAccp1, SOD2 activity is significantly lower in W191F ccp1 mutant cells than in DELTAccp1 deletion mutant cells | Saccharomyces cerevisiae |
W191F | catalytically inactive mature Ccp1 mutant, Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1 | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrial intermembrane space | - |
Saccharomyces cerevisiae | 5758 | - |
mitochondrion | Ccp1 | Saccharomyces cerevisiae | 5739 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Saccharomyces cerevisiae BY4741 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme partially by preparation of mitochondria | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
CCP1 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
malfunction | significantly higher H2O2 accumulation in ccp1-null cells and catalytically inactive Ccp1W191F mutant cells. Ccp1W191F is a more persistent H2O2 signaling protein than wild-type Ccp1 | Saccharomyces cerevisiae |
additional information | resting ferric (FeIII) Ccp1III is oxidized by H2O2 to compound I,which has a FeIV heme and a cation radical on residue W191. Compound I reacts with ferrous (FeII) Cyc1II to form compound II with a FeIV heme but no W191 radical. Reaction with a second Cyc1II reduces the FeIV heme to yield resting Ccp1III. The Ccp1W191F variant rapidly reacts with H2O2 but is very slowly reduced by Cyc1II such that it exhibits negligible Cyc1II-oxidizing activity, reaction mechanism, overview | Saccharomyces cerevisiae |
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 | Saccharomyces cerevisiae |