Any feedback?
Please rate this page

BRENDA support

Literature summary for 1.11.1.B10 extracted from

  • Shin, Y.; Lee, S.; Ku, M.; Kwak, M.K.; Kang, S.O.
    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 .
    View publication on PubMed


Localization Comment Organism GeneOntology No. Textmining


Organism UniProt Comment Textmining
Candida albicans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 D-ascorbate + H2O2 + 2 H+
Candida albicans D-ascorbate + D-dehydroascorbate + 2 H2O


Synonyms Comment Organism
Candida albicans


Organism Comment Expression
Candida albicans CCP1 deficiency enhances catalase-peroxidase KatG, EAPX1, and glutathione reductase GLR1 transcription down

General Information

General Information Comment Organism
physiological function D-erythroascorbate peroxidase EAPX1 deficiency causes glutathione deprivation, leading to the accumulation of methylglyoxal and reactive oxygen species, and induction of cytochrome c peroxidase CCP1. CCP1/EAPX1 double disruptants show severe growth defects due to D-erythroascorbic acid and glutathione depletion because of pyruvate overaccumulation Candida albicans