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Literature summary for 1.11.1.B10 extracted from

  • Kwak, M.K.; Song, S.H.; Ku, M.; Kang, S.O.
    Candida albicans erythroascorbate peroxidase regulates intracellular methylglyoxal and reactive oxygen species independently of D-erythroascorbic acid (2015), FEBS Lett., 589, 1863-1871 .
    View publication on PubMed
Search for more literature for 1.11.1.B10

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Candida albicans Q59X94
-
-

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

Synonyms Comment Organism
CaO19.584
-
 Candida albicans
CCP2
-
 Candida albicans
D-erythroascorbate peroxidase
-
 Candida albicans
EAPX1
-
 Candida albicans
erythroascorbate peroxidase
-
 Candida albicans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Candida albicans

Expression

Organism Comment Expression
Candida albicans expression is significantly induced in the presence of H2O2, menadione and diamide up

General Information

General Information Comment Organism
physiological function D-erythroascorbate peroxidase-deficient cells have remarkably increased intracellular reactive oxygen species and methylglyoxal independent of the intracellular D-erythroascorbate content, which leads to activation of catalase-peroxidase and cytochrome c peroxidase, resulting in defects in cell growth, viability, mitochondrial respiration, filamentation and virulence. EAPX1-deficient or EAPX1-overexpressing cells show more sensitivity or resistance against the exogenous H2O2 and menadione, respectively Candida albicans