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 .

Search for more literature for 1.11.1.B10

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

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

Synonyms	Comment	Organism
EAPX1	-	Candida albicans

Expression

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

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Release 2023.1 (January 2023)