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Literature summary for 1.14.14.154 extracted from

  • Alvarez-Rueda, N.; Fleury, A.; Loge, C.; Pagniez, F.; Robert, E.; Morio, F.; Le Pape, P.
    The amino acid substitution N136Y in Candida albicans sterol 14alpha-demethylase is involved in fluconazole resistance (2016), Med. Mycol., 54, 764-775 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutant and wild-type enzymes in Pichia pastoris Candida albicans

Protein Variants

Protein Variants Comment Organism
N136Y N136Y transformants show a reduced in vitro susceptibility to fluconazole compared to wild-type controls. The amino acid substitution N136Y in Candida albicans sterol 14alpha-demethylase is involved in fluconazole resistance Candida albicans

Inhibitors

Inhibitors Comment Organism Structure
fluconazole N136Y transformants show a reduced in vitro susceptibility to fluconazole compared to wild-type controls. The amino acid substitution N136Y in Candida albicans sterol 14alpha-demethylase is involved in fluconazole resistance Candida albicans

Organism

Organism UniProt Comment Textmining
Candida albicans C8XRD8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lanosterol + [reduced NADPH-hemoprotein reductase] + O2
-
Candida albicans ?
-
?

Synonyms

Synonyms Comment Organism
ERG11
-
Candida albicans

Cofactor

Cofactor Comment Organism Structure
NADPH-hemoprotein reductase A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._ Candida albicans