Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.3.13 extracted from

  • Khan, M.W.; Murali, A.
    Modeling of alcohol oxidase enzyme of Candida boidinii and in silico analysis of competitive binding of proton ionophores and FAD with enzyme (2017), Mol. Biosyst., 13, 1754-1769 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of structure, interaction with selective proton ionophores carbonyl cyanide m-chlorophenyl hydrazone and dinitrophenol and comparison with Pleurotus eryingii aryl oxidase. The modeled structures exhibit high similarity with respect to the FAD binding sites. The adenosine part of FAD is deeply buried inside AOX while the isoalloxazine ring sticks to the surface [Candida] boidinii

Inhibitors

Inhibitors Comment Organism Structure
carbonyl cyanide m-chlorophenyl hydrazone competitive with respect to FAD [Candida] boidinii
dinitrophenol competitive with respect to FAD [Candida] boidinii

Organism

Organism UniProt Comment Textmining
[Candida] boidinii Q00922
-
-

Subunits

Subunits Comment Organism
? x * 74000, calculated from sequence [Candida] boidinii

Synonyms

Synonyms Comment Organism
AOD1
-
[Candida] boidinii

Cofactor

Cofactor Comment Organism Structure
FAD
-
[Candida] boidinii