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Literature summary 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)

EC Number Crystallization (Comment) Organism
1.1.3.13 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

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.13 [Candida] boidinii Q00922
-
-

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.1.3.13 AOD1
-
 [Candida] boidinii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.13 FAD
-
 [Candida] boidinii