Jump to main content
Jump to site search


Modeling of alcohol oxidase enzyme of Candida boidinii and in silico analysis of competitive binding of proton ionophores and FAD with enzyme.

Abstract

Alcohol oxidase (AOX) is an important Flavin adenine dinucleotide (FAD) dependent oxidoreductase which is responsible for converting the methanol into formaldehyde and hydrogen peroxide for the growth of methylotrophic yeast Candida boidinii. Though AOX plays a crucial role in methanol catabolism, the experimental structure of AOX from Candida boidinii has not been elucidated. This study reports the first complete in silico model of AOX from C. boidinii. This paper reports the AOX structure modeled using the threading approach, followed by structure analysis and molecular dynamics simulation. The modeled structure was compared with aryl alcohol oxidase structure (glucose-methanol-choline family member, pdbID: 3fim). Docking study was performed to analyze the interaction between AOX and its cofactor FAD. The AOX modeled structure also exhibited high similarity in respect of FAD binding sites, substrate binding sites as seen with 3fim. It was observed that adenosine part of FAD deeply buried inside AOX while isoalloxazine ring sticking to the surface. This paper also reports the interaction of selective proton ionophores (CCCP and DNP) with AOX and reports their binding sites. These proton ionophores showed competitive binding with FAD. The occupancy of FAD binding sites by proton ionophore may lead to blocking the entry of FAD and thereby disruption of AOX import in peroxisome.

Back to tab navigation

Supplementary files

Publication details

The article was received on 15 May 2017, accepted on 01 Jun 2017 and first published on 02 Jun 2017


Article type: Paper
DOI: 10.1039/C7MB00287D
Citation: Mol. BioSyst., 2017, Accepted Manuscript
  •   Request permissions

    Modeling of alcohol oxidase enzyme of Candida boidinii and in silico analysis of competitive binding of proton ionophores and FAD with enzyme.

    M. W. Khan and A. Murali, Mol. BioSyst., 2017, Accepted Manuscript , DOI: 10.1039/C7MB00287D

Search articles by author

Spotlight

Advertisements