REVIEW: Quinone-Dependent Alcohol Dehydrogenases and FAD-Dependent Alcohol Oxidases

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A. R. Gvozdev¹, I. A. Tukhvatullin², and R. I. Gvozdev^2*

¹Biosensor AN Ltd., pr. Akademika Semenova 1, 142432 Chernogolovka, Moscow Region, Russia; fax: (496) 515-3588; E-mail: gari@icp.ac.ru

²Institute of Problems of Chemical Physics, Russian Academy of Sciences, pr. Akademika Semenova 1, 142432 Chernogolovka, Moscow Region, Russia; fax: (496) 522-3507; E-mail: ildar@cat.icp.ac.ru; gvozd@cat.icp.ac.ru

^* To whom correspondence should be addressed.

Received February 1, 2012; Revision received March 23, 2012

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This review considers quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases, enzymes that are present in numerous methylotrophic eu- and prokaryotes and significantly differ in their primary and quaternary structure. The cofactors of the enzymes are bound to the protein polypeptide chain through ionic and hydrophobic interactions. Microorganisms containing these enzymes are described. Methods for purification of the enzymes, their physicochemical properties, and spatial structures are considered. The supposed mechanism of action and practical application of these enzymes as well as their producers are discussed.

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KEY WORDS: methanol dehydrogenase, ethanol dehydrogenase, quinohemeprotein alcohol dehydrogenase, FAD-methanol oxidase, three-dimensional structure, mechanism of action

DOI: 10.1134/S0006297912080056

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