REVIEW: D-Amino Acid Oxidase: Structure, Catalytic Mechanism, and Practical Application

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V. I. Tishkov^* and S. V. Khoronenkova

Department of Chemical Enzymology, Faculty of Chemistry, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (7-095) 939-2742; E-mail: vit@enz.chem.msu.ru; tishkov@pochta.ru

^* To whom correspondence should be addressed.

Received July 15, 2004

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D-Amino acid oxidase (DAAO) is a FAD-dependent enzyme that plays an important role in microbial metabolism, utilization of endogenous D-amino acids, regulation of the nervous system, and aging in mammals. DAAO from yeasts Rhodotorula gracilis and Trigonopsis variabilis are used to convert cephalosporin C into 7-aminocephalosporanic acid, the precursor of other semi-synthetic cephalosporins. This review summarizes the recent data on the enzyme localization, physiological role, gene cloning and expression, and the studies on the enzyme structure, stability, catalytic mechanism, and practical applications.

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KEY WORDS: D-amino acid oxidase, cloning, expression, stability, protein engineering, Trigonopsis variabilis, Rhodotorula gracilis

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