New biotech applications from evolved D-amino acid oxidases.

Gianluca Molla, Loredano Pollegioni

Journal: Trends in biotechnology 2011;29(6):276-83

PMID: 21397351

Full Text on Elsevier Science View on PubMed

Abstract

D-Amino acid oxidase (DAAO) is a well-known flavoenzyme that catalyzes the oxygen-dependent oxidative deamination of amino acid D-isomers with absolute stereospecificity, which results in α-keto acids, ammonia and hydrogen peroxide. Recently, the extraordinary functional plasticity of DAAO has become evident; in turn, boosting research on this flavoprotein. Protein engineering has allowed for a redesign of DAAO substrate specificity, oxygen affinity, cofactor binding, stability, and oligomeric state. We review recent developments in utilizing DAAO, including as a biocatalyst for resolving racemic amino acid mixtures, as a tool for biosensing, and as a new mechanism of herbicide resistance. Perspectives for future biotechnological applications of this oxidative biocatalyst are also outlined.

Address: Dipartimento di Biotecnologie e Scienze Molecolari, Università degli Studi dell'Insubria, Varese, Italy. [email protected]

DOI: 10.1016/j.tibtech.2011.01.010

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MeSH Terms: Amino Acids, Ammonia, Biotechnology, Coenzymes, D-Amino-Acid Oxidase, Hydrogen Peroxide, Keto Acids, Oxygen, Protein Engineering, Protein Stability, Substrate Specificity