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.

New biotech applications from evolved D-amino acid oxidases.

POLLEGIONI, LOREDANO;MOLLA, GIANLUCA
2011-01-01

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.
2011
http://dx.doi.org/10.1016/j.tibtech.2011.01.010
Amino Acids; metabolism; Ammonia; Biotechnology; methods; Coenzymes; D-Amino-Acid Oxidase; chemistry/metabolism; Hydrogen Peroxide; Keto Acids; Oxygen; Protein Engineering; Protein Stability; Substrate Specificity
Pollegioni, Loredano; Molla, Gianluca
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11383/1730198
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