New biotech applications from evolved D-amino acid oxidases

被引:106
|
作者
Pollegioni, Loredano [1 ,2 ]
Molla, Gianluca [1 ,2 ]
机构
[1] Univ Insubria, Dipartimento Biotecnol & Sci Mol, Varese, Italy
[2] Politecn Milan, Prot Factory, Ctr Interuniv Biotecnol Prote, Varese, Italy
关键词
D-SERINE; GLYCINE OXIDASE; SUBSTRATE-SPECIFICITY; ACTIVE-SITE; D-ALANINE; YEAST; EVOLUTION; FUSION; ENZYME; THERMOSTABILITY;
D O I
10.1016/j.tibtech.2011.01.010
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
D-Amino acid oxidase (DAAO) is a well-known flavoenzyme that catalyzes the oxygen-dependent oxidative de-amination of amino acid D-isomers with absolute stereospecificity, which results in a-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.
引用
收藏
页码:276 / 283
页数:8
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