d-Aspartate oxidase: distribution, functions, properties, and biotechnological applications

被引:17
|
作者
Takahashi, Shouji [1 ]
机构
[1] Nagaoka Univ Technol, Dept Bioengn, Nagaoka, Niigata 9402188, Japan
基金
日本学术振兴会;
关键词
d-aspartate oxidase; Acidic d-amino acids; Flavoenzyme; Oxidoreductase; Applications; D-AMINO-ACID; FREE D-GLUTAMATE; SUBSTRATE-SPECIFICITY; ESCHERICHIA-COLI; ENZYME; RAT; YEAST; BRAIN; CLONING; KIDNEY;
D O I
10.1007/s00253-020-10439-9
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
Recently, substantial levels of acidic d-amino acids, such as d-aspartate and d-glutamate, have been identified in many organisms, from bacteria to mammals, suggesting that acidic d-amino acids have multiple physiological significances. Although acidic d-amino acids found in animals primarily originate from foodstuffs and/or bacteria, the d-aspartate-synthesizing enzyme aspartate racemase is identified in various animals. In eukaryotic organisms, acidic d-amino acids are primarily degraded by the flavoenzyme d-aspartate oxidase (DDO). DDO is found in multiple eukaryotic organisms and may play important roles in acidic d-amino acid utilization, elimination, and intracellular level regulation. Moreover, owing to its perfect enantioselectivity and stereoselectivity, DDO may be a valuable tool in several biotechnological applications, including the identification and quantification of acidic d-amino acids. In this mini-review, previous DDO reports are summarized and the potential bioengineering and biotechnological applications of DDO are discussed.
引用
收藏
页码:2883 / 2895
页数:13
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