Effect of site‐specific mutagenesis of tyrosine‐55, methionine‐110 and histidine‐217 in porcine kidney D‐amino acid oxidase on its catalytic function

FEBS Letters

Miyake, Yoshihiro¹  Momoi, Kyoko¹  Watanabe, Fusao¹  Fukui, Kiyoshi¹ 

[1] Department of Biochemistry, National Cardiovascular Center Research Institute, Fujishirodai 5-chome, Suita, Osaka 565, Japan

关键词: D-Amino acid oxidase;    Site-specific mutagenesis;    Protein engineering;    Reaction mechanism;    (Porcine kidney);    DAO;    D-amino acid oxidase;    kbp;    kilobase pair;   

DOI  :  10.1016/0014-5793(88)80494-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To assess the contributions of Tyr-55, Met-110 and His-217 in porcine kidney D-amino acid oxidase (EC 1.4.3.3, DAO) to its catalytic function, we constructed three mutant cDNAs coding for the enzymes possessing Phe-55, Leu-110 and Leu-217 by site-specific mutagenesis. The mutant and wild type cDNAs could be expressed in vitro with similar efficiency. The three mutant enzymes thus synthesized showed catalytic activities comparable to that of the wild type oxidase. It is concluded that Tyr-55, Met-110 and His-217 are not directly involved in the catalytic function.

【 授权许可】

Unknown