Purification and characterization of a novel glycine oxidase from Bacillus subtilis

FEBS Letters

Imanaka, Tadayuki²  Nishiya, Yoshiaki¹ 

[1] Tsuruga Institute of Biotechnology, Toyobo Co., Ltd., Toyo-cho 10-24, Tsuruga, Fukui 914-0047, Japan;Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 606-8501, Japan

关键词: Glycine oxidase;    Sarcosine oxidase;    d-Amino acid oxidase;    Bacillus subtilis;   

DOI  :  10.1016/S0014-5793(98)01313-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The open reading frame yjbR which had been sequenced as a part of the Bacillus subtilis genome project encodes a putative 40.9-kDa protein. The yjbR-coding sequence was slightly similar to those of bacterial sarcosine oxidases and possibly compatible with the tertiary structure of the porcine kidney d-amino acid oxidase. The yjbR gene product was overproduced in Escherichia coli, purified to homogeneity from the recombinant strain, and characterized. This protein effectively catalyzed the oxidation of sarcosine (N-methylglycine), N-ethylglycine and glycine. Lower activities on d-alanine, d-valine, and d-proline were detected although no activities were shown on l-amino acids and other d-amino acids. Since glycine is a product and not a substrate for sarcosine oxidase, this protein is not a type of demethylating enzymes but a novel deaminating oxidase, named glycine oxidase as a common name. Several enzymatic properties of the B. subtilis glycine oxidase were also investigated.

【 授权许可】

Unknown