Purification and characterization of a novel glycine oxidase from Bacillus subtilis.
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.
Nishiya
Y
Y
Tsuruga Institute of Biotechnology, Toyobo Co., Ltd., Fukui, Japan. yoshiaki_nishiya@bio-toyobo.co.jp
Imanaka
T
T
D000594:Amino Acid Oxidoreductases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli; D016680:Genome, Bacterial; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D016366:Open Reading Frames; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D015183:Restriction Mapping; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013552:Swine
D011994:Recombinant Proteins; D000594:Amino Acid Oxidoreductases; C115925:glycine oxidase