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Purification and characterization of a novel glycine oxidase from Bacillus subtilis
Author(s) -
Nishiya Yoshiaki,
Imanaka Tadayuki
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01313-1
Subject(s) - sarcosine , bacillus subtilis , d amino acid oxidase , biochemistry , glycine cleavage system , amino acid , oxidase test , glycine , alanine , biology , chemistry , enzyme , bacteria , genetics
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.