Purification and characterization of a novel glycine oxidase from Bacillus subtilis

FEBS Lett. 1998 Nov 6;438(3):263-6. doi: 10.1016/s0014-5793(98)01313-1.


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.

MeSH terms

  • Amino Acid Oxidoreductases / genetics*
  • Amino Acid Oxidoreductases / isolation & purification
  • Amino Acid Oxidoreductases / metabolism*
  • Animals
  • Bacillus subtilis / enzymology*
  • Bacillus subtilis / genetics
  • Chromatography, Ion Exchange
  • Escherichia coli
  • Genome, Bacterial
  • Kidney / enzymology
  • Kinetics
  • Open Reading Frames
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Restriction Mapping
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Swine


  • Recombinant Proteins
  • Amino Acid Oxidoreductases
  • glycine oxidase