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PMID:9827558
| Citation |
Nishiya, Y and Imanaka, T (1998) Purification and characterization of a novel glycine oxidase from Bacillus subtilis. FEBS Lett. 438:263-6 |
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| Abstract |
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. |
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| Keywords |
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 |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
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Contributes to |
GO:0043799: sarcosine oxidase activity |
ECO:0000250: |
UniProtKB:O31616
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F |
After finding a gene product termed yjbR they noticed that it had a sequence similarity with bacteria sarcosine oxidases. From there they measured yjbR gene products substrate specificity (table 2). They found that there is higher rate of activites with N-methyl-d-alanine, d-proline, d-alanine, and d-2-aminobutyrate. |
complete | ||
Notes
See also
References
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