Characterization of N-demethyllincosamide methyltransferases LmbJ and CcbJ
Language English Country Germany Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
Persistent link
https://www.medvik.cz/link/pmid24166757
- Keywords
- N-methyltransferases, Streptomyces, antibiotics, lincomycin, natural products,
- MeSH
- Anti-Bacterial Agents biosynthesis chemistry MeSH
- Biocatalysis * MeSH
- Lincomycin biosynthesis chemistry MeSH
- Lincosamides biosynthesis chemistry MeSH
- Methyltransferases chemistry metabolism MeSH
- Molecular Conformation MeSH
- Substrate Specificity MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Anti-Bacterial Agents MeSH
- celesticetin A MeSH Browser
- Lincomycin MeSH
- Lincosamides MeSH
- Methyltransferases MeSH
Chemical diversity: Two SAM-dependent N-methyltransferases-LmbJ from the biosynthesis of the antibiotic lincomycin and CcbJ from celesticetin biosynthesis-have been characterized and compared. Both tested enzymes form multimers and are able to utilize N-demethyllincomycin, the natural substrate of LmbJ, with comparable efficiency.
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