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Characterization of N-demethyllincosamide methyltransferases LmbJ and CcbJ
L. Najmanová, E. Kutejová, J. Kadlec, M. Polan, J. Olšovská, O. Benada, J. Novotná, Z. Kameník, P. Halada, J. Bauer, J. Janata,
Chembiochem.
2013 ;
14 (17) :
2259-62.
Language English Country Germany
Document type Journal Article, Research Support, Non-U.S. Gov't
Persistent link
https://www.medvik.cz/link/bmc14063870
- 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
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.
References provided by Crossref.org
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