| Literature DB >> 27270873 |
C Vranken1, A Fin, P Tufar, J Hofkens, M D Burkart, Y Tor.
Abstract
SalL, an enzyme that catalyzes the synthesis of SAM from l-methionine and 5'-chloro-5'-deoxyoadenosine, is shown to accept 5'-chloro-5'-deoxythienoadenosine as a substrate and facilitate the synthesis of a synthetic SAM analog with an unnatural nucleobase. This synthetic cofactor is demonstrated to replace SAM in the DNA methylation reaction with M.TaqI.Entities:
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Year: 2016 PMID: 27270873 PMCID: PMC4927405 DOI: 10.1039/c6ob00844e
Source DB: PubMed Journal: Org Biomol Chem ISSN: 1477-0520 Impact factor: 3.876