Ontology highlight
ABSTRACT:
SUBMITTER: Vranken C
PROVIDER: S-EPMC4927405 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Vranken C C Fin A A Tufar P P Hofkens J J Burkart M D MD Tor Y Y
Organic & biomolecular chemistry 20160606 26
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. ...[more]