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Chemoenzymatic synthesis and utilization of a SAM analog with an isomorphic nucleobase.


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.

SUBMITTER: Vranken C 

PROVIDER: S-EPMC4927405 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature

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Chemoenzymatic synthesis and utilization of a SAM analog with an isomorphic nucleobase.

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]

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