Chemoenzymatic synthesis and utilization of a SAM analog with an isomorphic nucleobaseElectronic supplementary information (ESI) available: Synthesis and characterization of new compounds, expression of SalL enzyme, enzymatic procedures and control experiments. See DOI: 10.1039/c6ob00844e

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...

Full description

Saved in:
Bibliographic Details
Main Authors Vranken, C, Fin, A, Tufar, P, Hofkens, J, Burkart, M. D, Tor, Y
Format Journal Article
Published 29.06.2016
Online AccessGet full text

Cover

More Information
Summary: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. Taq I. A synthetic SAM analog with an unnatural isomorphic nucleobase is enzymatically synthesized and shown to serve as a methyl donor.
Bibliography:10.1039/c6ob00844e
Electronic supplementary information (ESI) available: Synthesis and characterization of new compounds, expression of SalL enzyme, enzymatic procedures and control experiments. See DOI
ISSN:1477-0520
1477-0539
DOI:10.1039/c6ob00844e