Literature DB >> 23650044

A tandem chemoenzymatic methylation by S-adenosyl-L-methionine.

Joseph M Lipson1, Marie Thomsen, Bradley S Moore, Rasmus P Clausen, James J La Clair, Michael D Burkart.   

Abstract

Keep 'em methylated: The in situ preparation of the cofactor AdoMet was achieved by allowing the biosynthetic enzyme SalL to operate in the reverse direction by presentation of 5'-chloro-5'-deoxyadenosine at low salt concentrations. This reaction was readily coupled with DNA and small molecule methyltransferases to afford a regioselective method for chemo-enzymatic methylation and isotope incorporation.
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Year:  2013        PMID: 23650044      PMCID: PMC3749784          DOI: 10.1002/cbic.201300221

Source DB:  PubMed          Journal:  Chembiochem        ISSN: 1439-4227            Impact factor:   3.164


  32 in total

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Review 10.  Architectures, mechanisms and molecular evolution of natural product methyltransferases.

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  11 in total

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4.  Chemoenzymatic synthesis and in situ application of S-adenosyl-L-methionine analogs.

Authors:  Marie Thomsen; Stine B Vogensen; Jens Buchardt; Michael D Burkart; Rasmus P Clausen
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Review 9.  Methyltransferase-Directed Labeling of Biomolecules and its Applications.

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10.  A bicyclic S-adenosylmethionine regeneration system applicable with different nucleosides or nucleotides as cofactor building blocks.

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