Importance of the main chain of lysine for histone lysine methyltransferase catalysis

Literature Information

Publication Date 2019-05-20
DOI 10.1039/C9OB01038F
Impact Factor 3.876
Authors

Abbas H. K. Al Temimi, Ruben S. Teeuwen, Vu Tran, Arthur J. Altunc, Danny C. Lenstra, Wansheng Ren, Ping Qian, Hong Guo


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Abstract

Histone lysine methyltransferases (KMTs) are biomedicinally important class of epigenetic enzymes that catalyse methylation of lysine residues in histones and other proteins. Enzymatic and computational studies on the simplest lysine analogues that possess a modified main chain demonstrate that the lysine's backbone contributes significantly to functional KMT binding and catalysis.

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Organic & Biomolecular Chemistry

Organic & Biomolecular Chemistry
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Organic & Biomolecular Chemistry (OBC) publishes original and high impact research and reviews in organic chemistry. We welcome research that shows new or significantly improved protocols or methodologies in total synthesis, synthetic methodology or physical and theoretical organic chemistry as well as research that shows a significant advance in the organic chemistry or molecular design aspects of chemical biology, catalysis, supramolecular and macromolecular chemistry, theoretical chemistry, mechanism-oriented physical organic chemistry, medicinal chemistry or natural products. Articles published in the journal should report new work which makes a highly-significant impact in the field. Routine and incremental work is generally not suitable for publication in the journal. More details about key areas of our scope are below. In all cases authors should include in their article clear rationale for why their research has been carried out.

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