Protein Methyltransferases: A Distinct, Diverse, and Dynamic Family of Enzymes - PubMed (original) (raw)

Review

. 2016 Mar 22;55(11):1557-69.

doi: 10.1021/acs.biochem.5b01129. Epub 2015 Dec 22.

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Review

Protein Methyltransferases: A Distinct, Diverse, and Dynamic Family of Enzymes

P Ann Boriack-Sjodin et al. Biochemistry. 2016.

Abstract

Methyltransferase proteins make up a superfamily of enzymes that add one or more methyl groups to substrates that include protein, DNA, RNA, and small molecules. The subset of proteins that act upon arginine and lysine side chains are characterized as epigenetic targets because of their activity on histone molecules and their ability to affect transcriptional regulation. However, it is now clear that these enzymes target other protein substrates, as well, greatly expanding their potential impact on normal and disease biology. Protein methyltransferases are well-characterized structurally. In addition to revealing the overall architecture of the subfamilies of enzymes, structures of complexes with substrates and ligands have permitted detailed analysis of biochemical mechanism, substrate recognition, and design of potent and selective inhibitors. This review focuses on how knowledge gained from structural studies has impacted the understanding of this large class of epigenetic enzymes.

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