Issue 10, 2016
From the journal:

Molecular BioSystems

Exploring the origin of the catalytic power and product specificity of SET domain protein methyltransferase†

A. H. Lima,a   C. N. Alves,a   R. Prasad*b  and  J. Lameira*a  

* Corresponding authors

a Faculdade de Biotecnologia e Laboratório de Planejamento e Desenvolvimento de Fármacos, Universidade Federal do Pará, Belém, PA, Brazil
E-mail: lameira@ufpa.br

b Southern California, Department of Chemistry, SGM 418, 3620 McClintosk Avenue, Los Angeles, California 90089, USA
E-mail: rams.crux@yahoo.com

Abstract

Herein, we used computer simulation to evaluate the free energy activation barriers of the first and second methyl transfer for native SET8 PKMT and its Y334F mutant. The results suggest that the origin of SET8 catalytic power is mainly due to electrostatic preorganization.

Graphical abstract: Exploring the origin of the catalytic power and product specificity of SET domain protein methyltransferase

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Article information

DOI
https://doi.org/10.1039/C6MB00414H
Article type
Communication
Submitted
26 May 2016
Accepted
21 Jul 2016
First published
21 Jul 2016

Mol. BioSyst., 2016,12, 2980-2983

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Exploring the origin of the catalytic power and product specificity of SET domain protein methyltransferase

A. H. Lima, C. N. Alves, R. Prasad and J. Lameira, Mol. BioSyst., 2016, 12, 2980 DOI: 10.1039/C6MB00414H

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