A QM/MM study of Kemptide phosphorylation catalyzed by protein kinase A. The role of Asp166 as a general acid/base catalyst-Reference-Cited by-同舟云学术

A QM/MM study of Kemptide phosphorylation catalyzed by protein kinase A. The role of Asp166 as a general acid/base catalyst

Published:2015 Issue:5 Volume:17 Page:3497-3511
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Pérez-Gallegos Ayax¹²³⁴,Garcia-Viloca Mireia¹²³⁴,González-Lafont Àngels¹²³⁴,Lluch José M.¹²³⁴

Affiliation:

1. Institut de Biotecnologia i de Biomedicina and Departament de Química

2. Universitat Autònoma de Barcelona

3. 08193 Bellaterra (Barcelona)

4. Spain

Abstract

QM/MM calculations show that Asp166 is a general acid/base catalyst along the phosphoryl and proton transfer steps of Kemptide phosphorylation by protein kinase A.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2015/CP/C4CP03579H

Reference75 articles.

1. The Protein Kinase Complement of the Human Genome

2. Kinase Drug Discovery – What’s Next in the Field?

3. Kinetic and Catalytic Mechanisms of Protein Kinases

4. Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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