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Int. J. Mol. Sci. 2016, 17(7), 1018; doi:10.3390/ijms17071018

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT)

1
Infection and Immunity Program, Monash Biomedicine Discovery Institute; Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia
2
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia
*
Author to whom correspondence should be addressed.
Academic Editor: Claudiu T. Supuran
Received: 30 May 2016 / Revised: 14 June 2016 / Accepted: 20 June 2016 / Published: 28 June 2016
(This article belongs to the Special Issue Enzyme-Inhibitor Interaction as Examples of Molecular Recognition)

Abstract

General control non-repressible 5 (GCN5)-related N-acetyltransferases (GNAT) catalyze the transfer of an acyl moiety from acyl coenzyme A (acyl-CoA) to a diverse group of substrates and are widely distributed in all domains of life. This review of the currently available data acquired on GNAT enzymes by a combination of structural, mutagenesis and kinetic methods summarizes the key similarities and differences between several distinctly different families within the GNAT superfamily, with an emphasis on the mechanistic insights obtained from the analysis of the complexes with substrates or inhibitors. It discusses the structural basis for the common acetyltransferase mechanism, outlines the factors important for the substrate recognition, and describes the mechanism of action of inhibitors of these enzymes. It is anticipated that understanding of the structural basis behind the reaction and substrate specificity of the enzymes from this superfamily can be exploited in the development of novel therapeutics to treat human diseases and combat emerging multidrug-resistant microbial infections. View Full-Text
Keywords: GNAT; acetyltransferase; crystal structure; reaction mechanism; enzyme inhibitor; catalytic residues GNAT; acetyltransferase; crystal structure; reaction mechanism; enzyme inhibitor; catalytic residues
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Salah Ud-Din, A.I.M.; Tikhomirova, A.; Roujeinikova, A. Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT). Int. J. Mol. Sci. 2016, 17, 1018.

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