Structure and functions of the GNAT superfamily of acetyltransferases

被引：494

作者：

Vetting, MW ^{[1
]}

de Carvalho, LPS ^{[1
]}

Yu, M ^{[1
]}

Hegde, SS ^{[1
]}

Magnet, S ^{[1
]}

Roderick, SL ^{[1
]}

Blanchard, JS ^{[1
]}

机构：

[1] Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2005年 / 433卷 / 01期

关键词：

acetyltransferase; three-dimensional structure; steady-state kinetics; GNAT histone acetytransferase; chemical mechanism; structure and function of enzymes; protein modification; antibiotic resistance;

D O I：

10.1016/j.abb.2004.09.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Gcn5-related N-acetyltransferases are an enormous superfamily of enzymes that are universally distributed in nature and that use acyl-CoAs to acylate their cognate substrates. In this review, we will examine those members of this superfamily that have been both structurally and mechanistically characterized. These include aminoglycoside N-acetyltransferases. serotonin N-acetyltransferase, glucosamine-6-phosphate N-acetyltransferase, the histone acetyltransferases, mycothiol synthase, protein N-myristoyl-transferase, and the Fern family of amino acyl transferases. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：212 / 226

页数：15

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