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

共 73 条

[31] A potent inhibitor of the melatonin rhythm enzyme [J].

Khalil, EM ;

Cole, PA .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (24) :6195-6196

[32] Mechanism-based inhibition of the melatonin rhythm enzyme: Pharmacologic exploitation of active site functional plasticity [J].

Khalil, EM ;

De Angelis, J ;

Ishii, M ;

Cole, PA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (22) :12418-12423

[33] Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes [J].

Koledin, T ;

Newton, GL ;

Fahey, RC .

ARCHIVES OF MICROBIOLOGY, 2002, 178 (05) :331-337

[34] p300/CBP-associated factor histone acetyltransferase processing of a peptide substrate [J].

Lau, OD ;

Courtney, AD ;

Vassilev, A ;

Marzilli, LA ;

Cotter, RJ ;

Nakatani, Y ;

Cole, PA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (29) :21953-21959

[35] Aminoglycosides modified by resistance enzymes display diminished binding to the bacterial ribosomal aminoacyl-tRNA site [J].

Llano-Sotelo, B ;

Azucena, EF ;

Kotra, LP ;

Mobashery, S ;

Chow, CS .

CHEMISTRY & BIOLOGY, 2002, 9 (04) :455-463

[36] TARGETED GENE REPLACEMENT DEMONSTRATES THAT MYRISTOYL-COA/PROTEIN N-MYRISTOYLTRANSFERASE IS ESSENTIAL FOR VIABILITY OF CRYPTOCOCCUS-NEOFORMANS [J].

LODGE, JK ;

JACKSONMACHELSKI, E ;

TOFFALETTI, DL ;

PERFECT, JR ;

GORDON, JI .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (25) :12008-12012

[37] Genetic and biochemical studies establish that the fungicidal effect of a fully depeptidized inhibitor of Cryptococcus neoformans myristoyl-CoA:protein N-myristoyltransferase (Nmt) is Nmt-dependent [J].

Lodge, JK ;

Jackson-Machelski, E ;

Higgins, M ;

McWherter, CA ;

Sikorski, JA ;

Devadas, B ;

Gordon, JI .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (20) :12482-12491

[38] Activation of the cryptic aac(6′)-Iy aminoglycoside resistance gene of Salmonella by a chromosomal deletion generating a transcriptional fusion [J].

Magnet, S ;

Courvalin, P ;

Lambert, T .

JOURNAL OF BACTERIOLOGY, 1999, 181 (21) :6650-6655

[39] Kinetic and mutagenic characterization of the chromosomally encoded Salmonella enterica AAC(6′)-Iy aminoglycoside N-acetyltransferase [J].

Magnet, S ;

Lambert, T ;

Courvalin, P ;

Blanchard, JS .

BIOCHEMISTRY, 2001, 40 (12) :3700-3709

[40] Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis [J].

Mio, T ;

Yamada-Okabe, T ;

Arisawa, M ;

Yamada-Okabe, H .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (01) :424-429

← 1 2 3 4 5 6 7 8 →