Structure and functions of the GNAT superfamily of acetyltransferases

Matthew W. Vetting; Luiz Pedro Luiz; Michael Yu; Subray S. Hegde; Sophie Magnet; Steven L. Roderick; John S. Blanchard

doi:10.1016/j.abb.2004.09.003

Structure and functions of the GNAT superfamily of acetyltransferases

Matthew W. Vetting, Luiz Pedro Luiz, Michael Yu, Subray S. Hegde, Sophie Magnet, Steven L. Roderick, John S. Blanchard

Biochemistry

Research output: Contribution to journal › Short survey › peer-review

497 Scopus citations

Abstract

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-myristoyltransferase, and the Fem family of amino acyl transferases.

Original language	English (US)
Pages (from-to)	212-226
Number of pages	15
Journal	Archives of Biochemistry and Biophysics
Volume	433
Issue number	1
DOIs	https://doi.org/10.1016/j.abb.2004.09.003
State	Published - Jan 1 2005

Keywords

Acetyltransferase
Antibiotic resistance
Chemical mechanism
GNAT
Histone acetyltransferase
Protein modification
Steady-state kinetics
Structure and function of enzymes
Three-dimensional structure

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/j.abb.2004.09.003

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title = "Structure and functions of the GNAT superfamily of acetyltransferases",

abstract = "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-myristoyltransferase, and the Fem family of amino acyl transferases.",

keywords = "Acetyltransferase, Antibiotic resistance, Chemical mechanism, GNAT, Histone acetyltransferase, Protein modification, Steady-state kinetics, Structure and function of enzymes, Three-dimensional structure",

author = "Vetting, {Matthew W.} and Luiz, {Luiz Pedro} and Michael Yu and Hegde, {Subray S.} and Sophie Magnet and Roderick, {Steven L.} and Blanchard, {John S.}",

note = "Funding Information: This work was supported by Grants AI33696 and AI60899 (to J.S.B.) from the National Institutes of Health. M. Yu was supported by Training Grant T32 GM08572 from the National Institutes of Health. ",

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T1 - Structure and functions of the GNAT superfamily of acetyltransferases

AU - Vetting, Matthew W.

AU - Luiz, Luiz Pedro

AU - Yu, Michael

AU - Hegde, Subray S.

AU - Magnet, Sophie

AU - Roderick, Steven L.

AU - Blanchard, John S.

N1 - Funding Information: This work was supported by Grants AI33696 and AI60899 (to J.S.B.) from the National Institutes of Health. M. Yu was supported by Training Grant T32 GM08572 from the National Institutes of Health.

PY - 2005/1/1

Y1 - 2005/1/1

N2 - 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-myristoyltransferase, and the Fem family of amino acyl transferases.

AB - 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-myristoyltransferase, and the Fem family of amino acyl transferases.

KW - Acetyltransferase

KW - Antibiotic resistance

KW - Chemical mechanism

KW - GNAT

KW - Histone acetyltransferase

KW - Protein modification

KW - Steady-state kinetics

KW - Structure and function of enzymes

KW - Three-dimensional structure

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DO - 10.1016/j.abb.2004.09.003

M3 - Short survey

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AN - SCOPUS:9744255506

SN - 0003-9861

VL - 433

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JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

IS - 1

ER -

Structure and functions of the GNAT superfamily of acetyltransferases

Abstract

Keywords

ASJC Scopus subject areas

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