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

Research output: Contribution to journalShort survey

373 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 languageEnglish (US)
Pages (from-to)212-226
Number of pages15
JournalArchives of Biochemistry and Biophysics
Volume433
Issue number1
DOIs
StatePublished - Jan 1 2005

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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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