Title of article :
Structure and functions of the GNAT superfamily of acetyltransferases
Author/Authors :
Matthew W Vetting and Douglas H Ohlendorf، نويسنده , , Matthew W. and S. de Carvalho، نويسنده , , Luiz Pedro and Yu، نويسنده , , Michael and Hegde، نويسنده , , Subray S. and Magnet، نويسنده , , Sophie and Roderick، نويسنده , , Steven L. and Blanchard، نويسنده , , John S.، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2005
Pages :
15
From page :
212
To page :
226
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 :
three-dimensional structure , steady-state kinetics , Acetyltransferase , GNAT , Histone acetyltransferase , Chemical mechanism , protein modification , Structure and function of enzymes , Antibiotic resistance
Journal title :
Archives of Biochemistry and Biophysics
Serial Year :
2005
Journal title :
Archives of Biochemistry and Biophysics
Record number :
1626726
Link To Document :
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