Journal article
Kinetic mechanism of the GCN5-related chromosomal aminoglycoside acetyltransferase AAC(6')-Ii from Enterococcus faecium: evidence of dimer subunit cooperativity
Abstract
The aminoglycoside 6'-N-acetyltransferase AAC(6')-Ii from Enterococcus faecium is an important microbial resistance determinant and a member of the GCN5-related N-acetyltransferase (GNAT) superfamily. We report here the further characterization of this enzyme in terms of the kinetic mechanism of acetyl transfer and identification of rate-contributing step(s) in catalysis, as well as investigations into the binding of both acetyl-CoA and …
Authors
Draker K; Northrop DB; Wright GD
Journal
Biochemistry, Vol. 42, No. 21, pp. 6565–6574
Publication Date
June 3, 2003
DOI
10.1021/bi034148h
ISSN
0006-2960