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Kinetic mechanism of the GCN5-related chromosomal...
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