N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion.

ABSTRACT: NagA is a member of the amidohydrolase superfamily and catalyzes the deacetylation of N-acetyl-d-glucosamine-6-phosphate. The catalytic mechanism of this enzyme was addressed by the characterization of the catalytic properties of metal-substituted derivatives of NagA from Escherichia coli with a variety of substrate analogues. The reaction mechanism is of interest since NagA from bacterial sources is found with either one or two divalent metal ions in the active site. This observation indicates that there has been a divergence in the evolution of NagA and suggests that there are fundamental differences in the mechanistic details for substrate activation and hydrolysis. NagA from E. coli was inactivated by the removal of the zinc bound to the active site and the apoenzyme reactivated upon i

SUBMITTER: Hall RS 

PROVIDER: S-EPMC2533526 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature