White Rose University Consortium logo
University of Leeds logo University of Sheffield logo York University logo

Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase

Vincent, F., Davies, G.J. and Brannigan, J.A. (2005) Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase. Journal Of Biological Chemistry, 280 (20). pp. 19649-19655. ISSN 0021-9258

Full text not available from this repository.

Abstract

Glucosamine 6-phosphate is converted to fructose 6-phosphate and ammonia by the action of the enzyme glucosamine 6-phosphate deaminase, NagB. This reaction is the final step in the specific GlcNAc utilization pathway and thus decides the metabolic fate of GlcNAc. Sequence analyses suggest that the NagB "superfamily" consists of three main clusters: multimeric and allosterically regulated glucosamine-6-phosphate deaminases (exemplified by Escherichia coli NagB), phosphogluconolactonases, and monomeric hexosamine-6-phosphate deaminases. Here we present the three-dimensional structure and kinetics of the first member of this latter group, the glucosamine-6-phosphate deaminase, NagB, from Bacillus subtilis. The structures were determined in ligand-complexed forms at resolutions around 1.4 Å. BsuNagB is monomeric in solution and as a consequence is active (kcat 28 s-1, Km(app) 0.13 mM) without the need for allosteric activators. A decrease in activity at high substrate concentrations may reflect substrate inhibition (with Ki of 4 mM). The structure completes the NagB superfamily structural landscape and thus allows further interrogation of genomic data in terms of the regulation of NagB and the metabolic fate(s) of glucosamine 6-phosphate.

Item Type: Article
Academic Units: The University of York > Chemistry (York)
Depositing User: York RAE Import
Date Deposited: 24 Apr 2009 09:50
Last Modified: 24 Apr 2009 09:50
Published Version: http://dx.doi.org/10.1074/jbc.M502131200
Status: Published
Publisher: The American Society for Biochemistry and Molecular Biology
Identification Number: 10.1074/jbc.M502131200
URI: http://eprints.whiterose.ac.uk/id/eprint/6554

Actions (login required)

View Item View Item