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Bioorg Med Chem Lett. 2000 Dec 18;10(24):2795-8.

Inhibition of Escherichia coli glucosamine synthetase by novel electrophilic analogues of glutamine--comparison with 6-diazo-5-oxo-norleucine.

Author information

1
Division of Biomedicinal Chemistry, School of Pharmacy, The Queen's University of Belfast, Medical Biology Centre, Northern Ireland, UK. brian.walker@qub.ac.uk

Abstract

A series of electrophilic glutamine analogues based on 6-diazo-5-oxo-norleucine has been prepared, using novel synthetic routes, and evaluated as inhibitors of Escherichia coli glucosamine synthetase. The gamma-dimethylsulphonium salt analogue of glutamine was found to be one of the most potent inactivators of this enzyme yet reported, with an apparent second order rate constant (k2/Ki) of 3.5 x 10(5) M(-1) min(-1).

PMID:
11133094
DOI:
10.1016/s0960-894x(00)00565-5
[Indexed for MEDLINE]

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