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Bulgecin A: a novel inhibitor of binuclear metallo-beta-lactamases

Simm, Alan M., Loveridge, Edric Joel, Crosby, John, Avison, Matthew B., Walsh, Timothy Rutland and Bennett, Peter M. 2005. Bulgecin A: a novel inhibitor of binuclear metallo-beta-lactamases. Biochemical Journal 387 (3) , pp. 585-590. 10.1042/BJ20041542

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Abstract

Bulgecin A, a sulphonated N-acetyl-D-glucosamine unit linked to a 4-hydroxy-5-hydroxymethylproline ring by a b-glycosidic linkage, is a novel type of inhibitor for binuclear metallo-b-lactamases. Using steady-state kinetic analysis with nitrocefin as the b-lactam substrate, bulgecin A competitively inhibited the metallo-b-lactamase BceII from Bacillus cereus in its two-zinc form, but failed to inhibit when the enzyme was in the single-zinc form. The competitive inhibition was restored by restoring the second zinc ion. The single-zinc metallo-b-lactamase from Aeromonas veronii bv. sobria, ImiS, was not inhibited by bulgecin A. The tetrameric L1 metallo-b-lactamase from Stenotrophomonas maltophilia was subject to partial non-competitive inhibition, which is consistent with a kinetic model in which the enzyme bound to inhibitor retains catalytic activity. Docking experiments support the conclusion that bulgecin A co-ordinates to the zinc II site in metallo-b-lactamases via the terminal sulphonate group on the sugar moiety.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Chemistry
Medicine
Systems Immunity Research Institute (SIURI)
Subjects: R Medicine > R Medicine (General)
Uncontrolled Keywords: antibiotic resistance; bulgecin A; inhibitor; metallo-b-lactamase; Stenotrophomonas; zinc co-ordination.
ISSN: 1470-8728
Last Modified: 05 Jun 2017 01:33
URI: http://orca.cf.ac.uk/id/eprint/308

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