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Simm, A.M. et al.

Simm, Loveridge, Crosby, Avison, Walsh, Bennett,

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

Bulgecin A, a sulphonated N-acetyl-D-glucosamine unit linked to a 4-hydroxy-5-hydroxymethylproline ring by a beta-glycosidic linkage, is a novel type of inhibitor for binuclear metallo-beta-lactamases. Using steady-state kinetic analysis with nitrocefin as the beta-lactam substrate, bulgecin A competitively inhibited the metallo-beta-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-beta-lactamase from Aeromonas veronii bv. sobria, ImiS, was not inhibited by bulgecin A. The tetrameric L1 metallo-beta-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-beta-lactamases via the terminal sulphonate group on the sugar moiety.[1]

References

Bulgecin A: a novel inhibitor of binuclear metallo-beta-lactamases. Simm, A.M., Loveridge, E.J., Crosby, J., Avison, M.B., Walsh, T.R., Bennett, P.M. Biochem. J. (2005) [Pubmed]

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