Moreno Galleni

TL;DR: The 3‐D structure of Bacillus cereus (569/H/9) beta‐lactamase (EC 3.5.6) has been solved and an approximate internal molecular symmetry is found, with a 2‐fold axis passing roughly through the zinc ion and suggesting a possible gene duplication.

TL;DR: A unique mode of binding of the mercaptocarboxylate inhibitor in the enzyme active site provides a binding model for metallo beta-lactamase inhibition with utility for future drug design.

TL;DR: The blaIMP gene coding for the IMP-1 metallo-β-lactamase produced by a Pseudomonas aeruginosaclinical isolate was overexpressed via a T7 expression system in Escherichia coli BL21(DE3), and its product was purified to homogeneity with a final yield of 35 mg/liter of culture.

TL;DR: The possible mechanisms of action for the class B beta-lactamase are discussed, and it is concluded that zinc(II) acts as a Lewis acid to stabilize the dianionic form of the tetrahedral intermediate and to provide a hydroxide-ion bound nucleophile, whereas the carboxylate anion of Asp-90 acts as the general acid catalyst facilitating C-N bond fission.

TL;DR: The location and environment of the acquiredblaIMP gene, which encodes the IMP-1 metallo-β-lactamase, were investigated in a JapanesePseudomonas aeruginosa clinical isolate that produced the enzyme.