Role of zinc content on the catalytic efficiency of B1 metallo beta-lactamases
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Metallo-beta-lactamases (MbetaLs) are zinc-dependent enzymes able to hydrolyze and inactivate most beta-lactam antibiotics. The large diversity of active site structures and metal content among MbetaLs from different sources has limited the design of a pan ...
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Metallo-β-lactamases (MβLs) constitute an increasingly serious clinical threat by giving rise to β-lactam antibiotic resistance. They accommodate in their catalytic pocket one or two zinc ions, which are responsible for the hydrolysis of β-lactams. Recent ...
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Histone deacetylases (HDACs) constitute an important family of zinc-dependent enzymes responsible for catalyzing the cleavage of acetyl groups from acetyl-lysine residues in histone N-terminal tails. HDACs can potentially play a key role treating various c ...
A review on various methods for the selection of catalysts using phage display. The different approaches (selection of catalysts by binding and direct selections for catalytic activity) are presented. Metallo-beta -lactamase BCII from Bacillus cereus was u ...
Hybrid Car-Parrinello QM/MM calcns. are used to investigate the reaction mechanism of hydrolysis of a common b-lactam substrate (cefotaxime) by the monozinc b-lactamase from Bacillus cereus (BcII). The calcns. suggest a fundamental role for an active site ...
