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Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor.
Metallo beta-lactamase enzymes confer antibiotic resistance to bacteria by catalyzing the hydrolysis of beta-lactam antibiotics. This relatively new form of resistance is spreading unchallenged asExpand
A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem.
One strategy developed by bacteria to resist the action of beta-lactam antibiotics is the expression of metallo-beta-lactamases. CphA from Aeromonas hydrophila is a member of a clinically importantExpand
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.
The 3-D structure of Bacillus cereus (569/H/9) beta-lactamase (EC, which catalyses the hydrolysis of nearly all beta-lactams, has been solved at 2.5 A resolution by the multiple isomorphousExpand
Chromosome-Encoded CTX-M-3 from Kluyvera ascorbata: a Possible Origin of Plasmid-Borne CTX-M-1-Derived Cefotaximases
ABSTRACT A gene identical to plasmid-borne blaCTX-M-3 is present in the chromosome of one Kluyvera ascorbata strain. It is associated with a structure including an inverted repeat right and an openExpand
β-Lactamase Inhibitors Derived from Single-Domain Antibody Fragments Elicited in the Camelidae
ABSTRACT Small, soluble single-domain fragments derived from the unique variable region of dromedary heavy-chain antibodies (VHHs) against enzymes are known to be potent inhibitors. The immunizationExpand
Biochemical Characterization of the Pseudomonas aeruginosa 101/1477 Metallo-β-Lactamase IMP-1 Produced byEscherichia coli
ABSTRACT The blaIMP gene coding for the IMP-1 metallo-β-lactamase produced by a Pseudomonas aeruginosaclinical isolate (isolate 101/1477) was overexpressed via a T7 expression system in EscherichiaExpand
Structure of In31, ablaIMP-Containing Pseudomonas aeruginosa Integron Phyletically Related to In5, Which Carries an Unusual Array of Gene Cassettes
ABSTRACT The location and environment of the acquiredblaIMP gene, which encodes the IMP-1 metallo-β-lactamase, were investigated in a JapanesePseudomonas aeruginosa clinical isolate (isolateExpand
Standard Numbering Scheme for Class B β-Lactamases
Unlike for classes A and B, a standardized amino acid numbering scheme has not been proposed for the class C (AmpC) β-lactamases, which complicates communication in the field. Here, we propose aExpand
Metallo-beta-lactamases as emerging resistance determinants in Gram-negative pathogens: open issues.
The rapid spread of acquired metallo-beta-lactamases (MBLs) among major Gram-negative pathogens is a matter of particular concern worldwide and primarily in Europe, one of first continents where theExpand
Analysis of the importance of the metallo-beta-lactamase active site loop in substrate binding and catalysis.
The role of the mobile loop comprising residues 60-66 in metallo-beta-lactamases has been studied by site-directed mutagenesis, determination of kinetic parameters for six substrates and twoExpand