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      Genetic and biochemical characterization of a novel metallo-β-lactamase, TMB-1, from an Achromobacter xylosoxidans strain isolated in Tripoli, Libya.

      Antimicrobial Agents and Chemotherapy
      Achromobacter denitrificans, enzymology, genetics, isolation & purification, Amino Acid Sequence, Anti-Bacterial Agents, administration & dosage, therapeutic use, Carbapenems, Cephalosporins, Chromosomes, Bacterial, DNA, Bacterial, Gram-Negative Bacterial Infections, drug therapy, microbiology, Humans, Integrons, Kinetics, Libya, Microbial Sensitivity Tests, Molecular Sequence Data, Pseudomonas aeruginosa, Sequence Alignment, Sequence Homology, Amino Acid, beta-Lactamases, metabolism

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          Abstract

          An Achromobacter xylosoxidans strain from the Tripoli central hospital produced a unique metallo-β-lactamase, designated TMB-1, which is related to DIM-1 (62%) and GIM-1 (51%). bla(TMB-1) was embedded in a class 1 integron and located on the chromosome. The TMB-1 β-lactamase has lower k(cat) values than both DIM-1 and GIM-1 with cephalosporins and carbapenems. The K(m) values were more similar to those of GIM-1 than those of DIM-1, with the overall k(cat)/K(m) values being lower than those for GIM-1 and DIM-1.

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