6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.
AUTOR(ES)
Pratt, R F
RESUMO
6-beta-Bromopenicillanic acid, which arises from the epimerization of 6-alpha-bromopenicillanic acid in aqueous solution or from hydrogenation of 6,6-dibromopenicillanic acid, is a powerful, irreversible, active-site-directed inhibitor of several typical beta-lactamases (penicillinase; penicillin amido-beta-lactamhydrolase, EC 3.5.2.6); 6-alpha-bromopenicillanic acid, being completely inhibited at less than micromolar concentrations through what is probably a 1:1 interaction. The B. licheniformis exoenzyme is similarly susceptible, while the Staphylococcus aureus enzyme and the Escherichia coli (R factor) enzyme are less so; the B. cereus beta-lactamase II is not inhibited. Very high concentrations (greater than or equal to 0.1 M) of benzylpenicillin, a good substrate, are required to significantly reduce the rate of inhibition of B. cereus beta-lactamase I by 6-beta-bromopenicillanic acid.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=336068Documentos Relacionados
- In vitro evaluation of BRL 42715, a novel beta-lactamase inhibitor.
- Activity of cefoperazone and two beta-lactamase inhibitors, sulbactam and clavulanic acid, against Bacteroides spp. correlated with beta-lactamase production.
- 6 beta-Iodopenicillanic acid (UI-38,006), a beta-lactamase inhibitor that extends the antibacterial spectrum of beta-lactam compounds: initial bacteriological characterization.
- Efficacy of a beta-lactamase inhibitor combination for serious intraabdominal infections.
- Plasmid-determined beta-lactamase indistinguishable from the chromosomal beta-lactamase of Escherichia coli.
