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Molecular and biochemical analysis of AST-1, a class A beta-lactamase from Nocardia asteroides sensu stricto.

ABSTRACT: A beta-lactamase gene was cloned from a Nocardia asteroides sensu stricto clinical isolate. A recombinant plasmid, pAST-1, expressed the beta-lactamase AST-1 in Escherichia coli JM109. Its pI was 4.8, and its relative molecular mass was 31 kDa. E. coli JM109(pAST-1) was resistant to penicillins and narrow-spectrum cephalosporins. The beta-lactamase AST-1 had a restricted hydrolytic activity spectrum. Its activity was partially inhibited by clavulanic acid but not by sulbactam and tazobactam. AST-1 is an Ambler class A beta-lactamase sharing 65% amino acid identity with beta-lactamase FAR-1, the most closely related enzyme.

SUBMITTER: Poirel L

PROVIDER: S-EPMC90387 | biostudies-literature | 2001 Mar

REPOSITORIES: biostudies-literature

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Molecular and biochemical analysis of AST-1, a class A beta-lactamase from Nocardia asteroides sensu stricto.

Poirel L L Laurent F F Naas T T Labia R R Boiron P P Nordmann P P

Antimicrobial agents and chemotherapy 20010301 3

A beta-lactamase gene was cloned from a Nocardia asteroides sensu stricto clinical isolate. A recombinant plasmid, pAST-1, expressed the beta-lactamase AST-1 in Escherichia coli JM109. Its pI was 4.8, and its relative molecular mass was 31 kDa. E. coli JM109(pAST-1) was resistant to penicillins and narrow-spectrum cephalosporins. The beta-lactamase AST-1 had a restricted hydrolytic activity spectrum. Its activity was partially inhibited by clavulanic acid but not by sulbactam and tazobactam. AST ...[more]

PMID: 11181374

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