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Isolation and expression of a novel molecular class D beta-lactamase, OXA-61, from Campylobacter jejuni.

ABSTRACT: A novel beta-lactamase gene, blaOXA-61, from Campylobacter jejuni GC015 was cloned and its nucleotide sequence determined. blaOXA-61 encodes a protein of 257 amino acids in which the active-site STFK tetrad and conserved class D beta-lactamase motifs YGN and KTG were identified. A conserved sequence upstream of blaOXA-61 is required for expression in Campylobacter.

SUBMITTER: Alfredson DA 

PROVIDER: S-EPMC1140520 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature

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Isolation and expression of a novel molecular class D beta-lactamase, OXA-61, from Campylobacter jejuni.

Alfredson David A DA   Korolik Victoria V  

Antimicrobial agents and chemotherapy 20050601 6

A novel beta-lactamase gene, blaOXA-61, from Campylobacter jejuni GC015 was cloned and its nucleotide sequence determined. blaOXA-61 encodes a protein of 257 amino acids in which the active-site STFK tetrad and conserved class D beta-lactamase motifs YGN and KTG were identified. A conserved sequence upstream of blaOXA-61 is required for expression in Campylobacter. ...[more]

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