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Primary structure of OXA-3 and phylogeny of oxacillin-hydrolyzing class D beta-lactamases.

ABSTRACT: We determined the nucleotide sequence of the blaOXA-3(pMG25) gene from Pseudomonas aeruginosa. The bla structural gene encoded a protein of 275 amino acids representing one monomer of 31,879 Da for the OXA-3 enzyme. Comparisons between the OXA-3 nucleotide and amino acid sequences and those of class A, B, C, and D beta-lactamases were performed. An alignment of the eight known class D beta-lactamases including OXA-3 demonstrated the presence of conserved amino acids. In addition, conserved motifs composed of identical amino acids typical of penicillin-recognizing proteins and specific class D motifs were identified. These conserved motifs were considered for possible roles in the structure and function of oxacillinases. On the basis of the alignment and identity scores, a dendrogram was constructed. The phylogenetic data obtained revealed five groups of class D beta-lactamases with large evolutionary distances between each group.

SUBMITTER: Sanschagrin F

PROVIDER: S-EPMC162648 | biostudies-other | 1995 Apr

REPOSITORIES: biostudies-other

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Primary structure of OXA-3 and phylogeny of oxacillin-hydrolyzing class D beta-lactamases.

Sanschagrin F F Couture F F Levesque R C RC

Antimicrobial agents and chemotherapy 19950401 4

We determined the nucleotide sequence of the blaOXA-3(pMG25) gene from Pseudomonas aeruginosa. The bla structural gene encoded a protein of 275 amino acids representing one monomer of 31,879 Da for the OXA-3 enzyme. Comparisons between the OXA-3 nucleotide and amino acid sequences and those of class A, B, C, and D beta-lactamases were performed. An alignment of the eight known class D beta-lactamases including OXA-3 demonstrated the presence of conserved amino acids. In addition, conserved motif ...[more]

PMID: 7785990

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