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Sequence of PSE-2 beta-lactamase.

P Huovinen1, S Huovinen, G A Jacoby

  • 1Massachusetts General Hospital, Boston 02114.

Antimicrobial Agents and Chemotherapy
|January 1, 1988
PubMed
Summary
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The nucleotide sequence of PSE-2 beta-lactamase was determined, revealing its structure and relation to other beta-lactamases. This enzyme efficiently breaks down carbenicillin and oxacillin.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Beta-lactamase enzymes are crucial in bacterial resistance to antibiotics.
  • Understanding beta-lactamase structure aids in developing new antibacterial strategies.
  • PSE-2 beta-lactamase exhibits broad-spectrum activity against penicillin-class antibiotics.

Purpose of the Study:

  • To determine the nucleotide sequence of the PSE-2 beta-lactamase enzyme.
  • To analyze the deduced amino acid sequence for structural and functional insights.
  • To compare PSE-2 beta-lactamase with other known beta-lactamases like OXA-2 and TEM-1.

Main Methods:

  • Nucleotide sequencing of the PSE-2 beta-lactamase gene.
  • Bioinformatic analysis to deduce the amino acid sequence.

Related Experiment Videos

  • Sequence alignment and comparison with related beta-lactamase enzymes.

    • Main Results:

    • The complete nucleotide sequence of PSE-2 beta-lactamase was elucidated.
    • The enzyme comprises 266 amino acids.
    • 93 amino acid residues were identical to OXA-2 beta-lactamase, and the active site contained the Ser-Thr-Phe-Lys tetrad, common to TEM-1 beta-lactamase.

    Conclusions:

    • The determined sequence provides a basis for understanding PSE-2 beta-lactamase's hydrolytic activity.
    • Structural similarities suggest conserved functional mechanisms among beta-lactamases.
    • This information is valuable for antibiotic resistance research and therapeutic development.