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beta-Lactamases: quality and resistance.

Antone A. Medeiros1

  • 1Division of Biology and Medicine, Brown University, Providence, Rhode Island, USA.

Clinical Microbiology and Infection : the Official Publication of the European Society of Clinical Microbiology and Infectious Diseases
|February 1, 1997
PubMed
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Beta-lactamase enzymes cause resistance to beta-lactam antibiotics. This review covers beta-lactamase classification, serine beta-lactamase structure, and how mutations extend their hydrolysis profiles, impacting clinical treatment.

Area of Science:

  • Microbiology
  • Biochemistry
  • Pharmacology

Background:

  • Beta-lactamase enzymes are crucial for bacterial resistance to beta-lactam antibiotics.
  • These enzymes hydrolyze beta-lactam antibiotics, diminishing their therapeutic efficacy.
  • Serine beta-lactamases are the most prevalent class in clinical settings.

Purpose of the Study:

  • To review the molecular classification of beta-lactamases.
  • To describe the structure of the serine beta-lactamase active site.
  • To discuss mechanisms of beta-lactamase production and spread, including mutations.

Main Methods:

  • Literature review of beta-lactamase classification and structure.
  • Analysis of mechanisms for beta-lactamase production deregulation.

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  • Examination of clinical spread and mutational impacts on hydrolysis profiles.

    • Main Results:

    • Beta-lactamases are classified based on their active site composition (serine or zinc).
    • Serine beta-lactamases exhibit diverse structures and mechanisms of action.
    • Mutations can significantly alter the substrate specificity and hydrolysis capabilities of serine beta-lactamases.

    Conclusions:

    • Understanding beta-lactamase diversity and mechanisms is vital for combating antibiotic resistance.
    • The spread of beta-lactamases and adaptive mutations pose significant clinical challenges.
    • Further research into beta-lactamase inhibitors and novel therapeutic strategies is warranted.