Molecular structures of penicillin-binding proteins and beta-lactamases

Trends Microbiol. 1994 Oct;2(10):372-80. doi: 10.1016/0966-842x(94)90614-9.

Abstract

In the past, new antibacterial agents have been selected either from natural sources or by 'trial and error' modification of existing antibacterials. Future therapeutic strategies are likely to depend on increased knowledge of existing drug targets and the search for new targets. The machinery for the assembly of bacterial-cell-wall peptidoglycan is an ideal place to look.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / chemical synthesis*
  • Bacterial Proteins*
  • Biological Evolution
  • Carrier Proteins / chemistry*
  • Carrier Proteins / physiology
  • Drug Design
  • Hexosyltransferases*
  • Molecular Sequence Data
  • Molecular Weight
  • Muramoylpentapeptide Carboxypeptidase / chemistry*
  • Muramoylpentapeptide Carboxypeptidase / physiology
  • Penicillin-Binding Proteins
  • Peptidoglycan / biosynthesis
  • Peptidyl Transferases*
  • Protein Conformation
  • beta-Lactamases / chemistry*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Carrier Proteins
  • Penicillin-Binding Proteins
  • Peptidoglycan
  • Peptidyl Transferases
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase
  • beta-Lactamases