Penicillin binding proteins: role in initiation of murein synthesis in Escherichia coli.
Article Details
- CitationCopy to clipboard
de la Rosa EJ, de Pedro MA, Vazquez D
Penicillin binding proteins: role in initiation of murein synthesis in Escherichia coli.
Proc Natl Acad Sci U S A. 1985 Sep;82(17):5632-5.
- PubMed ID
- 3898066 [ View in PubMed]
- Abstract
The consequences of the specific inhibition of penicillin binding proteins (Pbps) by beta-lactam antibiotics immediately before resumption of active growth in Escherichia coli suggest that inhibition of murein biosynthesis does not prevent the earlier steps of the initiation of cell growth in mass. The activity of Pbp 2 is apparently critical for the initiation of murein biosynthesis. Provided that Pbp 2 remains active, the other Pbps (1a, 1b, 3, 4, 5, and 6) can be inhibited without any noticeable effect on the initial rate of incorporation of new precursors into macromolecular peptidoglycan. These precursors are, in addition, inserted with a high degree of cross-linkage.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Cefmetazole D-alanyl-D-alanine carboxypeptidase DacA Protein Escherichia coli (strain K12) YesInhibitorDetails Cefmetazole D-alanyl-D-alanine carboxypeptidase DacC Protein Escherichia coli (strain K12) YesInhibitorDetails Cefmetazole Penicillin-binding protein 1A Protein Escherichia coli (strain K12) YesInhibitorDetails Cefmetazole Penicillin-binding protein 1B Protein Escherichia coli (strain K12) YesInhibitorDetails Cefmetazole Peptidoglycan synthase FtsI Protein Escherichia coli (strain K12) YesInhibitorDetails