Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12.
Article Details
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Rake JB, Newman DJ, Actor P
Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12.
J Antibiot (Tokyo). 1984 May;37(5):572-6.
- PubMed ID
- 6376452 [ View in PubMed]
- Abstract
The binding of cefonicid (SK&F 75073), a new parenteral cephalosporin, to the penicillin-binding proteins (PBPs) of Escherichia coli K-12 (strain KN-126) was determined by competitive binding studies versus benzyl[14C]penicillin. Cefonicid showed its greatest affinity for PBPs 1a greater than 3 greater than 1b, bound with low affinity to PBPs 4 greater than 2, and did not bind to PBPs 5 and 6. Provisional affinity constants (cefonicid concentration that gave 50% inhibition of [14C]penicillin binding) were determined: PBP 1a, less than 0.25 microgram/ml; PBP 3, 0.7 microgram/ml; PBP 1b, 10 micrograms/ml; PBP 4, 26 micrograms/ml; PBP 2, 90 micrograms/ml; PBPs 5 and 6 greater than 256 micrograms/ml. Direct binding studies with [14C]-cefonicid confirmed this pattern of binding. Subinhibitory concentrations of cefonicid (MIC, broth 0.2 microgram/ml, agar 0.4 microgram/ml) induced filamentation of E. coli KN-126. This implies that PBP 3 is the primary inhibitory site despite the higher affinity of PBP 1a for this cephalosporin.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Cefonicid D-alanyl-D-alanine carboxypeptidase DacB Protein Escherichia coli (strain K12) YesInhibitorDetails Cefonicid Penicillin-binding protein 1A Protein Escherichia coli (strain K12) YesInhibitorDetails Cefonicid Penicillin-binding protein 1B Protein Escherichia coli (strain K12) YesInhibitorDetails Cefonicid Penicillin-binding protein 2 Protein Escherichia coli (strain K12) YesInhibitorDetails Cefonicid Peptidoglycan synthase FtsI Protein Escherichia coli (strain K12) YesInhibitorDetails