Sequence of active site peptides from the penicillin-sensitive D-alanine carboxypeptidase of Bacillus subtilis. Mechanism of penicillin action and sequence homology to beta-lactamases.

This publication has 35 references indexed in Scilit:

• Use of Model Enzymes in the Determination of the Mode of Action of Penicillins and Delta3-Cephalosporins
  Annual Review of Biochemistry, 1979
• Penicillinase active sites: Labelling of serine‐44 in β‐lactamase I by 6β‐bromopenicillanic acid
  FEBS Letters, 1979
• Crystallographic data for a penicillin receptor: Exocellular dd-carboxypeptidase-transpeptidase from Streptomyces R61
  Journal of Molecular Biology, 1979
• The Concept of the Penicillin Target from 1965 until Today: The Thirteenth Marjory Stephenson Memorial Lecture
  Journal of General Microbiology, 1977
• Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39
  Nature, 1975
• Fluorescamine: A Reagent for Assay of Amino Acids, Peptides, Proteins, and Primary Amines in the Picomole Range
  Science, 1972
• Biosynthesis of peptidoglycan by a cell wall preparation of Staphylococcus aureus and its inhibition by penicillin
  Biochemical and Biophysical Research Communications, 1972
• [6] Determination of cystine as cysteic acid
  Published by Elsevier ,1967
• Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.
  Proceedings of the National Academy of Sciences, 1965
• Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.
  Proceedings of the National Academy of Sciences, 1965