Hydroxylaminolysis of penicillin binding componenets is enzymatically catalyzed.

This publication has 26 references indexed in Scilit:

• Altered penicillin-binding components in penicillin-resistant mutants of Bacillus subtilis.
  Proceedings of the National Academy of Sciences, 1976
• The Catalytic Activity and Penicillin Sensitivity in the Liquid and Frozen States of Membrane‐Bound and Detergent‐Solubilised Transpeptidase of Streptomyces R61
  European Journal of Biochemistry, 1975
• Five Penicillin-binding Components Occur in Bacillus subtilis Membranes
  Journal of Biological Chemistry, 1972
• Isolation by Covalent Affinity Chromatography of the Penicillin-Binding Components from Membranes of Bacillus subtilis
  Proceedings of the National Academy of Sciences, 1972
• Facilitation of sodium borohyride reduction of esters of phenols and of acidic alcohols
  The Journal of Organic Chemistry, 1970
• Three-dimensional Structure of Tosyl-α-chymotrypsin
  Nature, 1967
• Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions.
  Proceedings of the National Academy of Sciences, 1966
• 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
• The Reduction of Esters with Sodium Borohydride¹
  The Journal of Organic Chemistry, 1963