Hydroxylaminolysis of penicillin binding componenets is enzymatically catalyzed.
Open Access
- 1 November 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (21), 7525-7529
- https://doi.org/10.1016/s0021-9258(17)40998-7
Abstract
No abstract availableThis 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 R61European Journal of Biochemistry, 1975
- Five Penicillin-binding Components Occur in Bacillus subtilis MembranesJournal of Biological Chemistry, 1972
- Isolation by Covalent Affinity Chromatography of the Penicillin-Binding Components from Membranes of Bacillus subtilisProceedings of the National Academy of Sciences, 1972
- Facilitation of sodium borohyride reduction of esters of phenols and of acidic alcoholsThe Journal of Organic Chemistry, 1970
- Three-dimensional Structure of Tosyl-α-chymotrypsinNature, 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 Borohydride1The Journal of Organic Chemistry, 1963