Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39
- 1 November 1975
- journal article
- Published by Springer Nature in Nature
- Vol. 258 (5531), 168-170
- https://doi.org/10.1038/258168a0
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
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- Molecular weight, amino acid composition and physicochemical properties of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R39Biochemical Journal, 1974
- Binding of β-lactam antibiotics to the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R39Biochemical Journal, 1974
- Molecular weight and amino acid composition of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R61Biochemical Journal, 1973
- Degradation of penicillin G methyl ester with trifluoroacetic acidThe Journal of Organic Chemistry, 1972
- Binding of14C-penicillin G toProteus mirabilisArchiv für Mikrobiologie, 1972
- 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