NMR evidence for the structure of the complex between penicillin and the DD‐carboxypeptidase of streptomyces R61
- 1 February 1979
- journal article
- Published by Wiley in FEBS Letters
- Vol. 98 (1) , 53-56
- https://doi.org/10.1016/0014-5793(79)80150-7
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
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- Occurrence of a serine residue in the penicillin‐binding site of the exocellular DD‐carboxy‐peptidase‐transpeptidase from Streptomyces R61FEBS Letters, 1976
- Determination of the configuration of the four D-benzylpenicilloatesThe Journal of Organic Chemistry, 1976
- Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61Nature, 1976
- Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39Nature, 1975
- Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from Bacillus stearothermophilus.Proceedings of the National Academy of Sciences, 1975
- Interaction between the Exocellular DD‐Carboxypeptidase‐Transpeptidase from Streptomyces R61, Substrate and β‐Lactam AntibioticsEuropean Journal of Biochemistry, 1975
- Kinetics of Interaction between the Exocellular DD‐Carboxypeptidase‐Transpeptidase from Streptomyces R61 and β‐Lactam AntibioticsEuropean Journal of Biochemistry, 1975
- Molecular weight and amino acid composition of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R61Biochemical Journal, 1973