Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxy-peptidase-transpeptidase fromStreptomycesR61
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Reference10 articles.
1. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.
2. Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61
3. Kinetics of Interaction between the Exocellular DD-Carboxypeptidase-Transpeptidase from Streptomyces R61 and beta-Lactam Antibiotics. A Choice of Models
4. Interaction between the Exocellular DD-Carboxypeptidase-Transpeptidase from Streptomyces R61, Substrate and beta-Lactam Antibiotics. A Choice of Models
5. Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39
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