Article
The catalytic mechanism of DD-peptidases: unexpected importance of tyrosine 280 in the transpeptidation reaction catalysed by the Streptomyces R61 DD-peptidase.
Cellular and molecular life sciences : CMLS - 1 Jul 1998
Wilkin J M, Lamotte-Brasseur J, Frère J M
Abstract excerpt
The study of the interactions between the Tyr280Phe mutant of the Streptomyces R61 DD-peptidase, various substrates and beta-lactam antibiotics shows that Tyr280 is involved not only in the formation of the acylenzyme with the peptide substrate and beta-lactam antibiotics, but also and specifical...
Topics
- Amino Acids
- Anti-Bacterial Agents
- Carboxypeptidases
- Catalysis
- Enzyme Stability
- Kinetics
- Lactams
- Mutation
- Peptidyl Transferases
- Protein Denaturation
- Recombinant Proteins
- Serine-Type D-Ala-D-Ala Carboxypeptidase
- Streptomyces