Article
Importance of the His-298 residue in the catalytic mechanism of the Streptomyces R61 extracellular DD-peptidase.
The Biochemical journal - 1 Mar 1992
Hadonou A M, Jamin M, Adam M, Joris B, Dusart J, Ghuysen J M, Frère J M
Abstract excerpt
Among the active-site-serine penicillin-recognizing proteins, the Streptomyces R61 extracellular DD-peptidase is the only one to have a His-Thr-Gly sequence [instead of Lys-Thr(Ser)-Gly] in 'box' VII. The His residue was replaced by Gln or Lys. Both mutations induced a marked decrease in the rates of both tripeptide substrate hydrolysis and acylation by benzylpenicillin and cephalosporin C. The rate of hydrolysis...
Topics
- Amino Acid Sequence
- Catalysis
- Fluorescence
- Genetic Vectors
- Histidine
- Hot Temperature
- Kinetics
- Lactams
- Molecular Sequence Data
- Muramoylpentapeptide Carboxypeptidase
- Mutagenesis, Site-Directed