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DD-peptidases and beta-lactamases: catalytic mechanisms and specificities
- Source :
- Journal of chemotherapy (Florence, Italy). 7(1)
- Publication Year :
- 1995
-
Abstract
- DD-peptidases and beta-lactamases share several common properties, including the formation of an acylenzyme intermediate in their catalytic pathways. In their interactions with beta-lactam antibiotics, the stability of this intermediate is much higher with the peptidases than with the beta-lactamases. The structural factors responsible for this difference have not been identified. The evolution of beta-lactamases is taking place before our eyes, since mutants are constantly selected which can hydrolyze the molecules newly introduced as "beta-lactamase resistant" in the chemotherapeutic arsenal.
- Subjects :
- Pharmacology
chemistry.chemical_classification
Mutation
Protein Conformation
Mutant
Molecular Sequence Data
Biology
Muramoylpentapeptide Carboxypeptidase
Serine-Type D-Ala-D-Ala Carboxypeptidase
medicine.disease_cause
Catalysis
beta-Lactamases
Substrate Specificity
Muramoylpentapeptide carboxypeptidase
Infectious Diseases
Enzyme
Protein structure
Oncology
chemistry
Biochemistry
medicine
Pharmacology (medical)
Amino Acid Sequence
Peptide sequence
Antibacterial agent
Subjects
Details
- ISSN :
- 1120009X
- Volume :
- 7
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Journal of chemotherapy (Florence, Italy)
- Accession number :
- edsair.doi.dedup.....fbe3b0394b7669e22018b783798c5735