Back to Search
Start Over
Interaction between class B beta-lactamases and suicide substrates of active-site serine beta-lactamases
- Source :
- FEBS letters. 443(2)
- Publication Year :
- 1999
-
Abstract
- The most widely used inactivators of active-site serine beta-lactamases behave as substrates of four class B metallo-beta-lactamases, but the efficiency of the catalytic process can vary by several orders of magnitude. A comparison of the kinetic parameters for the alpha and beta isomers of 6-iodopenicillanic acid shows that there is no general preference for the alpha isomer and that the efficient hydrolysis of imipenem by these enzymes must rest on other factors.
- Subjects :
- Imipenem
Tazobactam
Stereochemistry
Biophysics
Alpha (ethology)
Penicillanic Acid
Biochemistry
Catalysis
beta-Lactamases
Substrate Specificity
Serine
Isomerism
Structural Biology
Genetics
medicine
Binding site
Beta (finance)
Molecular Biology
Clavulanic Acid
chemistry.chemical_classification
6-β-Iodopenicillanic acid
Binding Sites
biology
Active site
Metallo-β-lactamase
Cell Biology
Orders of magnitude (mass)
Enzyme
chemistry
Sulbactam
biology.protein
medicine.drug
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 443
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....5a230a8896cbfe1eb938418ac3add50f