Back to Search
Start Over
Nuances of Mechanisms and Their Implications for Evolution of the Versatile β-Lactamase Activity: From Biosynthetic Enzymes to Drug Resistance Factors
- Source :
- Journal of the American Chemical Society. 119:7619-7625
- Publication Year :
- 1997
- Publisher :
- American Chemical Society (ACS), 1997.
-
Abstract
- β-Lactamases of classes A and C are believed to have evolved from bacterial enzymes involved in biosynthesis of the peptidoglycan, the so-called penicillin-binding proteins. All these enzymes undergo acylation at an active-site serine by β-lactam antibiotics as a common feature. However, the fate of the acyl-enzyme species is different for β-lactamases and penicillin-binding proteins; deacylation is rapid for the former, whereas it is slow for the latter. It is believed that the acquisition of the ability to deacylate the acyl-enzyme intermediate led to the evolution of β-lactamase activity, which is indispensable for the survival of bacteria in the face of challenge by β-lactam antibiotics. The mechanisms of deacylation of acyl-enzyme intermediates for β-lactamases are examined as a means to investigate structural factors in evolutionary descendency of classes A and C of β-lactamases from penicillin-binding proteins. It is known that in class A β-lactamases the hydrolytic water approaches the acyl-enzyme...
- Subjects :
- chemistry.chemical_classification
biology
medicine.drug_class
Antibiotics
General Chemistry
Drug resistance
biology.organism_classification
Biochemistry
Catalysis
Serine
Acylation
chemistry.chemical_compound
Colloid and Surface Chemistry
Enzyme
Biosynthesis
chemistry
medicine
Peptidoglycan
Bacteria
Subjects
Details
- ISSN :
- 15205126 and 00027863
- Volume :
- 119
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi...........5be1ec87381646a377e42718e568fbb2