Abstract
In CTX-M-9 extended-spectrum beta-lactamases (ESBLs), an S130G mutation induced a 40- to 650-fold increase in 50% inhibitory concentrations but decreased hydrolytic activity against cefotaxime. A D240K mutation did not modify enzymatic efficiency against ceftazidime. Residue K240 could interact with Q270 and therefore not with ceftazidime, in contrast with what was observed with certain TEM/SHV-type ESBLs.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Substitution
-
Anti-Bacterial Agents / pharmacology
-
Cefotaxime / metabolism
-
Ceftazidime / pharmacology
-
Cephalosporins / pharmacology
-
Escherichia coli Proteins*
-
Hydrolysis
-
Kinetics
-
Models, Molecular
-
Molecular Conformation
-
Mutation / genetics
-
Mutation / physiology
-
Plasmids / genetics
-
beta-Lactamases / genetics*
-
beta-Lactamases / metabolism*
Substances
-
Anti-Bacterial Agents
-
Cephalosporins
-
Escherichia coli Proteins
-
Ceftazidime
-
CTX-M-9 protein, E coli
-
beta-Lactamases
-
Cefotaxime