TEM-E1: a novel beta-lactamase conferring resistance to ceftazidime.
A novel beta-lactamase, conferring resistance to ceftazidime, has been identified to be encoded by a 31 kb plasmid (pUK720) in a clinical E. coli strain isolated in Belgium. The beta-lactamase, new designated TEM-E1, has a pI of approximately 5.4 and lies in between the iso-electric focused bands of the beta-lactamases TEM-1 and TEM-7. The TEM-E1 beta-lactamase has a similar molecular weight of 22,000 to the TEM-1 and it is also inhibited by clavulanic acid. However, the TEM-E1 enzyme differs from TEM-1 by its low rates and efficiency of hydrolysis for ceftazidime and cefotaxime, TEM-E1 has similar efficiency of hydrolysis values for ceftazidime and cefotaxime, but only confers resistance to ceftazidime.
Payne
D J
DJ
Department of Bacteriology, Medical School, University of Edinburgh.
Marriott
M S
MS
Amyes
S G
SG
D002442:Ceftazidime / Q000378:metabolism / Q000494:pharmacology*; D003227:Conjugation, Genetic; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000201:enzymology; D007525:Isoelectric Focusing; D007700:Kinetics; D008826:Microbial Sensitivity Tests; D008970:Molecular Weight; D001618:beta-Lactamases / Q000032:analysis*
D002442:Ceftazidime; D001618:beta-Lactamases