Open AccessTEM‐E1: a novel β‐lactamase conferring resistance to ceftazidime
Author(s) -
Payne D.J.,
Marriott M.S.,
Amyes S.G.B.
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03090.x
Subject(s) - ceftazidime , cefotaxime , clavulanic acid , microbiology and biotechnology , beta lactamase , plasmid , biology , bacteria , antibiotics , escherichia coli , biochemistry , dna , amoxicillin , genetics , gene , pseudomonas aeruginosa
A novel β‐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 β‐lactamase, new designated TEM‐E1, has a p I of approximately 5.4 and lies in between the iso‐electric focused bands of the β‐lactamases TEM‐1 and TEM‐7. The TEM‐E1 β‐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.