A new natural TEM derivative, named TEM-87, was identified in a Proteus mirabilis isolate from an Italian hospital. Compared to TEM-1, TEM-87 contains the following mutations: E104K, R164C, and M182T. Kinetic analysis of TEM-87 revealed extended-spectrum activity against oxyimino cephalosporins (preferentially ceftazidime) and aztreonam. Expression of blaTEM-87 in Escherichia coli decreased the host susceptibility to these drugs.
Perilli, M., Segatore, B., DE MASSIS, M.R., Franceschini, N., Bianchi, C., Rossolini, G.M., et al. (2002). Characterization of a new extended-spectrum beta-lactamase (TEM-87) isolated in Proteus mirabilis during an Italian survey. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 46(3), 925-928 [10.1128/AAC.46.3.925-928.2002].
Characterization of a new extended-spectrum beta-lactamase (TEM-87) isolated in Proteus mirabilis during an Italian survey
ROSSOLINI G. M.;
2002-01-01
Abstract
A new natural TEM derivative, named TEM-87, was identified in a Proteus mirabilis isolate from an Italian hospital. Compared to TEM-1, TEM-87 contains the following mutations: E104K, R164C, and M182T. Kinetic analysis of TEM-87 revealed extended-spectrum activity against oxyimino cephalosporins (preferentially ceftazidime) and aztreonam. Expression of blaTEM-87 in Escherichia coli decreased the host susceptibility to these drugs.
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https://hdl.handle.net/11365/8999
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