Characterization of a new TEM-derived beta-lactamase produced in a Serratia marcescens strain
Year: 1997
Type: article
Abstract: A natural TEM variant beta-lactamase was isolated from an epidemic strain of Serratia marcescens. Nucleotide gene sequencing revealed multiple point mutations located in the 42-to-44 tripeptide and positions 145 to 146, 178, and 238. In addition, a glutamic acid 212 deletion was also found. The purified enzyme was studied from a kinetic point of view, revealing the highest catalytic efficiency (k[cat]/Km) values for ceftazidime and aztreonam compared with the TEM-1 prototype enzyme. The in vitro resistance correlated with kinetic parameters, and the enzyme also mediated resistance to some penicillins and an ampicillin-clavulanic acid combination. The mutational and kinetic changes are discussed in relation to the three-dimensional crystallographic structure of the wild-type TEM-1 enzyme.
Authors: M Perilli, A Felici, N Franceschini, A De Santis, L Pagani, F Luzzaro, A Oratore, G M Rossolini, J R Knox, G Amicosante
Institution: University of L'Aquila
Language: English
Subfield: Molecular Medicine
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2106900216