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. 1997 Nov;41(11):2374–2382. doi: 10.1128/aac.41.11.2374

Characterization of a new TEM-derived beta-lactamase produced in a Serratia marcescens strain.

M Perilli 1, A Felici 1, N Franceschini 1, A De Santis 1, L Pagani 1, F Luzzaro 1, A Oratore 1, G M Rossolini 1, J R Knox 1, G Amicosante 1
PMCID: PMC164131  PMID: 9371336

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.

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Selected References

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