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

Mariagrazia Perilli | Zendy; Antonio Felici | Zendy; Nicola Franceschini | Zendy; Augusta De Santis | Zendy; Laura Pagani | Zendy; Francesco Luzzaro | Zendy; A Oratore | Zendy; Gian María Rossolini | Zendy; James R. Knox | Zendy; Gianfranco Amicosante | Zendy

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

Author(s) -

Mariagrazia Perilli,

Antonio Felici,

Nicola Franceschini,

Augusta De Santis,

Laura Pagani,

Francesco Luzzaro,

A Oratore,

Gian María Rossolini,

James R. Knox,

Gianfranco Amicosante

Publication year - 1997

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.41.11.2374

Subject(s) - aztreonam , serratia marcescens , ceftazidime , clavulanic acid , enzyme , microbiology and biotechnology , amp resistance , strain (injury) , point mutation , biology , cefotaxime , tripeptide , enzyme kinetics , chemistry , ampicillin , bacteria , biochemistry , escherichia coli , antibiotics , amino acid , gene , genetics , mutation , active site , amoxicillin , anatomy , pseudomonas aeruginosa

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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