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

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.

SUBMITTER: Perilli M

PROVIDER: S-EPMC164131 | biostudies-other | 1997 Nov

REPOSITORIES: biostudies-other

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

Perilli M M Felici A A Franceschini N N De Santis A A Pagani L L Luzzaro F F Oratore A A Rossolini G M GM Knox J R JR Amicosante G G

Antimicrobial agents and chemotherapy 19971101 11

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 ...[more]

PMID: 9371336

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