Biochemical characterization of TEM-92 extended-spectrum β-lactamase, a protein differing from TEM-52 in the signal peptide

Mariagrazia Perilli, Bernardetta Segatore, Maria Rosaria De Massis, Laura Pagani, Francesco Luzzaro, Gian Maria Rossolini, Gianfranco Amicosante

Research output: Contribution to journalArticlepeer-review

Abstract

A blaTEM-92 gene was cloned from a Proteus mirabilis isolate and expressed in Escherichia coli. Production of the enzyme caused reduction of susceptibility to penicillins and narrow- to expanded-spectrum cephalosporins but not to moxalactam and cephamycins. Determination of kinetic parameters with the purified enzyme revealed hydrolysis of expanded-spectrum cephalosporins, while cephamycins, moxalactam, and aztreonam were very poorly or not hydrolyzed. Clavulanate and penicillanic acid sulfones acylated TEM-92 slowly, and deacylation occurred at measurable rates.

Original languageEnglish
Pages (from-to)3981-3983
Number of pages3
JournalAntimicrobial Agents and Chemotherapy
Volume46
Issue number12
DOIs
Publication statusPublished - Dec 1 2002

ASJC Scopus subject areas

  • Pharmacology (medical)

Fingerprint Dive into the research topics of 'Biochemical characterization of TEM-92 extended-spectrum β-lactamase, a protein differing from TEM-52 in the signal peptide'. Together they form a unique fingerprint.

Cite this