Properties of ß-lactamase from Neisseria gonorrhoeae

Castillo, Marta C. de; Sesma, Fernando; Nader, Olga M. de; Holgado, A. Pesce De Ruiz

doi:10.1590/s0074-02761998000200020

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Transcript Analysis Of Zmo01031

Storage Stability Of β-Lactamase1

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“…A similar characteristic profile for the b-lactamase of Neisseria gonorrhoeae was reported (De Castillo et al 1998). The presence of Ca 2?…”

Section: Transcript Analysis Of Zmo0103supporting

confidence: 80%

Functional characterization of a putative β-lactamase gene in the genome of Zymomonas mobilis

Rajnish¹,

Asraf²,

Manju³

et al. 2011

Biotechnol Lett

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Zymomonas mobilis ZM4 is resistant to β-lactam antibiotics but there are no reports of a β-lactam resistance gene and its regulation. A putative β-lactamase gene sequence (ZMO0103) in the genome of Z. mobilis showed a 55% amino acid sequence identity with class C β-lactamase genes. qPCR analysis of the β-lactamase transcript indicated a higher level expression of the β-lactamase compared to the relative transcript quantities in antibiotic-susceptible bacteria. The putative β-lactamase gene was cloned, expressed in Escherichia coli BL21 and the product, AmpC, was purified to homogeneity. Its optimal activity was at pH 6 and 30 °C. Further, the β-lactamase had a higher affinity towards penicillins than cephalosporin antibiotics.

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