Biochemical Properties of Neisseria gonorrhoeae LgtE

1 Biochemical properties of Neisseria gonorrhoeae LgtE

Biochemical properties of Neisseria gonorrhoeae LgtE.

A fragment of chromosomal DNA encoding the lgtE gene of Neisseria gonorrhoeae strain F62 was amplified by PCR and cloned into the expression vector pET15b. Functional LgtE was purified and its biochemical properties were determined. The purified enzyme was maximally active in buffer containing manganese; minimal activity was obtained in buffer containing other divalent cations. LgtE was only ab...

Properties of ß-lactamase from Neisseria gonorrhoeae

ß-lactamase activity was studied in Neisseria gonorrhoeae strains. Optimum temperature was found to be 37°C. The enzyme was inactivated at temperatures higher than 60°C, but remained active during storage at low temperatures (4°C, -30°C and -70°C) for two months. Enzyme activity was observed within a pH range of 5.8-8.0, while the optimum pH was 7.0-7.2. Addition of Ni2+, Fe2+, Fe3+, Mn2+ and p...

Neisseria gonorrhoeae

Two fi-lactamase-producing strains of Neisseria gonorrhoeae were studied. The substrate profile, molecular weight, and isoelectric point of their ,8-lactamases were similar to those of the TEM-1 enzyme produced by many gram-negative bacilli. The gonococcal f8-lactamase was cell bound during exponential growth and was most likely located in the periplasm. Penicillin hydrolysis was efficient in i...

Neisseria gonorrhoeae

Expression of Type IV pili by the bacteria! pathogen Neisseria gonorrhoeae appears to be essential for colonization of the human host. Several N. gonorrhoeae gene products have been recently identified which bear homology to proteins invoived in pilus assembly and protein export in other bacterial systems. We report here the isolation and characterization of transposon insertion mutants in N. g...