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Detection and characterisation of the genes encoding glyoxalase I and II from Neisseria meningitidis

Meningococcal Research Group, Divisions of Microbiology, School of Clinical Laboratory Sciences, University of Nottingham Faculty of Medicine and Health Sciences, University Hospital, Nottingham NG7 2UH

Corresponding author: Dr D. A. A. Ala'Aldeen (e-mail: daa{at}nottingham.ac.uk).

Received 4 Sept. 1999; revised version received 20 Nov. 1999; accepted 25 Nov. 1999.

Abstract

Glyoxalase enzymes I and II are involved in a detoxification process consisting of conversion of reactive dicarbonyl compounds (e.g., methylglyoxal) to less reactive hydroxy acids. The structural gene for meningococcal glyoxalase I (gloA) was identified by screening an expression library with a rabbit antiserum. The meningococcal gloA gene consisted of 138 deduced amino acids, with a calculated mol. wt of 15.7 kDa. The DNA and deduced protein sequence of gloA was compared to known sequences of glyoxalase I enzymes and showed high homology with gloA of several eukaryotic and prokaryotic species. Insertion of a gloA-containing plasmid in Escherichia coli increa-sed the host organism's tolerance to methylglyoxal from <2 mM to >4 mM, thus demonstrating its functional identity. A databank search also revealed the presence of a putative gloB gene, encoding glyoxalase II (GlxII), in the recently released genomic sequences of Neisseria meningitidis and N. gonorrhoeae.

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