Kızıl, GökselWilks, KathrynWells, DamienAla'Aldeen, Dlawer A.A.2024-04-242024-04-242000Kızıl, G., Wilks, K., Wells, D. ve Ala'Aldeen, D. A. A. (2000). Detection and characterisation of the genes encoding glyoxalase I and II from Neisseria meningitidis. Journal of Medical Microbiology, 49(7), 669-673.0022-2615https://doi.org/10.1099/0022-1317-49-7-669https://hdl.handle.net/11468/23492https://www.microbiologyresearch.org/content/journal/jmm/10.1099/0022-1317-49-7-669Glyoxalase 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 increased 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.eninfo:eu-repo/semantics/openAccessArticle4976696732-s2.0-00339233581088209310.1099/0022-1317-49-7-669Q2