Detection and characterisation of the genes encoding glyoxalase I and II from Neisseria meningitidis.
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 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.
Kizil
Goksel
G
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.
Wilks
Kathy
K
Wells
D
D
Ala'aldeen
D A A
DAA
D000595:Amino Acid Sequence; D005798:Genes, Bacterial; D015698:Genomic Library; D007791:Lactoylglutathione Lyase / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000201:enzymology / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D013869:Thiolester Hydrolases / Q000235:genetics* / Q000302:isolation & purification; D000099301:Hydroxyacylglutathione Hydrolase
D007791:Lactoylglutathione Lyase; D013869:Thiolester Hydrolases; D000099301:Hydroxyacylglutathione Hydrolase