Microbial glyoxalase enzymes: metalloenzymes controlling cellular levels of methylglyoxal.
The glyoxalase system consists of two enzymes, glyoxalase I and glyoxalase II. This system is important in the detoxification of methylglyoxal. Detailed studies have determined that the glyoxalase I from Escherichia coli, Neisseria meningitidis and Yersinia pestis are maximally activated by Ni2+ and Co2+, and are inactive with Zn2+, a situation quite different from the human glyoxalase I enzyme, which is activated by Zn2+. Recent studies on the Pseudomonas aeruginosa genome have led to the characterization of three different glyoxalase I enzymes, two of which follow a Ni2+/Co2+ activation profile and the third exhibits a human-like preference for Zn2+.
Department of Chemistry, University of Waterloo, 200 University Avenue, Waterloo, Ontario N2L 3G1, Canada.
Nicole
N
Sukdeo
John F
JF
Honek
D000595:Amino Acid Sequence; D000818:Animals; D004926:Escherichia coli / Q000201:enzymology; D006801:Humans; D007791:Lactoylglutathione Lyase / Q000235:genetics / Q000502:physiology*; D008969:Molecular Sequence Data; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D011765:Pyruvaldehyde / Q000378:metabolism*; D016415:Sequence Alignment; D013045:Species Specificity; D013869:Thiolester Hydrolases / Q000235:genetics / Q000502:physiology*; D000099301:Hydroxyacylglutathione Hydrolase
D007791:Lactoylglutathione Lyase; D011765:Pyruvaldehyde; D013869:Thiolester Hydrolases; D000099301:Hydroxyacylglutathione Hydrolase