Bacterial glyoxalase enzymes

Seminars in Cell and Developmental Biology

Volumn 22, Issue 3, 2011, Pages 285-292

  Suttisansanee, Uthaiwan ^a   Honek, John F ^a  

^a UNIVERSITY OF WATERLOO   (Canada)

Author keywords

Bacteria; Clostridium; Escherichia coli; Glyoxalase; Metalloenzyme; Nickel; Zinc

Indexed keywords

BACTERIAL ENZYME; COBALT; GLYOXALASE; HYDROXYACYLGLUTATHIONE HYDROLASE; LACTOYLGLUTATHIONE LYASE; METHYLGLYOXAL; NICKEL; ZINC ION;

CATALYSIS; CATALYST; CLOSTRIDIUM ACETOBUTYLICUM; DETOXIFICATION; ESCHERICHIA COLI; NEISSERIA MENINGITIDIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN STRUCTURE; PSEUDOMONAS PUTIDA; REVIEW; STRUCTURE ACTIVITY RELATION; YERSINIA PESTIS;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM; ESCHERICHIA COLI;

EID: 79955962028     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2011.02.004     Document Type: Review

References (54)

1. Sukdeo N., Honek J.F. Microbial glyoxalase enzymes: metalloenzymes controlling cellular levels of methylglyoxal. Drug Metabol Drug Interact 2008, 23:29-50.
2. MacLean M.J., Ness L.S., Ferguson G.P., Booth I.R. The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli. Mol Microbiol 1998, 27:563-571.
3. Newton G.L., Fahey R.C. Determination of biothiols by bromobimane labeling and high-performance liquid chromatography. Methods Enzymol 1995, 251:148-166.
4. Fahey R.C., Brown W.C., Adams W.B., Worsham M.B. Occurrence of glutathione in bacteria. J Bacteriol 1978, 133:1126-1129.
5. Meister A. Glutathione biosynthesis and its inhibition. Methods Enzymol 1995, 252:26-30.
6. Newton G.L., Arnold K., Price M.S., Sherrill C., Delcardayre S.B., Aharonowitz Y., et al. Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes. J Bacteriol 1996, 178:1990-1995.
7. Hand C.E., Honek J.F. Biological chemistry of naturally occurring thiols of microbial and marine origin. J Nat Prod 2005, 68:293-308.
8. Hand C.E., Auzanneau F.I., Honek J.F. Conformational analyses of mycothiol, a critical intracellular glycothiol in Mycobacteria. Carbohydr Res 2006, 341:1164-1173.
9. Aronsson A.C., Marmstal E., Mannervik B. Glyoxalase I, a zinc metalloenzyme of mammals and yeast. Biochem Biophys Res Commun 1978, 81:1235-1240.
10. Saint-Jean A.P., Phillips K.R., Creighton D.J., Stone M.J. Active monomeric and dimeric forms of Pseudomonas putida glyoxalase I: evidence for 3D domain swapping. Biochemistry 1998, 37:10345-10353.
11. Clugston S.L., Barnard J.F., Kinach R., Miedema D., Ruman R., Daub E., et al. Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: evidence for optimal activation by nickel ions. Biochemistry 1998, 37:8754-8763.
12. Sukdeo N., Clugston S.L., Daub E., Honek J.F. Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes. Biochem J 2004, 384:111-117.
13. Kizil G., Wilks K., Wells D., Ala'Aldeen D.A. Detection and characterisation of the genes encoding glyoxalase I and II from Neisseria meningitidis. J Med Microbiol 2000, 49:669-673.
14. Vickers T.J., Greig N., Fairlamb A.H. A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major. Proc Natl Acad Sci USA 2004, 101:13186-13191.
15. Rhee H., Murata K., Kimura A. Purification and characterization of glyoxalase I from Pseudomonas putida. Biochem Biophys Res Commun 1986, 141:993-999.
16. Sukdeo N., Honek J.F. Pseudomonas aeruginosa contains multiple glyoxalase I-encoding genes from both metal activation classes. Biochim Biophys Acta 2007, 1774:756-763.
17. Cameron A.D., Olin B., Ridderstrom M., Mannervik B., Jones T.A. Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping. EMBO J 1997, 16:3386-3395.
18. Feierberg I., Cameron A.D., Aqvist J. Energetics of the proposed rate-determining step of the glyoxalase I reaction. FEBS Lett 1999, 453:90-94.
19. Bergdoll M., Eltis L.D., Cameron A.D., Dumas P., Bolin J.T. All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly. Protein Sci 1998, 7:1661-1670.
20. Deponte M., Sturm N., Mittler S., Harner M., Mack H., Becker K. Allosteric coupling of two different functional active sites in monomeric Plasmodium falciparum glyoxalase I. J Biol Chem 2007, 282:28419-28430.
21. He M.M., Clugston S.L., Honek J.F., Matthews B.W. Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation. Biochemistry 2000, 39:8719-8727.
22. Davidson G., Clugston S.L., Honek J.F., Maroney M.J. XAS investigation of the nickel active site structure in Escherichia coli glyoxalase I. Inorg Chem 2000, 39:2962-2963.
23. Cameron A.D., Ridderstrom M., Olin B., Kavarana M.J., Creighton D.J., Mannervik B. Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue. Biochemistry 1999, 38:13480-13490.
24. Ly H.D., Clugston S.L., Sampson P.B., Honek J.F. Syntheses and kinetic evaluation of hydroxamate-based peptide inhibitors of glyoxalase I. Bioorg Med Chem Lett 1998, 8:705-710.
25. Clugston S.L., Yajima R., Honek J.F. Investigation of metal binding and activation of Escherichia coli glyoxalase I: kinetic, thermodynamic and mutagenesis studies. Biochem J 2004, 377:309-316.
26. Su Z., Sukdeo N., Honek J.F. 15N-1H NMR HSQC evidence for distinct specificity of two active sites in Escherichia coli glyoxalase I. Biochemistry 2008, 47:13232-13241.
27. Ridderstrom M., Cameron A.D., Jones T.A., Mannervik B. Mutagenesis of residue 157 in the active site of human glyoxalase I. Biochem J 1997, 328(Pt. 1):231-235.
28. Armstrong R.N. Mechanistic diversity in a metalloenzyme superfamily. Biochemistry 2000, 39:13625-13632.
29. Alfredson D.A., Korolik V. Identification of putative zinc hydrolase genes of the metallo-beta-lactamase superfamily from Campylobacter jejuni. FEMS Immunol Med Microbiol 2007, 49:159-164.
30. O'Young J., Sukdeo N., Honek J.F. Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme. Arch Biochem Biophys 2007, 459:20-26.
31. Campos-Bermudez V.A., Leite N.R., Krog R., Costa-Filho A.J., Soncini F.C., Oliva G., et al. Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: new insights into metal ion selectivity. Biochemistry 2007, 46:11069-11079.
32. Stamp A.L., Owen P., Omari K.E., Nichols C.E., Lockyer M., Lamb H.K., et al. Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: an unusual Type II glyoxalase. Protein Sci 2010, 19:1897-1905.
33. Principato G.B., Rosi G., Talesa V., Giovannini E., Uotila L. Purification and characterization of two forms of glyoxalase II from the liver and brain of Wistar rats. Biochim Biophys Acta 1987, 911:349-355.
34. Talesa V., Uotila L., Koivusalo M., Principato G., Giovannini E., Rosi G. Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms. Biochim Biophys Acta 1988, 955:103-110.
35. Talesa V., Uotila L., Koivusalo M., Principato G., Giovannini E., Rosi G. Isolation of glyoxalase II from two different compartments of rat liver mitochondria. Kinetic and immunochemical characterization of the enzymes. Biochim Biophys Acta 1989, 993:7-11.
36. Talesa V., Principato G.B., Norton S.J., Contenti S., Mangiabene C., Rosi G. Isolation of glyoxalase II from bovine liver mitochondria. Biochem Int 1990, 20:53-58.
37. Talesa V., Rosi G., Contenti S., Mangiabene C., Lupattelli M., Norton S.J., et al. Presence of glyoxalase II in mitochondria from spinach leaves: comparison with the enzyme from cytosol. Biochem Int 1990, 22:1115-1120.
38. Norton S.J., Talesa V., Yuan W.J., Principato G.B., Glyoxalase I and glyoxalase II from Aloe vera: purification, characterization and comparison with animal glyoxalases. Biochem Int 1990, 22:411-418.
39. Ridderstrom M., Mannervik B. Molecular cloning and characterization of the thiolesterase glyoxalase II from Arabidopsis thaliana. Biochem J 1997, 322(Pt. 2):449-454.
40. Bito A., Haider M., Hadler I., Breitenbach M. Identification and phenotypic analysis of two glyoxalase II encoding genes from Saccharomyces cerevisiae, GLO2 and GLO4, and intracellular localization of the corresponding proteins. J Biol Chem 1997, 272:21509-21519.
41. Bito A., Haider M., Briza P., Strasser P., Breitenbach M. Heterologous expression, purification, and kinetic comparison of the cytoplasmic and mitochondrial glyoxalase II enzymes, Glo2p and Glo4p, from Saccharomyces cerevisiae. Protein Expr Purif 1999, 17:456-464.
42. Wenzel N.F., Carenbauer A.L., Pfiester M.P., Schilling O., Meyer-Klaucke W., Makaroff C.A., et al. The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-beta-lactamase family. J Biol Inorg Chem 2004, 9:429-438.
43. Campos-Bermudez V.A., Moran-Barrio J., Costa-Filho A.J., Vila A.J. Metal-dependent inhibition of glyoxalase II: a possible mechanism to regulate the enzyme activity. J Inorg Biochem 2010, 104:726-731.
44. Limphong P., McKinney R.M., Adams N.E., Bennett B., Makaroff C.A., Gunasekera T., et al. Human glyoxalase II contains an Fe(II)Zn(II) center but is active as a mononuclear Zn(II) enzyme. Biochemistry 2009, 48:5426-5434.
45. Daiyasu H., Osaka K., Ishino Y., Toh H. Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold. FEBS Lett 2001, 503:1-6.
46. Park H.S., Nam S.H., Lee J.K., Yoon C.N., Mannervik B., Benkovic S.J., et al. Design and evolution of new catalytic activity with an existing protein scaffold. Science 2006, 311:535-538.
47. Kim M.H., Choi W.C., Kang H.O., Lee J.S., Kang B.S., Kim K.J., et al. The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-l-homoserine lactone hydrolase. Proc Natl Acad Sci USA 2005, 102:17606-17611.
48. Thomas P.W., Stone E.M., Costello A.L., Tierney D.L., Fast W. The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein. Biochemistry 2005, 44:7559-7569.
49. Cameron A.D., Ridderstrom M., Olin B., Mannervik B. Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure 1999, 7:1067-1078.
50. Misra K., Banerjee A.B., Ray S., Ray M. Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into d-lactate without reduced glutathione. Biochem J 1995, 305(Pt. 3):999-1003.
51. Benov L., Sequeira F., Beema A.F. Role of rpoS in the regulation of glyoxalase III in Escherichia coli. Acta Biochim Pol 2004, 51:857-860.
52. Korithoski B., Levesque C.M., Cvitkovitch D.G. Involvement of the detoxifying enzyme lactoylglutathione lyase in Streptococcus mutans aciduricity. J Bacteriol 2007, 189:7586-7592.
53. Magnani D., Barre O., Gerber S.D., Solioz M. Characterization of the CopR regulon of Lactococcus lactis IL1403. J Bacteriol 2008, 190:536-545.
54. Roosild T.P., Castronovo S., Healy J., Miller S., Pliotas C., Rasmussen T., et al. Mechanism of ligand-gated potassium efflux in bacterial pathogens. Proc Natl Acad Sci USA 2010, 107:19784-19789.