Mechanistic imperative for the evolution of a metalloglutathione transferase of the vicinal oxygen chelate superfamily

Chemico-Biological Interactions

Volumn 111-112, Issue , 1998, Pages 41-50

  Laughlin, L Timothy ^a   Bernat, Bryan A ^a   Armstrong, Richard N ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Glutathione; Metallo enzymes; Vicinal oxygen chelate superfamily

Indexed keywords

FOSFOMYCIN; GLUTATHIONE TRANSFERASE; METAL ION; METALLOPROTEIN;

AMINO ACID SEQUENCE; BINDING SITE; CATALYSIS; CHELATION; ELECTRON SPIN RESONANCE; ENZYME MODIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; EVOLUTION; NONHUMAN; SHORT SURVEY;

ARCA; BACTERIA (MICROORGANISMS); EUKARYOTA; PROKARYOTA;

EID: 17944386988     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(97)00150-6     Document Type: Article

References (24)

1. Booth J., Boyland E., Sims P. An enzyme from rat liver catalyzing conjugation with glutathione. Biochem. J. 79:1961;516-524.
2. Combes B., Stakelum G.S. A liver enzyme that conjugates sulfobromophthalein sodium with glutathione. J. Clin. Invest. 40:1961;981-988.
3. Mannervik B., Danielson U.H. Glutathione transferases-structure and catalytic activity. CRC Crit. Rev. Biochem. 23:1988;283-337.
4. Ji X., von Rosenvinge E.C., Johnson W.W., Tomarev S.I., Piatigorsky J., Armstrong R.N., Gilliland G.L. Three-dimensional structure, catalytic properties and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry. 34:1995;5317-5328.
5. Pemble S., Schroeder K.R., Spencer S.R., Meyer D.J., Hallier E., Bolt H.M., Ketterer B., Taylor J.B. Human glutathione S-transferase Theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism. Biochem. J. 300:1994;271-276.
6. Pemble S.E., Wardle A.F., Taylor J.B. Glutathione S-transferase (GST) class Kappa: characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochem. J. 319:1996;754-759.
7. Morgenstern R., Guthenberg C., Depierre J.W. Microsomal glutathione transferase. Purification, initial characterization and demonstration that it is not identical to the cytosolic glutathione transferases A, B and C. Eur. J. Biochem. 128:1982;243-248.
8. Jakobsson P.J., Mancini J.A., Ford-Hutchinson A.W. Identification and characterization of a novel human microsomal glutathione S-transferase with leukotriene C4 synthase activity and significant sequence identity to 5-lipoxygenase-activating protein and leukotriene C4 synthase. J. Biol. Chem. 271:1996;22203-22210.
9. Armstrong R.N. Structure, catalytic mechanism and evolution of the glutathione transferases. Chem. Res. Toxicol. 10:1997;2-18.
10. Bernat B.A, Laughlin L.T., Armstrong R.N. Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases. Biochemistry. 36:1997;3050-3055.
11. Christensen B.G., Leanza W.J., Beattie T.R., Patchett A.A., Arison B.H., Ormond R.E., Kuehl F.A., Albers-Schonberg G., Jardetzky O. Phosphonomycin: structure and synthesis. Science. 166:1969;123-124.
12. Hendlin D., Stapley E.O., Jackson M., Wallick H., Miller A.K., Wolf F.J., Miller T.W., Chaiet L., Kahan F.M., Flotz E.L., Woodruff H.B., Mata J.M., Hernandez S., Mochales S. Phosphonomycin, a new antibiotic produced by strains of Streptomyces. Science. 166:1969;122-123.
13. Kahan F.M., Kahan J.S., Cassidy P.J., Kropp H. The mechanism of action of fosfomycin (phosphonomycin). Ann. New York Acad. Sci. 235:1974;364-385.
14. Marquardt J.L., Brown E.D., Lane W.S., Haley T.M., Ichikawa Y., Wong C.-H., Walsh C.T. Kinetics, stoichiometry and identification of the reactive thiolate in the inactivation of UDP-GlcNAc enolpyruvoyl transferase by the antibiotic fosfomycin. Biochemistry. 33:1994;10646-10651.
15. Arca P., Rico M., Brana A.F., Villar C.J., Hardisson C., Suarez J.E. Formation of an adduct between fosfomycin and glutathione: a new mechanism of antibiotic resistance in bacteria. Antimicrob. Agents Chemother. 32:1988;1552-1556.
16. Arca P., Hardisson C., Suarez J.E. Purification of a glutathione S-transferase that mediates fosfomycin resistance in bacteria. Antimicrob. Agents Chemother. 34:1990;844-848.
17. Altschul S.F., Gish W., Miller W., Myers E.W, Lipman D.J. Basic local alignment search tool. J. Mol. Biol. 215:1990;403-410.
18. Han S., Eltis L.D., Timmis K.N., Muchmore S.W., Bolin J.T. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science. 270:1995;976-980.
19. Zilhao R., Courvalin P. Nucleotide sequence of the fosB gene conferring fosfomycin resistance in Staphylococcus epidermis. FEMS Microbiol. Lett. 68:1990;267-272.
20. Sellin S., Eriksson L.E.G., Mannervik B. Fluorescence and nuclear relaxation enhancement studies of the binding of glutathione derivatives to manganese-reconstituted glyoxalase I from human erythrocytes. A model for the catalytic mechanism of the enzyme involving a hydrated metal ion. Biochemistry. 21:1982;4850-4857.
21. Shu L., Chioy Y.-M., Orville A.M., Miller M.A., Lipscomb J.D., Que L. Jr. X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-diooxygenase. Implications for the extradiol cleavage mechanism. Biochemistry. 34:1995;6649-6659.
22. Babbitt P.C., Hasson M.S., Wedekind J.E., Palmer D.R.J., Barrett W.C., Reed G.H., Rayment I., Ringe D., Kenyon G.L., Gerlt J.A. The enolase superfamily: a general strategy for enzyme-catalyzed abstraction of the α-protons of carboxylic acids. Biochemistry. 35:1996;16489-16501.
23. Koonin E.V., Mushegian A.R., Tatusov R.L., Altschul S.F., Bryant S.H., Bork P., Valencia A. Eukaryotic translation elongation factor 1γ contains a glutathione transferase domain- Study of a diverse, ancient protein superfamily using motif search and structural modeling. Protein Sci. 3:1994;2045-2054.
24. Pemble S.E., Taylor J.B. An evolutionary perspective on glutathione transferases inferred from class-Theta glutathione transferase cDNA sequences. Biochem. J. 287:1992;957-963.