Catalysis and structural properties of Leishmania infantum glyoxalase II: Trypanothione specificity and phylogeny

Biochemistry

Volumn 47, Issue 1, 2008, Pages 195-204

  Silva, Marta Sousa ^a,b   Barata, Lídia ^a   Ferreira, António E N ^a   Romão, Susana ^b   Tomás, Ana M ^b   Freire, Ana Ponces ^a   Cordeiro, Carlos ^a  

^a UNIVERSITY OF LISBON   (Portugal)

^b UNIVERSITY OF PORTO   (Portugal)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING SITES; BYPRODUCTS; CATALYSIS; DRUG PRODUCTS; PROTOZOA;

PHYLOGENY; SPERMIDINE MOLECULE; TRYPANOTHIONE SPECIFICITY;

ENZYME ACTIVITY;

GLYOXALASE; LACTIC ACID; METHYLGLYOXAL; SPERMIDINE;

ARABIDOPSIS; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; EVOLUTIONARY ADAPTATION; GLYCOLYSIS; INHIBITION KINETICS; LEISHMANIA INFANTUM; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM; TRYPANOSOMA;

EUKARYOTA; LEISHMANIA INFANTUM; PROKARYOTA; TRYPANOSOMATIDAE;

EID: 37849007277     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700989m     Document Type: Article

References (31)

1. Michels, P. A., Hannaert, V., and Bringaud, F. (2000) Metabolic aspects of glycosomes in trypanosomatidae - new data and views, Parasitol. Today 16, 482-489.
2. Hannaert, V., Bringaud, F., Opperdoes, F. R., and Michels, P. A. (2003) Evolution of energy metabolism and its compartmentation in kinetoplastida, Kinetoplastid Biol. Dis. 2, 11.
3. Muller, S., Liebau, E., Walter, R. D., and Krauth-Siegel, R. L. (2003) Thiol-based redox metabolism of protozoan parasites, Trends Parasitol. 19, 320-328.
4. Flohe, L., Hecht, H. J., and Steinert, P. (1999) Glutathione and trypanothione in parasitic hydroperoxide metabolism, Free Radicals Biol. Med. 27, 966-984.
5. Krauth-Siegel, R. L., Bauer, H., and Schirmer, R. H. (2005) Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia, Angew. Chem., Int. Ed. 44, 690-715.
6. Thornalley, P. J. (1990) The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life, Biochem. J. 269, 1-11.
7. Vickers, T. J., Greig, N., and Fairlamb, A. H. (2004) A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major, Proc. Natl. Acad. Sci. U.S.A. 101, 13186-13191.
8. Sousa Silva, M., Ferreira, A. E., Tomas, A. M., Cordeiro, C., and Ponces Freire, A. (2005) Quantitative assessment of the glyoxalase pathway in Leishmania infantum as a therapeutic target by modelling and computer simulation, FEBS J. 272, 2388-2398.
9. Irsch, T., and Krauth-Siegel, R. L. (2004) Glyoxalase II of African trypanosomes is trypanothione-dependent, J. Biol. Chem. 279, 22209-22217.
10. Cameron, A. D., Ridderstrom, M., Olin, B., and Mannervik, B. (1999) Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue, Structure Folding Des. 7, 1067-1078.
11. Trincao, J., Sousa, Silva, M., Barata, L., Bonifacio, C., Carvalho, S., Tomas, A. M., Ferreira, A. E. N., Cordeiro, C., Ponces, Freire, A., and Romao, M. J. (2006) Purification, crystallization and preliminary X-ray diffraction analysis of the glyoxalase II from Leishmania infantum, Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 62, 805-807.
12. Leslie, A. G. W. (1992) Recent changes to the MOSFLM package for processing film and image plate data, Joint CCP4 and ESF-EACBM Newsletters on Protein Crystallography, Vol. 26, Daresbury Laboratory, Warrington, U.K.
13. (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760-763.
14. Read, R. J. (2001) Pushing the boundaries of molecular replacement with maximum likelihood, Acta Crystallogr., Sect. D: Biol. Crystallogr. 57, 1373-1382.
15. Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics, Acta Crystallogr., Sect. D: Biol. Crystallogr. 60, 2126-2132.
16. Painter, J., and Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion, Acta Crystallogr., Sect. D: Biol. Crystallogr. 62, 439-450.
17. Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., and Ferrin, T. E. (2004) UCSF Chimera - a visualization system for exploratory research and analysis, J. Comput. Chem. 25, 1605-1612.
18. Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22, 4673-4680.
19. Vander, Jagt, D. L., Han, L. P., and Lehman, C. H. (1972) Kinetic evaluation of substrate specificity in the glyoxalase-I-catalyzed disproportionation of ketoaldehydes, Biochemistry 11, 3735-3740.
20. Martins, A. M., Cordeiro, C., and Freire, A. P. (1999) Glyoxalase II in Saccharomyces cerevisiae: In situ kinetics using the 5,5′- dithiobis(2-nitrobenzoic acid) assay, Arch. Biochem. Biophys. 366, 15-20.
21. Hertz-Fowler, C., Peacock, C. S., Wood, V., Aslett, M., Kerhornou, A., Mooney, P., Tivey, A., Berriman, M., Hall, N., Rutherford, K., Parkhill, J., Ivens, A. C., Rajandream, M. A., and Barrell, B. (2004) GeneDB: a resource for prokaryotic and eukaryotic organisms, Nucleic Acids Res. 32, D339-D343.
22. Padmanabhan, P. K., Mukherjee, A., Singh, S., Chattopadhyaya, S., Gowri, V. S., Myler, P. J., Srinivasan, N., and Madhubala, R. (2005) Glyoxalase I from Leishmania donovani: a potential target for anti-parasite drug, Biochem. Biophys. Res. Commun. 337, 1237-1248.
23. Crowder, M. W., Maiti, M. K., Banovic, L., and Makaroff, C. A. (1997) Glyoxalase II from A. thaliana requires Zn(II) for catalytic activity, FEBS Lett. 418, 351-354.
24. Ridderstrom, M., Saccucci, F., Hellman, U., Bergman, T., Principato, G., and Mannervik, B. (1996) Molecular cloning, heterologous expression, and characterization of human glyoxalase II, J. Biol. Chem. 271, 319-323.
25. Zang, T. M., Hollman, D. A., Crawford, P. A., Crowder, M. W., and Makaroff, C. A. (2001) Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis, J. Biol. Chem. 276, 4788-4795.
26. Concha, N. O., Rasmussen, B. A., Bush, K., and Herzberg, O. (1996) Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis, Structure 4, 823-836.
27. Brunger, A. T. (1992) Free R-Value - a Novel Statistical Quantity for Assessing the Accuracy of Crystal-Structures, Nature 355, 472-475.
28. Carfi, A., Pares, S., Duee, E., Galleni, M., Duez, C., Frere, J. M., and Dideberg, O. (1995) The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold, EMBO J. 14, 4914-4921.
29. Ariza, A., Vickers, T. J., Greig, N., Armour, K. A., Dixon, M. J., Eggleston, I. M., Fairlamb, A. H., and Bond, C. S. (2006) Specificity of the trypanothione-dependent Leishmania major glyoxalase I: structure and biochemical comparison with the human enzyme, Mol. Microbiol. 59, 1239-1248.
30. Potterton, E., McNicholas, S., Krissinel, E., Cowtan, K., and Noble, M. (2002) The CCP4 molecular-graphics project, Acta Crystallogr., Sect. D: Biol. Crystallogr. 58, 1955-1957.
31. Potterton, L., McNicholas, S., Krissinel, E., Gruber, J., Cowtan, K., Emsley, P., Murshudov, G. N., Cohen, S., Perrakis, A., and Noble, M. (2004) Developments in the CCP4 molecular-graphics project, Acta Crystallogr., Sect. D: Biol. Crystallogr. 60, 2288-2294.