Structural differences in triosephosphate isomerase from different species and discovery of a multitrypanosomatid inhibitor

Biochemistry

Volumn 45, Issue 8, 2006, Pages 2556-2560

  Olivares Illana, Vanesa ^a   Pérez Montfort, Ruy ^a   López Calahorra, Francisco ^b   Costas, Miguel ^a   Rodríguez Romero, Adela ^a   De Gómez Puyou, Marieta Tuena ^a   Puyou, Armando Gómez ^a  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b UNIVERSITY OF BARCELONA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIODIVERSITY; CRYSTAL STRUCTURE; ENZYME INHIBITION; ENZYMES; YEAST;

HOMODIMERIC TRIOSEPHOSPHATE ISOMERASE (TIM); MICROMOLAR RANGES; TRYPANOSOMA CRUZI (TCTIM); TRYPANOSOMATIDS;

ENZYME KINETICS;

6,6' BISBENZOTHIAZOLE 2,2' DIAMINE; ANTITRYPANOSOMAL AGENT; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENTAMOEBA HISTOLYTICA; ENZYME INACTIVATION; ENZYME STRUCTURE; LEISHMANIA; LEISHMANIA MEXICANA; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN STABILITY; SPECIES DIFFERENTIATION; STRUCTURE ANALYSIS; TRYPANOSOMA; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI;

ANIMALS; BENZOTHIAZOLES; CHICKENS; DOSE-RESPONSE RELATIONSHIP, DRUG; ENTAMOEBA HISTOLYTICA; ENZYME ACTIVATION; FLUORESCENCE; HUMANS; LEISHMANIA MEXICANA; SPECIES SPECIFICITY; THIAZOLES; TIME FACTORS; TRIOSE-PHOSPHATE ISOMERASE; TRYPANOSOMA BRUCEI BRUCEI; TRYPANOSOMA CRUZI;

ANIMALIA; ENTAMOEBA HISTOLYTICA; LEISHMANIA MEXICANA; PLASMODIUM FALCIPARUM; TRYPANOSOMA; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI; TRYPANOSOMATIDAE;

EID: 33644535470     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0522293     Document Type: Article

References (25)

1. Hu, Z., Ma, B., Wolfson, H., and Nussinov, R. (2000) Conservation of polar residues as hot spots at protein interfaces, Proteins: Struct., Funct., Genet. 39, 331-342.
2. Grishin, N. V., and Phillips, M. A. (1994) The subunit interfaces of oligomeric enzymes are conserved to a similar extent to the overall protein sequence, Protein Sci. 3, 2455-2458.
3. Nickbarg, E. B., Davenport, R. C., Petsko, G. A., and Knowles, J. R. (1988) Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism, Biochemistry 27, 5948-5960.
4. Gao, X.-G., Maldonado, E., Pérez-Montfort, R., Garza-Ramos, G., Tuena de Gómez-Puyou, M., Gómez-Puyou, A., and Rodríguez-Romero, A. (1999) Crystal structure of triosephosphate isomerase in hexane, Proc. Natl Acad. Sci. U.S.A. 96, 100062-100067.
5. Mattos, C., and Ringe, D. (1996) Locating and characterizing binding sites, Nat. Biotechnol. 14, 595-599.
6. Ringe, D. (1995) What makes a binding site a binding site? Curr. Opin. Struct. Biol. 5, 825-829.
7. Téllez-Valencia, A., Olivares-Illana, V., Hernández- Santoyo, A., Pérez-Montfort, R., Costas, M., Rodríguez-Romero, A., López-Calahorra, F., Tuena de Gómez-Puyou, M., and Gómez-Puyou, A. (2004) Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface, J. Mol. Biol. 341, 1353-1365.
8. Wierenga, R. K., Noble, M. E., M., Vriend, G., Nauche, S., and Hol, W. G. J. (1991) Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3- phosphate complex, J. Mol. Biol. 220, 995-1015.
9. Williams, J. C., Zeelen, J. P., Neubauer, G., Vriend, G., Backman, J., Michels, P. A., Lambeir, A. M., and Wierenga, R. K. (1999) Structural mutagenesis of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power, Protein Eng. 12, 243-250.
10. Lolis, E., Alber, T., Davenport, R. C., Rose, D., Hartman, F. C., and Petsko, G. A. (1990) Structure of yeast triosephosphate isomerase at 1.9 Å resolution, Biochemistry 29, 6609-6618.
11. Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D. C., Pogson, C. I., Wilson, I. A., Corran, P. H., Furth, A. J., Milman, J. D., Offord, R. E., Priddle, J. D., and Waley, S. G. (1975) Structure of chicken muscle triosephosphate isomerase determined at 2.5 Å resolution using amino acid sequence data, Nature 255, 609-614.
12. Mainfroid, V., Terpstra, P., Beauregard, M., Frere, J. M., Mande, S. C., Hol, W. G., Martial, J. A., and Goraj, K. (1996) Three hTIM mutants that provide new insights on why TIM is a dimer, J. Mol. Biol. 257, 441-456.
13. Velanker, S. S., Ray, S. S., Gokhale, R. S., Suma, S., Balaram, H., Balaram, S., and Murthy, M. R. (1997) Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design, Structure 5, 751-761.
14. Rodríguez-Romero, A., Hernández-Santoyo, A., del Pozo-Yauner, L., Kornhauser, A., and Fernández-Velasco, D. A. (2002) Structure and inactivation of triosephosphate isomerase from Entamoeba histolytica, J. Mol Biol. 322, 669-675.
15. Ostoa-Saloma, P., Garza-Ramos, G., Ramírez, J., Becker, I., Berzunza, I., Landa, A., Gómez-Puyou, A., Tuena de Gómez-Puyou, M., and Pérez-Montfort, R. (1997) Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi, Eur. J. Biochem. 244, 700-705.
16. Borchert, T. V., Pratt, K., Zeelen, J. P., Callens, M., Noble, M. E., Opperdoes, F. R., Michels, P. A., and Wierenga, R. K. (1993) Overexpression, of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant, Eur. J. Biochem. 211, 703-710.
17. Kohl, L., Callens, M., Wierenga, R. K., Opperdoes, F. R., and Michels, P. A. (1994) Triose-phosphate isomerase of Leishmania mexicana mexicana. Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein, Eur. J. Biochem. 220, 331-338.
18. Vázquez-Contreras, E., Zubillaga, R. A., Mendoza-Hernández, G., Costas, M., and Fernández-Velasco, D. A. (2000) Equilibrium Unfolding of Yeast Triosephosphate isomerase. A Monomeric intermediate in guanidine-HCl and two-state behaviour in urea, Protein Pept. Lett. 7, 57-64.
19. McVitttie, J. D., Esnouf, M. P., and Peacoke, A. R. (1972) The preparation and properties of triosephosphate isomerase from chicken muscle and a comparison with that from rabbit muscle, Eur. J. Biochem. 29, 67-73.
20. Pace, C. N., Vajdos, F., Fee, L., Grisley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-24123.
21. Bouanane, A., Lochon, P., and Neel, J. (1976) Nouveaux composes heterocycliques: le bis(chloro-2-benzothiazoles), Bull. Soc. Chim. Fr. (Chim. Mol.) 1843-1844.
22. Téllez-Valencia, A., Avila-Rios, S., Pérez-Montfort, R., Rodríguez-Romero, A., Tuena de Gómez Puyou, M., López-Calahorra, F., and Gómez-Puyou, A. (2002) Highly specific inactivation of triosephosphate isomerase from Trypanosoma cruzi, Biochem. Biophys. Res. Commun. 295, 958-963.
23. Eisenthal, R., and Cornish-Bowden, A. (1998) Prospects for antiparasitic drugs: The case of Trypanosoma brucei, the causative agent of African sleeping sickness, J. Biol. Chem. 273, 5500-5500.
24. Seidler, J., McGovern, S. J., Doman, T. N., and Soichet, B. K. (2003) Identification and prediction of promiscuous aggregating inhibitors among known drugs, J. Med. Chem. 46, 4477-4486.
25. Molinos-Gómez, A., Vidal, X., Maymo, M., Velasco, D., Matorell, J., and López-Calahorra, F. (2005) Tautomeric enhancement of the hyperpolarizability in new acridine benzothiazolylamine based NLO chromophores, Tetrahedron 61, 9075-9081.