Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues

Biochemistry

Volumn 46, Issue 3, 2007, Pages 659-668

  Rinaldo Matthis, Agnes ^a   Wing, Corin ^a   Ghanem, Mahmoud ^a   Deng, Hua ^a   Wu, Peng ^b   Gupta, Arti ^b   Tyler, Peter C ^c   Evans, Gary B ^c   Furneaux, Richard H ^c   Almo, Steven C ^a   Wang, Ching C ^b   Schramm, Vern L ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c CALLAGHAN INNOVATION   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; ELECTROSTATIC FEATURES; PURINE; TRICHOMONAS VAGINALIS;

CRYSTAL STRUCTURE; DISSOCIATION; ENZYME IMMOBILIZATION; HYDROGEN BONDS; NUCLEIC ACIDS; ORGANIC COMPOUNDS;

PROTOZOA;

ADENOSINE; HYDROXYL GROUP; HYDROXYPYRROLIDINE; IMMUCILLIN A; IMMUCILLIN H; ISOTOPE; PHOSPHOTRANSFERASE; PURINE; PURINE NUCLEOSIDE KINASE; PURINE NUCLEOSIDE PHOSPHORYLASE; PYRROLIDINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME STRUCTURE; HYDROGEN BOND; INFRARED SPECTROSCOPY; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; TRICHOMONAS VAGINALIS;

ADENINE; ANIMALS; CATALYTIC DOMAIN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PURINE-NUCLEOSIDE PHOSPHORYLASE; PYRROLIDINES; SUBSTRATE SPECIFICITY; TRICHOMONAS VAGINALIS;

BACTERIA (MICROORGANISMS); PLASMODIUM FALCIPARUM; PROTOZOA; TRICHOMONAS VAGINALIS;

EID: 33846349983     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061515r     Document Type: Article

References (32)

1. Radonjic, I. V., Dzamic, A. M., Mitrovic, S. M., Arsic, Arsenijevic, V. S., Popadic, D. M., and Kranjcic, Zec, I. F. (2005) Diagnosis of Trichomonas vaginalis infection: The sensitivities and specificities of microscopy, culture and PCR assay, Eur. J. Obstet. Gynecol. Reprod. Biol. 126, 116-120.
2. Gero, A. M., Kang, E. W., Harvey, J. E., Schofield, P. J., Clinch, K., and Furneaux, R. H. (2000) Trichomonas vaginalis: detection of nucleoside hydrolase activity as a potential screening procedure, Exp. Parasitol. 94, 125-128.
3. Zang, Y., Wang, W.-H., Wu, S.-W., Ealick, S. E., and Wang, C. C. (2005) Identification of a subversive substrate of Trichomonas vaginalis purine nucleoside phosphorylase and the crystal structure of the enzyme-substrate complex, J. Biol. Chem. 280, 22318-22325.
4. Brown, D. M., Upcroft, J. A., Dodd, H. N., Chen, N., and Upcroft, P. (1999) Alternative 2-keto acid oxidoreductase activities in Trichomonas vaginalis, Mol. Biochem. Parasitol. 98, 203-214.
5. de Koning, H. P., Bridges, D. J., and Burchmore, R. J. S. (2005) Purine and pyrimidine transport in pathogenic protozoa: From biology to therapy, FEMS Microbiol. Rev. 29, 987-1020.
6. Stoeckler, J. D. (1984) Purine Nucleoside Phosphorylase: A Target for Chemotherapy, in Development in Cancer Chemotherapy (Glazer, R. I., Ed.) pp 35-60, CRC Press, Inc., Boca Raton, FL.
7. Montgomery, J. A. (1993) Purine nucleoside phosphorylase: a target for drug design, Med. Res. Rev. 13, 209-228.
8. Bzowska, A., Kulikowska, E., and Shugar, D. (2000) Purine nucleoside phosphorylase: properties, functions and clinical aspects, Pharmacol. Ther. 88, 349-425.
9. Koellner, G., Bzowska, A., Wielgus-Kutrowska, B., Luic, M., Steiner, T., Saenger, W., and Stepinski, J. (2002) Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism, J. Mol. Biol. 315, 351-371.
10. Mazella, L. J., Parkin, D. W., Tyler, P. C., Furneaux, R. H., and Schramm, V. L. (1996) Mechanistic diagnosis of N-ribohydrolases and purine nucleoside phosphorylase, J. Am. Chem. Soc. 118, 2111-2112.
11. Singh, V., and Schramm, V. L. (2006) Transition state structure of human 5′-methylthioadenosine phosphorylase, J. Am. Chem. Soc. 128, 14691-14696.
12. Handlon, A. L., Xu, C., Muller-Steffner, H. M., Schuber, F., and Oppenheimer, N. J. (1994) 2′-Ribose substituent effects on the chemical and enzymatic hydrolysis of NAD+, J. Am. Chem. Soc. 116, 12087-12088.
13. Rosenburg, S., and Kirsch, J. F. (1981) Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and β-glucosidase: acid and alkaline hydrolysis, Biochemistry 20, 3196-3207.
14. Lewandowicz, A., Taylor, Ringia, E., Ting, L. M., Kim, K., Tyler, P. C., Evans, G. B., Zubkova, O. V., Mee, S., Painter, G. F., Lenz, D. H., Furneaux, R. H., and Schramm, V. L. (2005) Energetic mapping of transition state analogue interactions with human and plasmodium falciparum purine nucleoside phosphorylases, J. Biol. Chem. 280, 30320-30328.
15. Mungagala, N. R., and Wang, C. C. (2003) Adenosine is a primary precursor of all purine nucletides in Trichomonas vaginalis, Mol. Biochem. Parasitol. 127, 143-149.
16. Mungagala, N. R., and Wang, C. C. (2002) The purine nucleoside phosphorylase from Trichomonas vaginalis is a homologue of the bacterial enzyme, Biochemistry 41, 10382-10389.
17. Kim, B. K., Cha, S., and Parks, R. E., Jr. (1968) Purine nucleoside phosphorylase from human erythroyctes. II. Kinetic analysis and substrate-binding studies, J. Biol. Chem. 243, 1771-1776.
18. Kicska, G. A., Tyler, P. C., Evans, G. B., Furneaux, R. H., Kim, K., and Schramm, V. L. (2002) Transition state analogue inhibitors of purine nucleoside phosphorylase from Plasmodium falciparum, J. Biol. Chem. 277, 3219-3225.
19. Singh, V., Evans, G. B., Lenz, D. H., Mason, J. M., Clinch, K., Mee, S., Painter, G. F., Tyler, P. C., Furneaux, R. H., Lee, J. E., Howell, P. L., and Schramm, V. L. (2005) Femtomolar transition state analogue inhibitors of 5′-methylthioadenosine/S-adenosyl-homocysteine nucleosidase from Escherichia coli, J. Biol. Chem. 280, 18265-18273.
20. Miles, R. W., Tyler, P. C., Furneaux, R. H., Bagdassarian, C. K., and Schramm, V. L. (1998) One-third-the-sites transition-state inhibitors for purine nucleoside phosphorylase, Biochemistry 37, 8615-8621.
21. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
22. Vagin, A., and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement, J. Appl. Crystallogr. 30, 1022-1025.
23. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr., Sect. D 53, 240-255.
24. Potterton, E., Briggs, P., Turkenburg, M., and Dodson, E. (2003) A graphical user interface to the CCP4 program suite, Acta Crystallogr., Sect. D 59, 1131-1137.
25. Emsley, P., and Cowtan, K. (2004) Model-building tools for molecular graphics, Acta Crystallogr., Sect. D 60, 2126-2132.
26. DeLano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA.
27. Kicska, G. A., Tyler, P. C., Evans, G. B., Furneaux, R. H., Schramm, V. L., and Kim, K. (2002) Purine-less death in Plasmodium falciparum induced by Immucillin-H, a transition state analogue of purine nucleoside phosphorylase, J. Biol. Chem. 277, 3226-3231.
28. Kicska, G. A., Tyler, P. C., Evans, G. B., Furneaux, R. H., Shi, W., Fedorov, A., Lewandowicz, A., Cahill, S. M., Almo, S. C., and Schramm, V. L. (2002) Atomic dissection of the hydrogen bond network for transition-state analogue binding to purine nucleoside phosphorylase, Biochemistry 41, 14489-14498.
29. Ting, L. M., Shi, W., Lewandovicz, A., Singh, V., Mwakingwe, A., Birck, M. R., Ringia, E. A., Bench, G., Madrid, D. C., Tyler, P. C., Evans, G. B., Furneaux, R. H., and Schramm, V. L. (2005) Targetign a novel Plasmodium falciparum purine recycling pathway with specific immucillins, J. Biol. Chem. 280, 9547-9554.
30. Bennett, E. M., Li, C., Allan, P. W., Parker, W. B., and Ealick, S. E. (2003) Structural basis for substrate specificity of E. coli purine nucleoside phosphorylase, J. Biol. Chem. 278, 47110-47118.
31. Taylor Ringia, E. A., Tyler, P. C., Evans, G. B., Furneaux, R. H., Murkin, A. S., and Schramm, V. L. (2006) Transition state analogue discrimination by related purine nucleoside phosphorylases, J. Am. Chem. Soc. 128, 7126-7127.
32. Schramm, V. L. (2003) Enzymatic transition state poise and transition state analogues, Acc. Chem. Res. 36, 588-596.