Pre-Steady-State Analysis of the Nucleoside Hydrolase of Trypanosoma vivax. Evidence for Half-of-the-Sites Reactivity and Rate-Limiting Product Release

Biochemistry

Volumn 42, Issue 44, 2003, Pages 12902-12908

  Vandemeulebroucke, An ^a   Versées, Wim ^a   De Vos, Stefan ^a   Van Holsbeke, Els ^a   Steyaert, Jan ^a  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

TRANSITION STATES;

BIOASSAY; CHEMICAL BONDS; ENZYME KINETICS; FLUORESCENCE; HYDROLYSIS; MICROORGANISMS; NUCLEIC ACIDS;

ENZYMES;

BETA PURINE; NUCLEOSIDASE; NUCLEOSIDE; PURINE DERIVATIVE; PURINE NUCLEOSIDE; PYRIMIDINE; RIBOSE; RIBOSYL OXACARBENIUM; UNCLASSIFIED DRUG; WATER;

ARTICLE; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME REACTIVATION; FLUORESCENCE; HYDROLYSIS; ISOMERISM; PRIORITY JOURNAL; STEADY STATE; TRYPANOSOMA VIVAX;

ANIMALS; BINDING SITES; GUANOSINE; HYDROLYSIS; KINETICS; N-GLYCOSYL HYDROLASES; PROTEIN CONFORMATION; PROTOZOAN PROTEINS; PURINE NUCLEOSIDES; RIBOSE; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; TRYPANOSOMA VIVAX;

TRYPANOSOMA; TRYPANOSOMA VIVAX;

EID: 0242592081     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0347914     Document Type: Article

References (24)

1. Bzowska, A., Kulikowska, E., and Shugar, D. (2000) Purine nucteoside phosphorylase: properties, functions, and clinical aspects, Pharmacol. Ther. 88, 349-425.
2. Seegmiller, J. E., Rosenbloom, F. M., and Kelley, W. N. (1967) Enzyme defect associated with a sex-linked human neurological disorder and excessive purine synthesis, Science 155, 1682-1684.
3. Aronov, A. M., Munagala, N. R., de Montellano, P. R. O., Kuntz, I. D., and Wang, C. C. (2000) Rational Design of Selective Submicromolar Inhibitors of Trichichomonas foetus Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferase, Biochemistry 39, 4684-4691.
4. Parkin, D. W., Horenstein, B. A., Abdulah, D. R., Estupiñán, B., and Schramm, V. L. (1991) Nucleoside Hydrolase from Crithidia fasciculata. Metabolic role, purification, specificity, and kinetic mechanism, J. Biol. Chem. 266, 20658-20665.
5. Versées, W., Decanniere, K., Pellé, R., Depoorter, J., Brosens, E., Parkin, D. W., and Steyaert, J. (2001) Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax, J. Mol. Biol. 307, 1363-1379.
6. Parkin, D. W. (1996) Purine-specific nucleoside N-ribohydrolase from Trypanosoma brucei brucei. Purification, specificity, and kinetic mechanism, J. Biol. Chem. 271, 21713-21719.
7. Estupiñán, B., and Schramm, V. L. (1994) Guanosine-inosine-preferring nucleoside N-glycohydrolase from Crithidia fasciculata, J. Biol. Chem. 269, 23068-23073.
8. Horenstein, B. A., Parkin, D. W., Estupiñán, B., and Schramm, V. L. (1991) Transition-State Analysis of Nucleoside Hydrolase from Crithidia fasciculata, Biochemistry 30, 10788-10795.
9. Horenstein, B. A., and Schramm, V. L. (1993) Correlation of the electrostatic potential surface of an enzymatic transition state with novel transition-state inhibitors, Biochemistry 32, 9917-9925.
10. Versées, W., Decanniere, K., Van Holsbeke, E., Devroede, N., and Steyaert, J. (2002) Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax, J. Biol. Chem. 277, 15938-15946.
11. Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of protein, Protein Sci. 4, 2411-2423.
12. Cornish-Bowden, A. (1995) Fundamentals of enzyme kinetics, Portland Press Ltd., New York.
13. Johnson, K. A (1992) Enzymes 20, 1-61.
14. Fersht, A. R. (1985) Enzyme Structure and Mechanism, W. H. Freeman and Company, New York.
15. Ogbunude, P. O. J., Ikediobi, C. O., and Ukoha, A. I. (1985) Adenosine cycle in African trypanosomes, Ann. Trop. Med. Parasitol. 79, 7-11.
16. Hammond, D. J., and Gutteridge, W. E. (1984) Purine and pyrimidine metabolism in the trypanosomatidae, Mol. Biochem. Parasitol. 13, 243-261.
17. Berens, R. L., Krug, E. D., and Marr, J. J. (1995) in Biochemistry and Molecular Biology of Parasites (Marr, J. J., and Müller, M.) pp 89-117, Academic Press, New York.
18. Kline, P. C., and Schramm, V. L. (1992) Purine nucleoside phosphorylase. Inosine hydrolysis, tight binding of the hypoxanthine intermediate, and third-the-sites reactivity, Biochemistry 31, 5964-5973.
19. Levitzki, A., Stallcup, W. B., and Koshland, D. E., Jr. (1971) Half-of-the-sites reactivity and the conformational states of cytidine triphosphate synthetase, Biochemistry 10, 3371-3378.
20. Hiromi, K. (1979) Kinetics of Fast Enzyme Reactions, John Wiley & Sons, New York.
21. Degano, M., Almo, S. C., Sacchetini, J. C., and Schramm, V. L. (1998) Trypanosomal Nucleoside Hydrolase. A Novel Mechanism from the Structure with a Transition-State Inhibitor, Biochemistry 37, 6277-6285.
22. Gelbin, A., Schneider, B., Clowney, L., Hsieh, S.-U., Olson, W. K., and Berman, H. M. (1996) Geometric Parameters in Nucleic Acids: Sugar and Phosphate Constituents, J. Am. Chem. Soc. 118, 519-529.
23. King, E. L., and Altman, C. (1956) J. Phys. Chem. 60, 1375-1378.
24. Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.