Towards the mechanism of trimeric purine nucleoside phosphorylases: Stopped-flow studies of binding of multisubstrate analogue inhibitor - 2-amino-9-[2-(phosphonomethoxy)ethyl]-6-sulfanylpurine

Biophysical Chemistry

Volumn 125, Issue 2-3, 2007, Pages 260-268

  Wielgus Kutrowska, B ^a   Antosiewicz, J M ^a   Dlugosz, M ^a   Holy A ^b   Bzowska, A ^a  

^a UNIVERSITY OF WARSAW   (Poland)

^b INSTITUTE OF ORGANIC CHEMISTRY AND BIOCHEMISTRY   (Czech Republic)

Author keywords

Fluorescence; Numerical integration; PME 6 thio Gua; PNP; Stopped flow

Indexed keywords

2 AMINO 9 [2 (PHOSPHONOMETHOXY)ETHYL] 6 SULFANYLPURINE; LIGAND; POTASSIUM CHLORIDE; PURINE DERIVATIVE; PURINE NUCLEOSIDE PHOSPHORYLASE; TIOGUANINE; UNCLASSIFIED DRUG;

ALKALINITY; ARTICLE; BINDING SITE; CATALYSIS; CATALYST; CELLULOMONAS; CONFORMATIONAL TRANSITION; DISSOCIATION CONSTANT; DRUG PROTEIN BINDING; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; IONIC STRENGTH; KINETICS; LINEAR REGRESSION ANALYSIS; MEASUREMENT; PKA; PRIORITY JOURNAL; REACTION ANALYSIS; SPECTROFLUOROMETRY; STOPPED FLOW SPECTROFLUORIMETER;

BACTERIAL PROTEINS; BINDING SITES; CELLULOMONAS; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; MODELS, BIOLOGICAL; PROTEIN BINDING; PROTEIN CONFORMATION; PURINE-NUCLEOSIDE PHOSPHORYLASE; PURINES; SUBSTRATE SPECIFICITY;

CELLULOMONAS SP.; MAMMALIA;

EID: 33846452894     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.08.008     Document Type: Article

References (32)

1. Bzowska A., Kulikowska E., and Shugar D. Purine nucleoside phosphorylase: properties, functions and clinical aspects. Pharmacol. Ther. 88 (2000) 349-425
2. Miles R.W., Tyler P.C., Furneaux R.H., Bagdassarian C.K., and Schramm V.L. One third-the-sites transition-state inhibitors for purine nucleoside phosphorylase. Biochemisty 37 (1998) 8615-8621
3. Wang F., Miles R.W., Kicska G., Nieves E., Schramm V.L., and Angeletti R.H. Immucillin-H binding to purine nucleoside phosphorylase reduces dynamic solvent exchange. Protein Sci. 9 (2000) 1660-1668
4. Erion M.D., Stoeckler J.D., Guida W.C., Walter R.L., and Ealick S.E. Purine nucleoside phosphorylase. 2. Catalytic mechanism. Biochemistry 36 (1997) 11735-11748
5. Tebbe J., Bzowska A., Wielgus-Kutrowska B., Kazimierczuk Z., Schröder W., Shugar D., Saenger W., and Koellner G. Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs. J. Mol. Biol. 294 (1999) 1239-1255
6. Fedorov A., Shi W., Kicska G., Fedorov E., Tyler P.C., Furneaux R.H., Hanson J.C., Gainsford G.J., Larese J.Z., Schramm V.L., and Almo S.C. Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis. Biochemistry 40 (2001) 853-860
7. Wielgus-Kutrowska B., Frank J., Hol A., Koelner G., and Bzowska A. Interactions of trimeric purine nucleoside phosphorylases with ground state analogues: calorimetric and fluorimetric studies. Nucleosides Nucleotides Nucleic Acids 22 (2003) 1695-1698
8. Bzowska A., Koelner G., Wielgus-Kutrowska B., Stroh A., Raszewski G., Holý A., Steiner T., and Frank J. Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: important implications for the mechanism of catalysis. J. Mol. Biol. 342 (2004) 1015-1032
9. Kline P.C., and Schramm V.L. Purine nucleoside phosphorylase. Inosine hydrolysis, tight binding of the hypoxanthine intermediate, and third-the-sites reactivity. Biochemistry 31 (1992) 5964-5973
10. Bzowska A. Calf spleen purine nucleoside phosphorylase: complex kinetic mechanism, hydrolysis of 7-methylguanosine and oligomeric state in solution. Biochim. Biophys. Acta 1596 (2002) 293-317
11. Wielgus-Kutrowska B., and Bzowska A. Probing the mechanism of purine nucleoside phosphorylase by steady-state kinetic studies and ligand binding characterisation determined by fluorimetric titrations. Biochim. Biophys. Acta 1764 (2006) 887-902
12. Dlugosz M., Bzowska A., and Antosiewicz J.M. Stopped-flow studies of guanine binding by calf spleen purine nucleoside phosphorylase. Biophys. Chem. 115 (2005) 67-76
13. Behlke J., Koellner G., and Bzowska A. Oligomeric structure of mammalian purine nucleoside phosphorylase in solution determined by analytical ultracentrifugation. Z. Naturforsch., C 60 (2005) 927-931
14. Modrak-Wojcik A., Stepniak K., Akoev V., Zolkiewski M., and Bzowska A. Molecular architecture of E. coli purine nucleoside phosphorylase studied by analytical ultracentrifugation and CD spectroscopy. Protein Sci. 15 (2006) 1794-1800
15. Kalckar H.M. Differential spectrophotometry of purine compounds by means of specific enzymes: I. Determination of hydroxypurines. J. Biol. Chem. 167 (1947) 429-443
16. Stoeckler J.D., Agarwal R.P., Agarwal K.C., and Parks Jr. R.E. Purine nucleoside phosphorylase from human erythrocytes. Methods Enzymol. 51 (1978) 530-538
17. Wielgus-Kutrowska B., Bzowska A., Tebbe J., Koellner G., and Shugar D. Purine nucleoside phosphorylase (PNP) from Cellulomonas sp.: physico-chemical properties, and binding of substrates determined by ligand-dependent enhancement of enzyme intrinsic fluorescence, and by protective effects of ligands on thermal inactivation of the enzyme. Biochim. Biophys. Acta 1597 (2002) 320-334
18. Holý A., Günter J., Dvoráková H., Masjídková M., Andrei G., Snoeck R., Balzarini J., and De Clercq E. Structure-antivirial activity relationship in the series of pyrimidine and purine N-[2[(2-phosphonometoxy)ethyl] nucleotide analogues. Derivatives substituted at the carbon atoms of the base. J. Med. Chem. 42 (1999) 2064-2086
19. Fox J.J., Wempen I., Hampton A., and Doeerr I.L. Thiation of Nucleosides I. Synthesis of 2-amino-6-mercapto-9-beta-d-ribofuranosylpurine ("thioguanosine") and related purine nucleosides. J. Am. Chem. Soc. 80 (1958) 1669-1674
20. Fernández-Botello A., Griesser R., Holý A., Moreno V., and Sigel H. Acid-base and metal-ion-binding properties of 9-[2-(2-phosphonoethoxy)-ethyl]-adenine (PEEA), a relative of the antiviral nucleotide analogue 9-[2-(phosphonomethoxy)-ethyl]-adenine (PMEA). An exercise on the quantification of isomeric complex equilibria in solution. Inorganic Chem. 44 (2005) 5104-5117
21. Dl{bar}ugosz M., Bojarska E., and Antosiewicz J.M. A procedure for analysis of stopped-flow transients for protein-ligand association. J. Biochem. Biophys. Methods 51 (2002) 179-193
22. Porter D.J.T. Purine nucleoside phosphorylase. Kinetic mechanism of the enzyme from calf spleen. J. Biol. Chem. 267 (1992) 7342-7351
23. Koelner G., Luić M., Shugar D., Saenger W., and Bzowska A. Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 Å resolution. J. Mol. Biol. 265 (1997) 202-216
24. Johnson K.A. Transient-state kinetic analysis of enzyme reaction pathways. In: Sigman D.S. (Ed). The Enzymes vol. XX (1992), Academic Press, Inc., San Diego 1-61
25. Strickland S., Palmer G., and Massey V. Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid kinetic data. J. Biol. Chem. 250 (1975) 4048-4052
26. Rhee S.G., and Chock P.B. Mechanistic studies of glutamine synthetase from Escherichia coli: kinetics of ADP and orthophosphate binding to the unadenylated enzyme. Biochemistry 15 (1976) 1755-1760
27. Wierzchowski J., Bzowska A., Stepniak K., and Shugar D. Interactions of calf spleen purine nucleoside phosphorylase with 8-azaguanine, and a bisubstrate analogue inhibitor: implications for the reaction mechanism. Z. Naturforsch. 59c (2004) 713-725
28. Deng H., Murkin A.S., and Schramm V.L. Phosphate activation in the ground state of purine nucleoside phosphorylase. J. Am. Chem. Soc. 128 (2006) 7765S-7771S
29. Blackburn G.M., and Kent D.E. Synthesis of alpha- and gamma-fluoroalkylphosphonates. J. Chem. Perkin Trans. I (1986) 913-917
30. Mao C., Cook W.J., Zhou M., Fedorov A.A., Almo S.C., and Ealick S.E. Biochemistry 37 (1998) 7135-7146
31. Lui M., Koellner G., Yokomatsu T., Shibuya S., and Bzowska A. Calf spleen purine-nucleoside phosphorylase: crystal structure of the binary complex with a potent multisubstrate analogue inhibitor. Acta Crystallogr., D Biol. Crystallogr. 60 (2004) 1417-1424
32. Canduri F., Fadel V., Basso L.A., Palma M.S., Santos D.S., and de Azevedo Jr. W.F. New catalytic mechanism for human purine nucleoside phosphorylase. Biochem. Biophys. Res. Commun. 327 (2005) 646-649