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Volumn 47, Issue 8, 2008, Pages 2577-2583

Second-sphere amino acids contribute to transition-state structure in bovine purine nucleoside phosphorylase

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CRYSTALLOGRAPHY; ENZYME ACTIVITY; ISOTOPES; REACTION KINETICS;

EID: 39749099953     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7021365     Document Type: Article
Times cited : (14)

References (27)
  • 1
    • 0026690264 scopus 로고
    • Purine nucleoside phosphorylase. Inosine hydrolysis, tight binding of the hypoxanthine intermediate, and third-the-sites reactivity
    • 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.
    • (1992) Biochemistry , vol.31 , pp. 5964-5973
    • Kline, P.C.1    Schramm, V.L.2
  • 2
    • 0027729453 scopus 로고
    • Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction
    • Kline, P. C., and Schramm, V. L. (1993) Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction, Biochemistry 32, 13212-13219.
    • (1993) Biochemistry , vol.32 , pp. 13212-13219
    • Kline, P.C.1    Schramm, V.L.2
  • 3
    • 0028932756 scopus 로고
    • Pre-steady-state transition-state analysis of the hydrolytic reaction catalyzed by purine nucleoside phosphorylase
    • Kline, P. C., and Schramm, V. L. (1995) Pre-steady-state transition-state analysis of the hydrolytic reaction catalyzed by purine nucleoside phosphorylase, Biochemistry 34, 1153-1162.
    • (1995) Biochemistry , vol.34 , pp. 1153-1162
    • Kline, P.C.1    Schramm, V.L.2
  • 4
    • 1042299983 scopus 로고    scopus 로고
    • Transition state analysis for human and Plasmodium falciparum purine nucleoside phosphorylases
    • Lewandowicz, A., and Schramm, V. L. (2004) Transition state analysis for human and Plasmodium falciparum purine nucleoside phosphorylases, Biochemistry 43, 1458-1468.
    • (2004) Biochemistry , vol.43 , pp. 1458-1468
    • Lewandowicz, A.1    Schramm, V.L.2
  • 6
    • 29444445067 scopus 로고    scopus 로고
    • Transition states and inhibitors of the purine nucleoside phosphorylase family
    • Taylor Ringia, E. A., and Schramm, V. L. (2005) Transition states and inhibitors of the purine nucleoside phosphorylase family, Curr. Top. Med. Chem. 5, 1237-1258.
    • (2005) Curr. Top. Med. Chem , vol.5 , pp. 1237-1258
    • Taylor Ringia, E.A.1    Schramm, V.L.2
  • 7
    • 34247603923 scopus 로고    scopus 로고
    • Neighboring group participation in the transition state of human purine nucleoside phosphorylase
    • Murkin, A. S., Birck, M. R., Rinaldo-Matthis, A., Shi, W., Taylor, E. A., Almo, S. C., and Schramm, V. L. (2007) Neighboring group participation in the transition state of human purine nucleoside phosphorylase, Biochemistry 46, 5038-5049.
    • (2007) Biochemistry , vol.46 , pp. 5038-5049
    • Murkin, A.S.1    Birck, M.R.2    Rinaldo-Matthis, A.3    Shi, W.4    Taylor, E.A.5    Almo, S.C.6    Schramm, V.L.7
  • 9
    • 33750979005 scopus 로고    scopus 로고
    • Transition-state structure of human 5́-methylthioadenosine phosphorylase
    • Singh, V., and Schramm, V. L. (2006) Transition-state structure of human 5́-methylthioadenosine phosphorylase, J. Am. Chem. Soc. 128, 14691-14696.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 14691-14696
    • Singh, V.1    Schramm, V.L.2
  • 11
    • 0028087716 scopus 로고
    • + with the specific incorporation of atomic labels
    • + with the specific incorporation of atomic labels, J. Am. Chem. Soc. 116, 6531-6536.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 6531-6536
    • Rising, K.A.1    Schramm, V.L.2
  • 12
    • 0021229835 scopus 로고
    • 3H kinetic isotope effects on acid-catalyzed glycosidic bond hydrolysis of AMP, dAMP, and inosine
    • 3H kinetic isotope effects on acid-catalyzed glycosidic bond hydrolysis of AMP, dAMP, and inosine, J. Biol. Chem. 259, 9411-9417.
    • (1984) J. Biol. Chem , vol.259 , pp. 9411-9417
    • Parkin, D.W.1    Leung, H.B.2    Schramm, V.L.3
  • 13
    • 0038522525 scopus 로고    scopus 로고
    • Over-the-barrier transition state analogues and crystal structure with Mycobacterium tuberculosis purine nucleoside phosphorylase
    • Lewandowicz, A., Shi, W., Evans, G. B., Tyler, P. C., Furneaux, R. H., Basso, L. A., Santos, D. S., Almo, S. C., and Schramm, V. L. (2003) Over-the-barrier transition state analogues and crystal structure with Mycobacterium tuberculosis purine nucleoside phosphorylase, Biochemistry 42, 6057-6066.
    • (2003) Biochemistry , vol.42 , pp. 6057-6066
    • Lewandowicz, A.1    Shi, W.2    Evans, G.B.3    Tyler, P.C.4    Furneaux, R.H.5    Basso, L.A.6    Santos, D.S.7    Almo, S.C.8    Schramm, V.L.9
  • 14
    • 0032537481 scopus 로고    scopus 로고
    • One-third-the-sites transition-state inhibitors for purine nucleoside phosphorylase
    • 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.
    • (1998) Biochemistry , vol.37 , pp. 8615-8621
    • Miles, R.W.1    Tyler, P.C.2    Furneaux, R.H.3    Bagdassarian, C.K.4    Schramm, V.L.5
  • 16
    • 0020610472 scopus 로고
    • Synthesis of "9-deazaguanosine" and other new pyrrolo[3,2-d]-pyrimidine C-nucleosides
    • Lim, M.-I., Ren, Y.-Y., Otter, B. A., and Klein, R. S. (1983) Synthesis of "9-deazaguanosine" and other new pyrrolo[3,2-d]-pyrimidine C-nucleosides, J. Org. Chem. 48, 780-788.
    • (1983) J. Org. Chem , vol.48 , pp. 780-788
    • Lim, M.-I.1    Ren, Y.-Y.2    Otter, B.A.3    Klein, R.S.4
  • 17
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J. F., and Walsh, C. T. (1988) The behavior and significance of slow-binding enzyme inhibitors, Adv. Enzymol. Relat. Areas Mol. Biol. 61, 201-301.
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 19
    • 39749124957 scopus 로고    scopus 로고
    • Remote mutations alter transition-state structure of human purine nucleoside phosphorylase
    • Luo, M., Li, L., and Schramm, V. L. (2008) Remote mutations alter transition-state structure of human purine nucleoside phosphorylase, Biochemistry 47, 2565-2576.
    • (2008) Biochemistry , vol.47 , pp. 2565-2576
    • Luo, M.1    Li, L.2    Schramm, V.L.3
  • 20
    • 37349047044 scopus 로고    scopus 로고
    • Gutierrez, J. A., Luo, M., Singh, V. P., Li, L., Brown, R. L., Norris, G. E., Evans, G. B., Furneaux, R. H., Tyler, P. C., Painter, G. F., Lenz, D. H., and Schramm, V. L. (2007) Picomolar inhibitors as transition state probes of 5′-methylthioadenosine nucleosidases, ACS Chem. Biol. 2, 725-734.
    • Gutierrez, J. A., Luo, M., Singh, V. P., Li, L., Brown, R. L., Norris, G. E., Evans, G. B., Furneaux, R. H., Tyler, P. C., Painter, G. F., Lenz, D. H., and Schramm, V. L. (2007) Picomolar inhibitors as transition state probes of 5′-methylthioadenosine nucleosidases, ACS Chem. Biol. 2, 725-734.
  • 21
    • 0018858255 scopus 로고
    • The isotope trapping method: Desorption rates of productive E. S complexes
    • Rose, I. A. (1980) The isotope trapping method: desorption rates of productive E. S complexes, Methods Enzymol. 64, 47-59.
    • (1980) Methods Enzymol , vol.64 , pp. 47-59
    • Rose, I.A.1
  • 22
    • 0019349208 scopus 로고
    • The expression of isotope effects on enzyme-catalyzed reactions
    • Northrop, D. B. (1981) The expression of isotope effects on enzyme-catalyzed reactions, Annu. Rev. Biochem. 50, 103-131.
    • (1981) Annu. Rev. Biochem , vol.50 , pp. 103-131
    • Northrop, D.B.1
  • 23
    • 39749127000 scopus 로고    scopus 로고
    • Frisch, A, Ed, 2nd ed, Gaussian
    • Frisch, A., Ed. (1999) Gaussian 98 user's reference, 2nd ed., Gaussian.
    • (1999) Gaussian 98 user's reference
  • 24
    • 0034350512 scopus 로고    scopus 로고
    • A program for studies of isotope effects using Hessian modifications
    • Anisimov, V., and Paneth, P. (1999) A program for studies of isotope effects using Hessian modifications, J. Math. Chem. 26, 75-86.
    • (1999) J. Math. Chem , vol.26 , pp. 75-86
    • Anisimov, V.1    Paneth, P.2
  • 25
    • 0036102164 scopus 로고    scopus 로고
    • Substrate entropy in enzyme enantioselectivity: An experimental and molecular modeling study of a lipase
    • Ottosson, J., Fransson, L., and Hult, K. (2002) Substrate entropy in enzyme enantioselectivity: an experimental and molecular modeling study of a lipase, Protein Sci. 11, 1462-1471.
    • (2002) Protein Sci , vol.11 , pp. 1462-1471
    • Ottosson, J.1    Fransson, L.2    Hult, K.3
  • 26
    • 0032860328 scopus 로고    scopus 로고
    • Enzymatic transition-state analysis and transition-state analogs
    • Schramm, V. L. (1999) Enzymatic transition-state analysis and transition-state analogs, Methods Enzymol. 308, 301-355.
    • (1999) Methods Enzymol , vol.308 , pp. 301-355
    • Schramm, V.L.1
  • 27
    • 34250201455 scopus 로고    scopus 로고
    • Transition State Analysis of Acid-catalyzed dAMP Hydrolysis
    • McCan, J. A. B., and Berti, P. J. (2007) Transition State Analysis of Acid-catalyzed dAMP Hydrolysis, J. Am. Chem. Soc. 129, 7055-7064.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 7055-7064
    • McCan, J.A.B.1    Berti, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.