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Volumn 43, Issue 7, 2004, Pages 1980-1987

Assignment of Downfield Proton Resonances in Purine Nucleoside Phosphorylase·Immucillin-H Complex by Saturation-Transferred NOEs

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYSIS; CRYSTAL STRUCTURE; ENZYMES; HYDROGEN BONDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RESONANCE;

EID: 1242285470     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0358115     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 0001157528 scopus 로고
    • (Glazer, R. J., Ed.), CRC Press Inc., Boca Raton, FL
    • Stoeckler, J. D. (1984) in Developments in Cancer Chemotherapy (Glazer, R. J., Ed.) pp 35-60, CRC Press Inc., Boca Raton, FL.
    • (1984) Developments in Cancer Chemotherapy , pp. 35-60
    • Stoeckler, J.D.1
  • 2
    • 0034452004 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylases: Properties, functions, and clinical aspects
    • Bzowska, A., Kulikowska, E., and Shugar, D. (2000) Purine nucleoside phosphorylases: properties, functions, and clinical aspects, Pharmacology Ther. 88, 349-425.
    • (2000) Pharmacology Ther. , vol.88 , pp. 349-425
    • Bzowska, A.1    Kulikowska, E.2    Shugar, D.3
  • 4
    • 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, 8615-21.
    • (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
  • 5
    • 0036479245 scopus 로고    scopus 로고
    • Purine-less death in Plasmodium falciparum induced by immucillin-H, a transition state analogue of purine nucleoside phosphorylase
    • 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, 3226-31.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3226-3231
    • Kicska, G.A.1    Tyler, P.C.2    Evans, G.B.3    Furneaux, R.H.4    Schramm, V.L.5    Kim, K.6
  • 6
    • 0036479331 scopus 로고    scopus 로고
    • Transition state analogue inhibitors of purine nucleoside phosphorylase from Plasmodium falciparum
    • 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, 3219-25.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3219-3225
    • Kicska, G.A.1    Tyler, P.C.2    Evans, G.B.3    Furneaux, R.H.4    Kim, K.5    Schramm, V.L.6
  • 8
    • 0033519996 scopus 로고    scopus 로고
    • The 2.0 A structure of malarial purine phosphoribosyltransferase in complex with a transition-state analogue inhibitor
    • Shi, W., Li, C. M., Tyler, P. C., Furneaux, R. H., Cahill, S. M., Girvin, M. E., Grubmeyer, C., Schramm, V. L., and Almo, S. C. (1999) The 2.0 A structure of malarial purine phosphoribosyltransferase in complex with a transition-state analogue inhibitor, Biochemistry 38, 9872-80.
    • (1999) Biochemistry , vol.38 , pp. 9872-9880
    • Shi, W.1    Li, C.M.2    Tyler, P.C.3    Furneaux, R.H.4    Cahill, S.M.5    Girvin, M.E.6    Grubmeyer, C.7    Schramm, V.L.8    Almo, S.C.9
  • 9
    • 0032587578 scopus 로고    scopus 로고
    • The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor
    • Shi, W., Li, C. M., Tyler, P. C., Furneaux, R. H., Grubmeyer, C., Schramm, V. L., and Almo, S. C. (1999) The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor, Nat. Struct. Biol. 6, 588-93.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 588-593
    • Shi, W.1    Li, C.M.2    Tyler, P.C.3    Furneaux, R.H.4    Grubmeyer, C.5    Schramm, V.L.6    Almo, S.C.7
  • 12
    • 0032438194 scopus 로고    scopus 로고
    • Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin
    • Lin, J., Westler, W. M., Cleland, W. W., Markley, J. L., and Frey, P. A. (1998) Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin, Proc. Natl. Acad. Sci. U.S.A. 95, 14664-8.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14664-14668
    • Lin, J.1    Westler, W.M.2    Cleland, W.W.3    Markley, J.L.4    Frey, P.A.5
  • 13
    • 0028040716 scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases
    • comment
    • Frey, P. A., Whitt, S. A., and Tobin, J. B. (1994) A low-barrier hydrogen bond in the catalytic triad of serine proteases, Science 264, 1927-30 (comment).
    • (1994) Science , vol.264 , pp. 1927-1930
    • Frey, P.A.1    Whitt, S.A.2    Tobin, J.B.3
  • 14
    • 0029758171 scopus 로고    scopus 로고
    • Protonation-state dependence of hydrogen bond strengths and exchange rates in a serine protease catalytic triad: Bovine chymotrypsinogen A
    • Markley, J. L., and Westler, W. M. (1996) Protonation-state dependence of hydrogen bond strengths and exchange rates in a serine protease catalytic triad: bovine chymotrypsinogen A, Biochemistry 35, 11092-7.
    • (1996) Biochemistry , vol.35 , pp. 11092-11097
    • Markley, J.L.1    Westler, W.M.2
  • 15
    • 0031127432 scopus 로고    scopus 로고
    • Understanding enzymic catalysis: The importance of short, strong hydrogen bonds
    • Gerlt, J. A., Kreevoy, M. M., Cleland, W., and Frey, P. A. (1997) Understanding enzymic catalysis: the importance of short, strong hydrogen bonds, Chem. Biol. 4, 259-67.
    • (1997) Chem. Biol. , vol.4 , pp. 259-267
    • Gerlt, J.A.1    Kreevoy, M.M.2    Cleland, W.3    Frey, P.A.4
  • 16
    • 0032872140 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for the detection and study of low-barrier hydrogen bonds on enzymes
    • Mildvan, A. S., Harris, T. K., and Abeygunawardana, C. (1999) Nuclear magnetic resonance methods for the detection and study of low-barrier hydrogen bonds on enzymes, Methods Enzymol. 308, 219-45.
    • (1999) Methods Enzymol. , vol.308 , pp. 219-245
    • Mildvan, A.S.1    Harris, T.K.2    Abeygunawardana, C.3
  • 17
    • 10544255345 scopus 로고    scopus 로고
    • A low-barrier hydrogen bond in subtilisin: 1H and 15N NMR studies with peptidyl trifluoromethyl ketones
    • Halkides, C. J., Wu, Y. Q., and Murray, C. J. (1996) A low-barrier hydrogen bond in subtilisin: 1H and 15N NMR studies with peptidyl trifluoromethyl ketones. Biochemistry 35, 15941-8.
    • (1996) Biochemistry , vol.35 , pp. 15941-15948
    • Halkides, C.J.1    Wu, Y.Q.2    Murray, C.J.3
  • 18
    • 0030734269 scopus 로고    scopus 로고
    • NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase
    • Harris, T. K., Abeygunawardana, C., and Mildvan, A. S. (1997) NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase, Biochemistry 36, 14661-75.
    • (1997) Biochemistry , vol.36 , pp. 14661-14675
    • Harris, T.K.1    Abeygunawardana, C.2    Mildvan, A.S.3
  • 19
    • 0030819258 scopus 로고    scopus 로고
    • Hydrogen bonding at the active site of delta 5-3-ketosteroid isomerase
    • Zhao, Q., Abeygunawardana, C., Gittis, A. G., and Mildvan, A. S. (1997) Hydrogen bonding at the active site of delta 5-3-ketosteroid isomerase, Biochemistry 36, 14616-26.
    • (1997) Biochemistry , vol.36 , pp. 14616-14626
    • Zhao, Q.1    Abeygunawardana, C.2    Gittis, A.G.3    Mildvan, A.S.4
  • 20
    • 0025952945 scopus 로고
    • NMR observation of exchangeable protons of pyridoxal phosphate and histidine residues in cytosolic aspartate aminotransferase
    • Kintanar, A., Metzler, C. M., Metzler, D. E., and Scott, R. D. (1991) NMR observation of exchangeable protons of pyridoxal phosphate and histidine residues in cytosolic aspartate aminotransferase, J. Biol. Chem. 266, 17222-9.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17222-17229
    • Kintanar, A.1    Metzler, C.M.2    Metzler, D.E.3    Scott, R.D.4
  • 24
    • 0037413528 scopus 로고    scopus 로고
    • 8-Aza-immucillins as transition-state analogue inhibitors of purine nucleoside phosphorylase and nucleoside hydrolases
    • Evans, G. B., Furneaux, R. H., Gainsford, G. J., Hanson, J. C., Kicska, G. A., Sauve, A. A., Schramm, V. L., and Tyler, P. C. (2003) 8-Aza-immucillins as transition-state analogue inhibitors of purine nucleoside phosphorylase and nucleoside hydrolases, J. Med. Chem. 46, 155-60.
    • (2003) J. Med. Chem. , vol.46 , pp. 155-160
    • Evans, G.B.1    Furneaux, R.H.2    Gainsford, G.J.3    Hanson, J.C.4    Kicska, G.A.5    Sauve, A.A.6    Schramm, V.L.7    Tyler, P.C.8
  • 25
    • 0035943311 scopus 로고    scopus 로고
    • Addition of lithiated 9-deazapurine derivatives to a carbohydrate cyclic imine: Convergent synthesis of the aza-C-nucleoside immucillins
    • Evans, G. B., Furneaux, R. H., Hutchison, T. L., Kezar, H. S., Morris, P. E., Jr., Schramm, V. L., and Tyler, P. C. (2001) Addition of lithiated 9-deazapurine derivatives to a carbohydrate cyclic imine: convergent synthesis of the aza-C-nucleoside immucillins, J. Org. Chem. 66, 5723-30.
    • (2001) J. Org. Chem. , vol.66 , pp. 5723-5730
    • Evans, G.B.1    Furneaux, R.H.2    Hutchison, T.L.3    Kezar, H.S.4    Morris Jr., P.E.5    Schramm, V.L.6    Tyler, P.C.7
  • 26
    • 0000809682 scopus 로고
    • 1H Overhauser Effects in the presence of spin diffusion
    • 1H Overhauser Effects in the presence of spin diffusion, J. Magn. Reson. 33, 675-680.
    • (1979) J. Magn. Reson. , vol.33 , pp. 675-680
    • Wagner, G.1    Wüthrich, K.2
  • 27
    • 0000393431 scopus 로고
    • Theory and application of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteins
    • Clore, G. M., and Gronenborn, A. M. (1982) Theory and application of the transferred nuclear overhauser effect to the study of the conformations of small ligands bound to proteins, J. Magn. Reson. 48, 402-417.
    • (1982) J. Magn. Reson. , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 28
    • 0033580680 scopus 로고    scopus 로고
    • NMR experiments reveal distinct antibody-bound conformations of a synthetic disaccharide representing a general structural element of bacterial lipopolysaccharide epitopes
    • Haselhorst, T., Espinosa, J. F., Jimenez-Barbero, J., Sokolowski, T., Kosma, P., Brade, H., Brade, L., and Peters, T. (1999) NMR experiments reveal distinct antibody-bound conformations of a synthetic disaccharide representing a general structural element of bacterial lipopolysaccharide epitopes, Biochemistry 38, 6449-59.
    • (1999) Biochemistry , vol.38 , pp. 6449-6459
    • Haselhorst, T.1    Espinosa, J.F.2    Jimenez-Barbero, J.3    Sokolowski, T.4    Kosma, P.5    Brade, H.6    Brade, L.7    Peters, T.8
  • 29
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer, M., and Meyer, B. (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy, Angew. Chem. Int. Ed. 38, 1784-1788.
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 30
    • 79960698472 scopus 로고
    • Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients
    • Hwang, T. L., and Shaka, A. J. (1995) Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients, J. Magn. Reson., A 112, 275-279.
    • (1995) J. Magn. Reson., A , vol.112 , pp. 275-279
    • Hwang, T.L.1    Shaka, A.J.2
  • 31
    • 0033819339 scopus 로고    scopus 로고
    • Immucillin-H binding to purine nucleoside phosphorylase reduces dynamic solvent exchange
    • Wang, F., Miles, R. W., Kicska, G., Nieves, E., Schramm, V. L., and Angeletti, R. H. (2000) Immucillin-H binding to purine nucleoside phosphorylase reduces dynamic solvent exchange, Protein Sci. 9, 1660-8.
    • (2000) Protein Sci. , vol.9 , pp. 1660-1668
    • Wang, F.1    Miles, R.W.2    Kicska, G.3    Nieves, E.4    Schramm, V.L.5    Angeletti, R.H.6
  • 32
    • 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, 13212-9.
    • (1993) Biochemistry , vol.32 , pp. 13212-13219
    • Kline, P.C.1    Schramm, V.L.2
  • 33
    • 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, 1153-62.
    • (1995) Biochemistry , vol.34 , pp. 1153-1162
    • Kline, P.C.1    Schramm, V.L.2
  • 34
    • 0035695812 scopus 로고    scopus 로고
    • Atomic motion in enzymatic reaction coordinates
    • Schramm, V. L., and Shi, W. (2001) Atomic motion in enzymatic reaction coordinates, Curr. Opin. Struct. Biol. 11, 657-65.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 657-665
    • Schramm, V.L.1    Shi, W.2
  • 36
    • 0038407231 scopus 로고    scopus 로고
    • Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts
    • Neal, S., Nip, A. M., Zhang, H., and Wishart, D. S. (2003) Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts, J. Biomol. NMR 26, 215-40.
    • (2003) J. Biomol. NMR , vol.26 , pp. 215-240
    • Neal, S.1    Nip, A.M.2    Zhang, H.3    Wishart, D.S.4
  • 37
    • 10944271376 scopus 로고
    • Calculation of nuclear magnetic resonance spectra of aromatic hydrocarbon
    • Johnson, C. E., and Bovey, F. A. (1958) Calculation of nuclear magnetic resonance spectra of aromatic hydrocarbon, J. Chem. Phys. 29, 1012-1014.
    • (1958) J. Chem. Phys. , vol.29 , pp. 1012-1014
    • Johnson, C.E.1    Bovey, F.A.2
  • 38
    • 0027982960 scopus 로고
    • Hydrogen bonding in proteins as studied by amide hydrogen D/H fractionation factors: Application to staphylococcal nuclease
    • Loh, S. N., and Markley, J. L. (1994) Hydrogen bonding in proteins as studied by amide hydrogen D/H fractionation factors: application to staphylococcal nuclease, Biochemistry 33, 1029-36.
    • (1994) Biochemistry , vol.33 , pp. 1029-1036
    • Loh, S.N.1    Markley, J.L.2
  • 39
    • 33847085649 scopus 로고
    • Structures and isotopic fractionation factors of complexes, A1HA2-
    • Kreevoy, M. M., and Liang, T. M. (1980) Structures and isotopic fractionation factors of complexes, A1HA2-, J. Am. Chem. Soc. 102, 3315-3322.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 3315-3322
    • Kreevoy, M.M.1    Liang, T.M.2
  • 40
    • 0037205913 scopus 로고    scopus 로고
    • Computer simulations of trypanosomal nucleoside hydrolase: Determination of the protonation state of the bound transition-state analogue
    • Mazumder, D., Kahn, K., and Bruice, T. C. (2002) Computer simulations of trypanosomal nucleoside hydrolase: determination of the protonation state of the bound transition-state analogue, J. Am. Chem. Soc. 124, 8825-33.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8825-8833
    • Mazumder, D.1    Kahn, K.2    Bruice, T.C.3


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