메뉴 건너뛰기




Volumn 2, Issue 11, 2007, Pages 725-734

Picomolar inhibitors as transition-state probes of 5′-methylthioadenosine nucleosidases

Author keywords

[No Author keywords available]

Indexed keywords

5' METHYLTHIOADENOSINE NUCLEOSIDASE INHIBITOR; ANTIINFECTIVE AGENT; CARBON 14; DADME IMMUCILLIN A; ENZYME INHIBITOR; IMMUCILLIN A; METHYLTHIOADENOSINE NUCLEOSIDASE; NUCLEOSIDASE; TRITIUM; UNCLASSIFIED DRUG;

EID: 37349047044     PISSN: 15548929     EISSN: None     Source Type: Journal    
DOI: 10.1021/cb700166z     Document Type: Article
Times cited : (57)

References (32)
  • 1
    • 0035543093 scopus 로고    scopus 로고
    • The depth of chemical time and the power of enzymes as catalysts
    • Wolfenden, R., and Snider, M. J. (2001) The depth of chemical time and the power of enzymes as catalysts, Acc. Chem. Res. 34, 938-945.
    • (2001) Acc. Chem. Res , vol.34 , pp. 938-945
    • Wolfenden, R.1    Snider, M.J.2
  • 2
    • 27944458409 scopus 로고    scopus 로고
    • Enzymatic transition states and transition state analogues
    • Schramm, V. L. (2005) Enzymatic transition states and transition state analogues, Curr. Opin. Struct. Biol. 15, 604-613.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 604-613
    • Schramm, V.L.1
  • 3
    • 9744244983 scopus 로고    scopus 로고
    • Enzymatic transition states: Thermodynamics, dynamics and analogue design
    • Schramm, V. L. (2005) Enzymatic transition states: thermodynamics, dynamics and analogue design, Arch. Biochem. Biophys. 433, 13-26.
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 13-26
    • Schramm, V.L.1
  • 4
    • 33947201538 scopus 로고    scopus 로고
    • Transition-state analysis of S. pneumoniae 5′-methylthioadenosine nucleosidase
    • Singh, V., and Schramm, V. L. (2007) Transition-state analysis of S. pneumoniae 5′-methylthioadenosine nucleosidase, J. Am. Chem. Soc. 129, 2783-2795.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 2783-2795
    • Singh, V.1    Schramm, V.L.2
  • 5
    • 23944446462 scopus 로고    scopus 로고
    • Transition state structure of 5′-methylthioadenosine/ S-adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues
    • Singh, V., Lee, J. E., Nunez, S., Howell, P. L., and Schramm, V. L. (2005) Transition state structure of 5′-methylthioadenosine/ S-adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues, Biochemistry 44, 11647-11659.
    • (2005) Biochemistry , vol.44 , pp. 11647-11659
    • Singh, V.1    Lee, J.E.2    Nunez, S.3    Howell, P.L.4    Schramm, V.L.5
  • 6
    • 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
  • 7
    • 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
  • 8
    • 4644314829 scopus 로고    scopus 로고
    • Do electrostatic interactions with positively charged active site groups tighten the transition state for enzymatic phosphoryl transfer?
    • Nikolic-Hughes, I., Rees, D. C., and Herschlag, D. (2004) Do electrostatic interactions with positively charged active site groups tighten the transition state for enzymatic phosphoryl transfer? J. Am. Chem. Soc. 126, 11814-11819.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 11814-11819
    • Nikolic-Hughes, I.1    Rees, D.C.2    Herschlag, D.3
  • 9
    • 0032558125 scopus 로고    scopus 로고
    • Kinetic analysis of a protein tyrosine kinase reaction transition state in the forward and reverse directions
    • Kim, K., and Cole, P. A. (1998) Kinetic analysis of a protein tyrosine kinase reaction transition state in the forward and reverse directions, J. Am. Chem. Soc. 120, 6851-6858.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 6851-6858
    • Kim, K.1    Cole, P.A.2
  • 10
    • 34347227434 scopus 로고    scopus 로고
    • Transition-state variation in human, bovine, and Plasmodium falciparum adenosine deaminases
    • Luo, M., Singh, V., Taylor, E. A., and Schramm, V. L. (2007) Transition-state variation in human, bovine, and Plasmodium falciparum adenosine deaminases, J. Am. Chem. Soc. 129, 8008-8017.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 8008-8017
    • Luo, M.1    Singh, V.2    Taylor, E.A.3    Schramm, V.L.4
  • 11
  • 12
    • 9744244276 scopus 로고    scopus 로고
    • The use of isotope effects to determine enzyme mechanisms
    • Cleland, W. W. (2005) The use of isotope effects to determine enzyme mechanisms, Arch. Biochem. Biophys. 433, 2-12.
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 2-12
    • Cleland, W.W.1
  • 13
    • 0000529274 scopus 로고
    • Isotopic mapping of transition-state structural features associated with enzymic catalysis of methyl transfer
    • Rodgers, J., Femec, D. A., and Schowen, R. L. (1982) Isotopic mapping of transition-state structural features associated with enzymic catalysis of methyl transfer, J. Am. Chem. Soc. 104, 3263-3268.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 3263-3268
    • Rodgers, J.1    Femec, D.A.2    Schowen, R.L.3
  • 14
    • 0003160376 scopus 로고
    • Isotope effects on enzyme-catalyzed β-eliminations
    • Cook, P. E, Ed, pp, CRC, Boca Raton, FL
    • Anderson, V. E. (1991) Isotope effects on enzyme-catalyzed β-eliminations. In Enzyme Mechanisms from Isotope Effects (Cook, P. E, Ed.) pp 389-418, CRC, Boca Raton, FL
    • (1991) Enzyme Mechanisms from Isotope Effects , pp. 389-418
    • Anderson, V.E.1
  • 15
    • 0034897764 scopus 로고    scopus 로고
    • The LuxS family of bacterial autoinducers: Biosynthesis of a novel quorum-sensing signal molecule
    • Schauder, S., Shokat, K., Surette, M. G., and Bassler, B. L. (2001) The LuxS family of bacterial autoinducers: biosynthesis of a novel quorum-sensing signal molecule, Mol. Microbiol. 41, 463-476.
    • (2001) Mol. Microbiol , vol.41 , pp. 463-476
    • Schauder, S.1    Shokat, K.2    Surette, M.G.3    Bassler, B.L.4
  • 16
    • 0035070998 scopus 로고    scopus 로고
    • Quorum sensing as an integral component of gene regulatory networks in Gram-negative bacteria
    • Withers, H., Swift, S., and Williams, P. (2001) Quorum sensing as an integral component of gene regulatory networks in Gram-negative bacteria, Curr. Opin. Microbiol. 4, 186-193.
    • (2001) Curr. Opin. Microbiol , vol.4 , pp. 186-193
    • Withers, H.1    Swift, S.2    Williams, P.3
  • 17
    • 34547102012 scopus 로고    scopus 로고
    • A transition state analogue of 5′-methylthioadenosine phosphorylase induces apoptosis in head and neck cancers
    • Basu, I., Cordovano, G., Das, I., Belbin, T. J., Guha, C., and Schramm, V. L. (2007) A transition state analogue of 5′-methylthioadenosine phosphorylase induces apoptosis in head and neck cancers, J. Biol. Chem. 282, 21477-21486.
    • (2007) J. Biol. Chem , vol.282 , pp. 21477-21486
    • Basu, I.1    Cordovano, G.2    Das, I.3    Belbin, T.J.4    Guha, C.5    Schramm, V.L.6
  • 18
    • 22244445554 scopus 로고    scopus 로고
    • Evans, 6. B., Furneaux, R. H., Lenz, D. H., Painter, G. F., Schramm, V. L., Singh, V., and Tyler, P. C. (2005) Second generation transition state analogue inhibitors of human 5′-methylthioadenosine phosphorylase, J. Med. Chem. 48, 4679-4689.
    • Evans, 6. B., Furneaux, R. H., Lenz, D. H., Painter, G. F., Schramm, V. L., Singh, V., and Tyler, P. C. (2005) Second generation transition state analogue inhibitors of human 5′-methylthioadenosine phosphorylase, J. Med. Chem. 48, 4679-4689.
  • 19
    • 2542531592 scopus 로고    scopus 로고
    • Targeting the polyamine pathway with transition-state analogue inhibitors of 5′-methylthioadenosine phosphorylase
    • Evans, G. B., Furneaux, R. H., Schramm, V. L, Singh, V., and Tyler, P. C. (2004) Targeting the polyamine pathway with transition-state analogue inhibitors of 5′-methylthioadenosine phosphorylase, J. Med. Chem. 47, 3275-8281.
    • (2004) J. Med. Chem , vol.47 , pp. 3275-8281
    • Evans, G.B.1    Furneaux, R.H.2    Schramm, V.L.3    Singh, V.4    Tyler, P.C.5
  • 23
    • 33750979005 scopus 로고    scopus 로고
    • Transition-state structure of human 5′-methylthioadenosine phosphorylase
    • Singh, V., and Schramm, V. L. (2006) Transition-state structure of human 5′-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
  • 25
    • 1542366683 scopus 로고    scopus 로고
    • Nucleophilic participation in the transition state for human thymidine phosphorylase
    • Birck, M. R., and Schramm, V. L. (2004) Nucleophilic participation in the transition state for human thymidine phosphorylase, J. Am. Chem. Soc. 126, 2447-2453.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 2447-2453
    • Birck, M.R.1    Schramm, V.L.2
  • 26
    • 0016832598 scopus 로고
    • Steady-state analysis of kinetic isotope effects in enzymic reactions
    • Northrop, D. B. (1975) Steady-state analysis of kinetic isotope effects in enzymic reactions, Biochemistry 14, 2644-2651.
    • (1975) Biochemistry , vol.14 , pp. 2644-2651
    • Northrop, D.B.1
  • 27
    • 23944452200 scopus 로고    scopus 로고
    • Structural rationale for the affinity of pico- and femtomolar transition state analogues of Escherichia coli 5′-methylthioadenosine/ S-adenosylhomocysteine nucleosidase
    • Lee, J. E., Singh, V., Evans, G. B., Tyler, P. C., Furneaux, R. H., Cornell, K. A., Riscoe, M. K., Schramm, V. L., and Howell, P. L. (2005) Structural rationale for the affinity of pico- and femtomolar transition state analogues of Escherichia coli 5′-methylthioadenosine/ S-adenosylhomocysteine nucleosidase, J. Biol. Chem. 280, 18274-18282.
    • (2005) J. Biol. Chem , vol.280 , pp. 18274-18282
    • Lee, J.E.1    Singh, V.2    Evans, G.B.3    Tyler, P.C.4    Furneaux, R.H.5    Cornell, K.A.6    Riscoe, M.K.7    Schramm, V.L.8    Howell, P.L.9
  • 28
    • 0346096864 scopus 로고    scopus 로고
    • Picomolar transition state analogue inhibitors of human 5′-methylthioadenosine phosphorylase and X-ray structure with MT-immucillin-A
    • Singh, V., Shi, W., Evans, G. B., Tyler, P. C., Furneaux, R. H., Almo, S. C., and Schramm, V. L. (2004) Picomolar transition state analogue inhibitors of human 5′-methylthioadenosine phosphorylase and X-ray structure with MT-immucillin-A, Biochemistry 43, 9-18.
    • (2004) Biochemistry , vol.43 , pp. 9-18
    • Singh, V.1    Shi, W.2    Evans, G.B.3    Tyler, P.C.4    Furneaux, R.H.5    Almo, S.C.6    Schramm, V.L.7
  • 29
    • 13644264724 scopus 로고    scopus 로고
    • Membrane dynamics of the amphiphilic siderophore, acinetoferrin
    • Luo, M., Fadeev, E. A., and Groves, J. T. (2005) Membrane dynamics of the amphiphilic siderophore, acinetoferrin, J. Am. Chem. Soc. 127, 1726-1736.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 1726-1736
    • Luo, M.1    Fadeev, E.A.2    Groves, J.T.3
  • 31
    • 34250201455 scopus 로고    scopus 로고
    • Transition state analysis of acid-catalyzed dAMP hydrolysis
    • McCann, 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
    • McCann, J.A.B.1    Berti, P.J.2
  • 32
    • 36148932926 scopus 로고    scopus 로고
    • Transition state structure of Neisseria meningitides 5′methylthioadenosine/S-adenosylhomocysteine nucleosidase
    • in press
    • Singh, V., Luo, M., Brown, R. L, Norris, G. E., and Schramm, V. L. (2007) Transition state structure of Neisseria meningitides 5′methylthioadenosine/S-adenosylhomocysteine nucleosidase. J. Am. Chem. Soc., in press
    • (2007) J. Am. Chem. Soc
    • Singh, V.1    Luo, M.2    Brown, R.L.3    Norris, G.E.4    Schramm, V.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.