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Volumn 45, Issue 25, 2006, Pages 7778-7786

Effects of ligand binding and oxidation on hinge-bending motions in S-adenosyl-L-homocysteine hydrolase

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; COMPLEXATION; ENZYMES; MOLECULAR STRUCTURE; OXIDATION; SUBSTRATES;

EID: 33746888705     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0523106     Document Type: Article
Times cited : (15)

References (17)
  • 1
    • 70449254180 scopus 로고
    • The enzymatic synthesis of S-adenosyl-L-homocy steine from adenosine and homocysteine
    • de la Haba, G., and Cantoni, G. L. (1959) The enzymatic synthesis of S-adenosyl-L-homocy steine from adenosine and homocysteine, J. Biol. Chem. 234, 603-608.
    • (1959) J. Biol. Chem. , vol.234 , pp. 603-608
    • De La Haba, G.1    Cantoni, G.L.2
  • 3
    • 18544386701 scopus 로고    scopus 로고
    • Domain motions and the open-to-closed conformational transition of an enzyme: A normal mode analysis of 5-adenosyl-L-homocysteine hydrolase
    • Wang, M., Borchardt, R. T., Schowen, R. L., and Kuczera, K. (2005) Domain motions and the open-to-closed conformational transition of an enzyme: A normal mode analysis of 5-adenosyl-L-homocysteine hydrolase, Biochemistry 44, 7228-7239.
    • (2005) Biochemistry , vol.44 , pp. 7228-7239
    • Wang, M.1    Borchardt, R.T.2    Schowen, R.L.3    Kuczera, K.4
  • 5
    • 0031947190 scopus 로고    scopus 로고
    • Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength
    • Turner, M. A., Yuan, C. S., Borchardt, R. T., Hershfield, M. S., Smith, G. D., and Howell, P. L. (1998) Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength, Nat. Struct. Biol. 5, 369-376.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 369-376
    • Turner, M.A.1    Yuan, C.S.2    Borchardt, R.T.3    Hershfield, M.S.4    Smith, G.D.5    Howell, P.L.6
  • 7
    • 0034664088 scopus 로고    scopus 로고
    • Substrate binding stabilizes S-adenosylhomocysteine hydrolase in a closed conformation
    • Yin, D., Yang, X., Hu, Y., Kuczera, K., Schowen, R. L., Borchardt, R. T., and Squier, T. C. (2000) Substrate binding stabilizes S-adenosylhomocysteine hydrolase in a closed conformation, Biochemistry 39, 9811-9818.
    • (2000) Biochemistry , vol.39 , pp. 9811-9818
    • Yin, D.1    Yang, X.2    Hu, Y.3    Kuczera, K.4    Schowen, R.L.5    Borchardt, R.T.6    Squier, T.C.7
  • 8
    • 0037172784 scopus 로고    scopus 로고
    • Contributions of active site residues to the partial and overall catalytic activities of human S-adenosylhomocysteine hydrolase
    • Elrod, P., Zhang, J., Yang, X., Yin, D., Hu, Y., Borchardt, R. T., and Schowen, R. L. (2002) Contributions of active site residues to the partial and overall catalytic activities of human S-adenosylhomocysteine hydrolase, Biochemistry 41, 8134-8142.
    • (2002) Biochemistry , vol.41 , pp. 8134-8142
    • Elrod, P.1    Zhang, J.2    Yang, X.3    Yin, D.4    Hu, Y.5    Borchardt, R.T.6    Schowen, R.L.7
  • 9
    • 33746933117 scopus 로고    scopus 로고
    • Ph.D. Thesis, Department of Molecular Biosciences, University of Kansas, Lawrence, KS
    • Wang, M. (2005) Ph.D. Thesis, Department of Molecular Biosciences, University of Kansas, Lawrence, KS.
    • (2005)
    • Wang, M.1
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0029961930 scopus 로고    scopus 로고
    • Chemical modification and site-directed mutagenesis of cysteine residues in human placental S-adenosylhomocysteine hydrolase
    • Yuan, C. S., Ault-Riche, D. B., and Borchardt, R. T. (1996) Chemical modification and site-directed mutagenesis of cysteine residues in human placental S-adenosylhomocysteine hydrolase, J. Biol. Chem. 271, 28009-28016.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28009-28016
    • Yuan, C.S.1    Ault-Riche, D.B.2    Borchardt, R.T.3
  • 12
    • 17844387194 scopus 로고    scopus 로고
    • Fluorescence properties of fluorescein, tetramethyl-rhodamine and Texas Red linked to a DNA aptamer
    • Unruh, J. R., Gokulrangan, G., Wilson, G. S., and Johnson, C. K. (2005) Fluorescence properties of fluorescein, tetramethyl-rhodamine and Texas Red linked to a DNA aptamer, Photochem. Photobiol. 81, 682-690.
    • (2005) Photochem. Photobiol. , vol.81 , pp. 682-690
    • Unruh, J.R.1    Gokulrangan, G.2    Wilson, G.S.3    Johnson, C.K.4
  • 13
    • 0026718393 scopus 로고
    • Parameter estimation by least-squares methods
    • Johnson, M. L., and Faunt, L. M. (1992) Parameter estimation by least-squares methods, Methods Enzymol. 210, 1-37.
    • (1992) Methods Enzymol. , vol.210 , pp. 1-37
    • Johnson, M.L.1    Faunt, L.M.2
  • 14
    • 0037465432 scopus 로고    scopus 로고
    • Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: Transition-state stabilization and the avoidance of abortive reactions
    • Yang, X., Hu, Y., Yin, D. H., Turner, M. A., Wang, M., Borchardt, R. T., Howell, P. L., Kuczera, K., and Schowen, R. L. (2003) Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: Transition-state stabilization and the avoidance of abortive reactions, Biochemistry 42, 1900-1909.
    • (2003) Biochemistry , vol.42 , pp. 1900-1909
    • Yang, X.1    Hu, Y.2    Yin, D.H.3    Turner, M.A.4    Wang, M.5    Borchardt, R.T.6    Howell, P.L.7    Kuczera, K.8    Schowen, R.L.9
  • 15
    • 0025786181 scopus 로고
    • Mechanism of bovine liver S-adenosylhomocysteine hydrolase. Steady-state and pre-steady-state kinetic analysis
    • Porter, D. J., and Boyd, F. L. (1991) Mechanism of bovine liver S-adenosylhomocysteine hydrolase. Steady-state and pre-steady-state kinetic analysis, J. Biol. Chem. 266, 21616-21625.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21616-21625
    • Porter, D.J.1    Boyd, F.L.2
  • 16
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia de la Torre, J., Huertas, M. L., and Carrasco, B. (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure, Biophys. J. 78, 719-730.
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.