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Volumn 5, Issue 5, 1998, Pages 369-376

Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSYLHOMOCYSTEINASE; S ADENOSYLMETHIONINE;

EID: 0031947190     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0598-369     Document Type: Review
Times cited : (144)

References (54)
  • 2
    • 70449254180 scopus 로고
    • The enzymatic synthesis of S-adenosyl-L-homocysteine from adenosine and homocysteine
    • de la Haba, G. & Cantoni, G. The enzymatic synthesis of S-adenosyl-L-homocysteine from adenosine and homocysteine. J. Biol. Chem. 234, 603-608 (1959).
    • (1959) J. Biol. Chem. , vol.234 , pp. 603-608
    • De La Haba, G.1    Cantoni, G.2
  • 3
    • 0020284631 scopus 로고
    • Pharmacological and biochemical aspects of S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase
    • Ueland, P.M. Pharmacological and biochemical aspects of S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase. Pharmacol. Rev. 34, 223-253 (1982).
    • (1982) Pharmacol. Rev. , vol.34 , pp. 223-253
    • Ueland, P.M.1
  • 4
    • 0028269238 scopus 로고
    • The mouse lethal nonagouti (Ax) mutation deletes the S-adenosylhomocysteine hydrolase (Ahcy) gene
    • Miller, M.W. et al. The mouse lethal nonagouti (Ax) mutation deletes the S-adenosylhomocysteine hydrolase (Ahcy) gene. EMBO J 13, 1806-1816 (1994).
    • (1994) EMBO J , vol.13 , pp. 1806-1816
    • Miller, M.W.1
  • 5
    • 0018800321 scopus 로고
    • The mechanism of action of S-adenosylhomocysteinase
    • Palmer, J.L & Abeles, R.H. The mechanism of action of S-adenosylhomocysteinase. J. Biol. Chem. 254, 1217-1226 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 1217-1226
    • Palmer, J.L.1    Abeles, R.H.2
  • 6
    • 0018075296 scopus 로고
    • S-adenosylhomocysteine hydrolase is an adenosine-binding protein: A target for adenosine toxicity
    • Hershfield, M.S., Kredich, N.M. S-adenosylhomocysteine hydrolase is an adenosine-binding protein: a target for adenosine toxicity. Science 202, 757-760 (1978).
    • (1978) Science , vol.202 , pp. 757-760
    • Hershfield, M.S.1    Kredich, N.M.2
  • 8
    • 0017717986 scopus 로고
    • Role of S-adenosylhomocysteine in adenosinemediated toxicity in cultured mouse T lymphoma cells
    • Kredich, N.M. & Martin, D.W., Jr. Role of S-adenosylhomocysteine in adenosinemediated toxicity in cultured mouse T lymphoma cells. Cell 12, 931-938 (1977).
    • (1977) Cell , vol.12 , pp. 931-938
    • Kredich, N.M.1    Martin Jr., D.W.2
  • 9
    • 0018765904 scopus 로고
    • In vivo inactivation of erythrocyte S-adenosylhomocysteine hydrolase by 2′-deoxyadenosine in adenosine deaminase-deficient patients
    • Hershfield, M.S., Kredich, N.M., Ownby, D.R., Ownby, H. & Buckley, R. In vivo inactivation of erythrocyte S-adenosylhomocysteine hydrolase by 2′-deoxyadenosine in adenosine deaminase-deficient patients. J. Clin. Invest. 63, 807-811 (1979).
    • (1979) J. Clin. Invest. , vol.63 , pp. 807-811
    • Hershfield, M.S.1    Kredich, N.M.2    Ownby, D.R.3    Ownby, H.4    Buckley, R.5
  • 10
    • 0025866175 scopus 로고
    • S-adenosyl-L-homocysteine hydrolase as a target for antiviral chemotherapy
    • Wolfe, M.S., Borchardt, R.T. S-adenosyl-L-homocysteine hydrolase as a target for antiviral chemotherapy. J. Med. Chem. 34, 1521-1530 (1991).
    • (1991) J. Med. Chem. , vol.34 , pp. 1521-1530
    • Wolfe, M.S.1    Borchardt, R.T.2
  • 11
    • 0025298557 scopus 로고
    • Antimalarial activity of a 4′,5′-unsaturated 5′-fluoroadenosine mechanism-based inhibitor of S-adenosyl-L-homocysteine hydrolase
    • Bitonti, A.J., Baumann, R.J., Jarvi, E.T., McCarthy, J.R. & McCann, P.P. Antimalarial activity of a 4′,5′-unsaturated 5′-fluoroadenosine mechanism-based inhibitor of S-adenosyl-L-homocysteine hydrolase. Biochem. Pharmacol. 40, 601-606 (1990).
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 601-606
    • Bitonti, A.J.1    Baumann, R.J.2    Jarvi, E.T.3    McCarthy, J.R.4    McCann, P.P.5
  • 12
    • 0027293757 scopus 로고
    • Immunosuppression mediated by an inhibitor of S-adenosyl-L-homocysteine hydrolase. Prevention and treatment of collagen-induced arthritis
    • Wolos, J.A., Frondorf, K.A. & Esser, R.E. Immunosuppression mediated by an inhibitor of S-adenosyl-L-homocysteine hydrolase. Prevention and treatment of collagen-induced arthritis. J. Immunol. 151, 526-534 (1993).
    • (1993) J. Immunol. , vol.151 , pp. 526-534
    • Wolos, J.A.1    Frondorf, K.A.2    Esser, R.E.3
  • 13
    • 0030958787 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of human placental S-adenosylhomocysteine hydrolase
    • Turner, M.A. et al. Crystallization and preliminary X-ray analysis of human placental S-adenosylhomocysteine hydrolase. Acta Crystallogr. D53, 339-341 (1997).
    • (1997) Acta Crystallogr. , vol.D53 , pp. 339-341
    • Turner, M.A.1
  • 14
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58 (1991).
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 15
    • 0027232494 scopus 로고
    • Effects of 4′-modified analogs of aristeromycin on the metabolism of S-adenosyl-L-homocysteine in murine L929 cells
    • Ault-Riche, D.B. et al. Effects of 4′-modified analogs of aristeromycin on the metabolism of S-adenosyl-L-homocysteine in murine L929 cells. Mol. Pharmacol. 43, 989-997 (1993).
    • (1993) Mol. Pharmacol. , vol.43 , pp. 989-997
    • Ault-Riche, D.B.1
  • 18
    • 0031045818 scopus 로고    scopus 로고
    • Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement
    • Ramakrishnan, V. & Biou, V. Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement. Meths Enz. 76, 538-557 (1997).
    • (1997) Meths Enz. , vol.76 , pp. 538-557
    • Ramakrishnan, V.1    Biou, V.2
  • 19
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program for processing and analyzing diffraction data from macromolecules in Methods
    • eds. Carter, C.W. & Sweet, R.M. Academic Press, New York
    • Furey, W. & Swaninathan, S. PHASES-95: A program for processing and analyzing diffraction data from macromolecules in Methods in Enzymology (eds. Carter, C.W. & Sweet, R.M.) 590-633 (Academic Press, New York, 1997).
    • (1997) Enzymology , pp. 590-633
    • Furey, W.1    Swaninathan, S.2
  • 20
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR System (CNS): A new software system for macromolecular structure determination
    • submitted
    • Brünger, A.T. et al. Crystallography and NMR System (CNS): A new software system for macromolecular structure determination. Acta Crystallogr. D, submitted (1998).
    • (1998) Acta Crystallogr. D
    • Brünger, A.T.1
  • 21
    • 0030841589 scopus 로고    scopus 로고
    • Detecting folding motifs and similarities in protein structures
    • Kleijwegt, G.J. & Jones, T.A. Detecting folding motifs and similarities in protein structures. Meths Enz. 277, 525-545 (1997).
    • (1997) Meths Enz. , vol.277 , pp. 525-545
    • Kleijwegt, G.J.1    Jones, T.A.2
  • 22
    • 0026536258 scopus 로고
    • Crystal structure of NAD-dependent formate dehydrogenase
    • Lamzin, V.S. et al. Crystal structure of NAD-dependent formate dehydrogenase, Eur. J. Biochem. 206, 441-452 (1992).
    • (1992) Eur. J. Biochem. , vol.206 , pp. 441-452
    • Lamzin, V.S.1
  • 24
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34, 167-339 (1981).
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 25
    • 0029562477 scopus 로고
    • NAD-binding domains of dehydrogenases
    • Lesk, A.M. NAD-binding domains of dehydrogenases. Curr. Opin. Struct. Biol. 5, 775-783 (1995).
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 775-783
    • Lesk, A.M.1
  • 26
    • 0002815512 scopus 로고
    • D-Glyceraldehyde-3-phosphate dehydrogenase: Three-dimensional structure and evolutionary significance
    • Buehner, M., Ford, G.C., Moras, D., Olsen, K.W. & Rossmann, M.G. D-Glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance. Proc. Natl. Acad. Sci. USA 70, 3052-3054 (1973).
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3052-3054
    • Buehner, M.1    Ford, G.C.2    Moras, D.3    Olsen, K.W.4    Rossmann, M.G.5
  • 27
    • 0029108068 scopus 로고
    • Structure of 6-phosphogluconate dehydrogenase refined at 2Å resolution
    • Philips, C., Gover, S. & Adams, M.J. Structure of 6-phosphogluconate dehydrogenase refined at 2Å resolution. Acta Crystallogr. D51, 290-307 (1995).
    • (1995) Acta Crystallogr. , vol.D51 , pp. 290-307
    • Philips, C.1    Gover, S.2    Adams, M.J.3
  • 28
    • 0025838697 scopus 로고
    • Three-dimensional structure of holo 3α,20β-hydroxysteroid dehydrogenase: A member of a short-chain dehydrogenase family
    • Ghosh, D. et al. Three-dimensional structure of holo 3α,20β-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family. Proc. Natl. Acad Sci. USA 88, 10064-10068 (1991).
    • (1991) Proc. Natl. Acad Sci. USA , vol.88 , pp. 10064-10068
    • Ghosh, D.1
  • 30
    • 0029919169 scopus 로고    scopus 로고
    • Three-dimensional structure of the inosine-uridine nucleoside N-ribohydrolase from Crithidia fasciculata
    • Degano, M., Gopaul, D.N., Scapin, G., Schramm, V.L. & Sacchettini, J.C. Three-dimensional structure of the inosine-uridine nucleoside N-ribohydrolase from Crithidia fasciculata. Biochemistry 35, 5971-5981 (1996).
    • (1996) Biochemistry , vol.35 , pp. 5971-5981
    • Degano, M.1    Gopaul, D.N.2    Scapin, G.3    Schramm, V.L.4    Sacchettini, J.C.5
  • 31
    • 0028081341 scopus 로고
    • A single mutation at lysine 426 of human placental S-adenosylhomocysteine hydrolase inactivates the enzyme
    • Ault-Riche, D.B., Yuan, C.S. & Borchardt, R.T. A single mutation at lysine 426 of human placental S-adenosylhomocysteine hydrolase inactivates the enzyme. J. Biol. Chem. 269, 31472-31478 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 31472-31478
    • Ault-Riche, D.B.1    Yuan, C.S.2    Borchardt, R.T.3
  • 32
    • 0028278602 scopus 로고
    • Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 Å resolution
    • Goldberg, J.D., Yoshida, T. & Brick, P. Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 Å resolution. J. Mol. Biol. 236, 1123-1140 (1994).
    • (1994) J. Mol. Biol. , vol.236 , pp. 1123-1140
    • Goldberg, J.D.1    Yoshida, T.2    Brick, P.3
  • 33
    • 77956844792 scopus 로고    scopus 로고
    • Design and synthesis of S-Adenosylhomocysteine hydrolase inhibitors as broad-spectrum antiviral agents
    • Yuan, C.-S., Liu, S., Wnuk, S.F., Robins, M.J., Borchardt, R.T. Design and synthesis of S-Adenosylhomocysteine hydrolase inhibitors as broad-spectrum antiviral agents. Adv. Antiviral Drug Des. 2, 41-88 (1996).
    • (1996) Adv. Antiviral Drug Des. , vol.2 , pp. 41-88
    • Yuan, C.-S.1    Liu, S.2    Wnuk, S.F.3    Robins, M.J.4    Borchardt, R.T.5
  • 34
    • 0020491939 scopus 로고
    • S-Adenosylhomocysteinase: Mechanism of inactivation by 2′-deoxyadenosine and interaction with other nucleosides
    • Abeles, R.H., Fish, S. & Lapinskas, B. S-Adenosylhomocysteinase: Mechanism of inactivation by 2′-deoxyadenosine and interaction with other nucleosides. Biochemistry 21, 5557-5562 (1982).
    • (1982) Biochemistry , vol.21 , pp. 5557-5562
    • Abeles, R.H.1    Fish, S.2    Lapinskas, B.3
  • 35
    • 0028030684 scopus 로고
    • Low-barrier hydrogen bonds and enzymic catalysis
    • Cleland, W.W. & Kreevoy, M.M. Low-barrier hydrogen bonds and enzymic catalysis. Science 264, 1887-1890 (1994).
    • (1994) Science , vol.264 , pp. 1887-1890
    • Cleland, W.W.1    Kreevoy, M.M.2
  • 36
    • 0022256696 scopus 로고
    • Chemical modification of S-adenosylhomocysteinase by a water-soluble carbodiimide
    • Takata, Y., Tomoharu, G. & Fujioka, M. Chemical modification of S-adenosylhomocysteinase by a water-soluble carbodiimide. Arch. Biochem. Biophys. 240, 827-835 (1985).
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 827-835
    • Takata, Y.1    Tomoharu, G.2    Fujioka, M.3
  • 37
    • 0022999804 scopus 로고
    • S-adenosylhomocysteinase from rat liver. Amino acid sequences of the peptides containing active site cysteine residues modified by treatment with 5′-p-fluorosulfonylbenzoyladenosine
    • Gomi, T., Ogawa, H. & Fujioka, M. S-adenosylhomocysteinase from rat liver. Amino acid sequences of the peptides containing active site cysteine residues modified by treatment with 5′-p-fluorosulfonylbenzoyladenosine. J. Biol. Chem. 261, 13422-13425 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 13422-13425
    • Gomi, T.1    Ogawa, H.2    Fujioka, M.3
  • 38
    • 0021760631 scopus 로고
    • 5′-[p-(Fluorosulfonyl)benzoyl] adenosine-mediated inactivation of S-adenosylhomocysteinase
    • Takata, Y. & Fujioka, M. 5′-[p-(Fluorosulfonyl)benzoyl] adenosine-mediated inactivation of S-adenosylhomocysteinase. Biochemistry 23, 4357-4362 (1984).
    • (1984) Biochemistry , vol.23 , pp. 4357-4362
    • Takata, Y.1    Fujioka, M.2
  • 39
    • 0021094369 scopus 로고
    • Evidence for an essential histidine residue in S-adenosylhomocysteinase from rat liver
    • Gomi, T. & Fujioka, M. Evidence for an essential histidine residue in S-adenosylhomocysteinase from rat liver. Biochemistry 22, 137-143 (1983).
    • (1983) Biochemistry , vol.22 , pp. 137-143
    • Gomi, T.1    Fujioka, M.2
  • 40
    • 0027507869 scopus 로고
    • Ligand-dependent changes in intrinsic fluorescence of S-adenosylhomocysteine hydrolase: Implications for the mechanism of inhibitor-induced inhibition
    • Yuan, C.-S., Yeh, J., Squier, T.C., Rawitch, A. & Borchardt, R.T. Ligand-dependent changes in intrinsic fluorescence of S-adenosylhomocysteine hydrolase: implications for the mechanism of inhibitor-induced inhibition. Biochemistry 32, 10414-10422 (1993).
    • (1993) Biochemistry , vol.32 , pp. 10414-10422
    • Yuan, C.-S.1    Yeh, J.2    Squier, T.C.3    Rawitch, A.4    Borchardt, R.T.5
  • 42
    • 0028079891 scopus 로고
    • (E)-5′,6′-didehydro-6′-deoxy-6′- fluorohomoadenosine: A substrate that measures the hydrolytic activity ofS-adenosylhomocysteine hydrolase
    • Yuan, C.S., Wnuk, S.F., Liu, S., Robins, M.J. & Borchardt, R.T. (E)-5′,6′-didehydro-6′-deoxy-6′-fluorohomoadenosine: a substrate that measures the hydrolytic activity ofS-adenosylhomocysteine hydrolase. Biochemistry 33, 12305-12311 (1994).
    • (1994) Biochemistry , vol.33 , pp. 12305-12311
    • Yuan, C.S.1    Wnuk, S.F.2    Liu, S.3    Robins, M.J.4    Borchardt, R.T.5
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Meths Enz. 276, 307-326 (1997).
    • (1997) Meths Enz. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 84952400925 scopus 로고
    • Data reduction and error analysis for accurate single crystal diffraction intensities
    • Blessing, R.H. Data reduction and error analysis for accurate single crystal diffraction intensities. Crystallogr. Rev. 1, 3-58 (1987).
    • (1987) Crystallogr. Rev. , vol.1 , pp. 3-58
    • Blessing, R.H.1
  • 45
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French, S. & Wilson, K. On the treatment of negative intensity observations. Acta Crystallogr. A34, 517-525 (1978).
    • (1978) Acta Crystallogr. , vol.A34 , pp. 517-525
    • French, S.1    Wilson, K.2
  • 47
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 48
    • 0002700643 scopus 로고
    • eds. Bailey, S., Hubbard, R. & Waller, D. SERC Daresbury, Warrington;
    • Kleijwegt, G.J. & Jones, T.A. In From first map to final model (eds. Bailey, S., Hubbard, R. & Waller, D.) 59-66 (SERC Daresbury, Warrington; 1994).
    • (1994) From First Map to Final Model , pp. 59-66
    • Kleijwegt, G.J.1    Jones, T.A.2
  • 49
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474 (1992).
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 50
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 51
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 52
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G. & Thornton, J.M. PROMOTIF - a program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 53
    • 0028181017 scopus 로고
    • An algorithm for automatically generating protein topology cartoons
    • Flores, T.P., Moss, D.S. & Thornton, J.M. An algorithm for automatically generating protein topology cartoons. Protein Engng. 7, 31-37 (1994).
    • (1994) Protein Engng. , vol.7 , pp. 31-37
    • Flores, T.P.1    Moss, D.S.2    Thornton, J.M.3
  • 54
    • 0003456102 scopus 로고
    • Yale University Press, New Haven, Connecticut
    • Brünger, A.T. XPLOR Version 3.1 (Yale University Press, New Haven, Connecticut; 1993).
    • (1993) XPLOR Version 3.1
    • Brünger, A.T.1


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