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Volumn 165, Issue 3, 2009, Pages 133-139

Crystal structures of the Apo and Holo form of rat catechol-O-methyltransferase

Author keywords

Apo form; Catechol O methyltransferase; Holo form; X ray crystal structure

Indexed keywords

APOENZYME; CATECHOL METHYLTRANSFERASE; HOLOENZYME; LIGAND; S ADENOSYLMETHIONINE;

EID: 58849155679     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.11.012     Document Type: Article
Times cited : (19)

References (31)
  • 1
    • 0036784071 scopus 로고    scopus 로고
    • Kinetics and crystal structure of catechol-O-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application
    • Bonifacio M.J., Archer M., Rodrigues M.L., Matias P.M., Learmonth D.A., Carrondo M.A., and Soares-Da-Silva P. Kinetics and crystal structure of catechol-O-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application. Mol. Pharmacol. 62 (2002) 795-805
    • (2002) Mol. Pharmacol. , vol.62 , pp. 795-805
    • Bonifacio, M.J.1    Archer, M.2    Rodrigues, M.L.3    Matias, P.M.4    Learmonth, D.A.5    Carrondo, M.A.6    Soares-Da-Silva, P.7
  • 3
    • 0028103275 scopus 로고    scopus 로고
    • CCP4: Collaborative Computational Project Number 4, 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • CCP4: Collaborative Computational Project Number 4, 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
  • 4
    • 0032501378 scopus 로고    scopus 로고
    • Importance of correlated motions in forming highly reactive near attack conformations in catechol O-methyltransferase
    • Edmond Y.L., and Thomas C.B. Importance of correlated motions in forming highly reactive near attack conformations in catechol O-methyltransferase. J. Am. Chem. Soc. 120 (1998) 12387-12394
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12387-12394
    • Edmond, Y.L.1    Thomas, C.B.2
  • 5
    • 0034596363 scopus 로고    scopus 로고
    • Comparison of the dynamics for ground-state and transition-state structures in the active site of catechol-O-methyltransferase
    • Edmond Y.L., and Thomas C.B. Comparison of the dynamics for ground-state and transition-state structures in the active site of catechol-O-methyltransferase. J. Am. Chem. Soc. 122 (2000) 7165-7171
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7165-7171
    • Edmond, Y.L.1    Thomas, C.B.2
  • 6
    • 0016829492 scopus 로고
    • Catechol-O-methyltransferase: Pharmacological aspects and physiological role
    • Guldberg H.C., and Marsden C.A. Catechol-O-methyltransferase: Pharmacological aspects and physiological role. Pharmacol. Rev. 27 (1975) 135-206
    • (1975) Pharmacol. Rev. , vol.27 , pp. 135-206
    • Guldberg, H.C.1    Marsden, C.A.2
  • 9
    • 0035133553 scopus 로고    scopus 로고
    • Molecular mechanism controlling the rate and specificity of catechol O-methyltransferase by human soluble catechol O-methyltransferase
    • Lautala P., Ulmanen I., and Taskinen J. Molecular mechanism controlling the rate and specificity of catechol O-methyltransferase by human soluble catechol O-methyltransferase. Mol. Pharmacol. 59 (2001) 393-402
    • (2001) Mol. Pharmacol. , vol.59 , pp. 393-402
    • Lautala, P.1    Ulmanen, I.2    Taskinen, J.3
  • 10
    • 9744243460 scopus 로고    scopus 로고
    • Synthesis, biological evaluation, and molecular modeling studies of a novel, peripherally selective inhibitor of catechol-O-methyltransferase
    • Learmonth D.A., Palma P.N., Vieira-Coelho M.A., and Soares-Da-Silva P. Synthesis, biological evaluation, and molecular modeling studies of a novel, peripherally selective inhibitor of catechol-O-methyltransferase. J. Med. Chem. 47 (2004) 6207-6217
    • (2004) J. Med. Chem. , vol.47 , pp. 6207-6217
    • Learmonth, D.A.1    Palma, P.N.2    Vieira-Coelho, M.A.3    Soares-Da-Silva, P.4
  • 11
    • 0000942054 scopus 로고    scopus 로고
    • X-ray crystal structure of a bisubstrate inhibitor bound to the enzyme catechol-O-methyltransferase: a dramatic effect of inhibitor preorganization on binding affinity
    • Lerner C., Ruf A., Gramlich V., Masjost B., Zürcher G., Joakob-Roetne R., Borroni E., and Diederich F. X-ray crystal structure of a bisubstrate inhibitor bound to the enzyme catechol-O-methyltransferase: a dramatic effect of inhibitor preorganization on binding affinity. Angew. Chem. Int. Ed. 113 (2001) 4164-4166
    • (2001) Angew. Chem. Int. Ed. , vol.113 , pp. 4164-4166
    • Lerner, C.1    Ruf, A.2    Gramlich, V.3    Masjost, B.4    Zürcher, G.5    Joakob-Roetne, R.6    Borroni, E.7    Diederich, F.8
  • 12
    • 58849088851 scopus 로고    scopus 로고
    • Leslie, A.G.W., 1992. Recent changes to the MOSFLM package for processing film and image plate data. In: Joint CCP4 and ESF-EAMCB Newsletter on Protein Crystallography, vol. 26. Daresbury Laboratory, Warrington, United Kingdom.
    • Leslie, A.G.W., 1992. Recent changes to the MOSFLM package for processing film and image plate data. In: Joint CCP4 and ESF-EAMCB Newsletter on Protein Crystallography, vol. 26. Daresbury Laboratory, Warrington, United Kingdom.
  • 13
    • 0028918413 scopus 로고
    • Kinetics of human soluble and membrane-bound catechol-O-methyltransferase: a revised mechanism and description of the thermolabile variant of the enzyme
    • Lotta T., Vidgren J., Tilgmann C., Ulmanen I., Melén K., Julkunen I., and Taskinen J. Kinetics of human soluble and membrane-bound catechol-O-methyltransferase: a revised mechanism and description of the thermolabile variant of the enzyme. Biochemistry 34 (1995) 4202-4210
    • (1995) Biochemistry , vol.34 , pp. 4202-4210
    • Lotta, T.1    Vidgren, J.2    Tilgmann, C.3    Ulmanen, I.4    Melén, K.5    Julkunen, I.6    Taskinen, J.7
  • 14
    • 0026595563 scopus 로고
    • Expression of enzymatically active rat live and human placental catechol-O-methyltransferase in Escherichia coli; purification and partial characterization of the enzyme
    • Lundstrom K., Tilgman C., Peranen J., Kalkkinen K., and Ulmanen I. Expression of enzymatically active rat live and human placental catechol-O-methyltransferase in Escherichia coli; purification and partial characterization of the enzyme. Biochim. Biophys. Acta 1129 (1992) 149-154
    • (1992) Biochim. Biophys. Acta , vol.1129 , pp. 149-154
    • Lundstrom, K.1    Tilgman, C.2    Peranen, J.3    Kalkkinen, K.4    Ulmanen, I.5
  • 15
    • 0024511327 scopus 로고
    • New selective COMT inhibitors: useful adjuncts for Parkinson's disease?
    • Männistö P.T., and Kaakkola S. New selective COMT inhibitors: useful adjuncts for Parkinson's disease?. Trends Pharmacol. Sci. 10 (1989) 54-56
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 54-56
    • Männistö, P.T.1    Kaakkola, S.2
  • 16
    • 0038287034 scopus 로고    scopus 로고
    • Catechol-O-methyltransferase (COMT): biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors
    • Männistö P.T., and Kaakkola S. Catechol-O-methyltransferase (COMT): biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors. Pharmacol. Rev. 51 (1999) 593-628
    • (1999) Pharmacol. Rev. , vol.51 , pp. 593-628
    • Männistö, P.T.1    Kaakkola, S.2
  • 17
    • 0034677685 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and in vitro evaluation of bisubstrate inhibitors for catechol O-methyltransferase (COMT)
    • Masjost B., Ballmer P., Borroni E., Zurcher G., Winkler F.K., Jakob-Roente R., and Diederich F. Structure-based design, synthesis, and in vitro evaluation of bisubstrate inhibitors for catechol O-methyltransferase (COMT). Chem. Eur. J. 6 (2000) 971-982
    • (2000) Chem. Eur. J. , vol.6 , pp. 971-982
    • Masjost, B.1    Ballmer, P.2    Borroni, E.3    Zurcher, G.4    Winkler, F.K.5    Jakob-Roente, R.6    Diederich, F.7
  • 18
    • 0025272639 scopus 로고
    • Current approaches to macromolecular crystallization
    • McPherson A. Current approaches to macromolecular crystallization. Eur. J. Biochem. 189 (1990) 1-23
    • (1990) Eur. J. Biochem. , vol.189 , pp. 1-23
    • McPherson, A.1
  • 19
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50 (1994) 157-163
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 20
    • 0031033450 scopus 로고    scopus 로고
    • Catalytic hydroxyl/amine dyads within serine proteases
    • Paetzel M., and Dalbey R.E. Catalytic hydroxyl/amine dyads within serine proteases. Trends Biochem. Sci. 22 (1997) 28-31
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 28-31
    • Paetzel, M.1    Dalbey, R.E.2
  • 21
    • 33745268904 scopus 로고    scopus 로고
    • Comparative study of ortho- and meta-nitrated inhibitors of catechol-O-methyltransferase: interactions with the active site and regioselectivity of O-methylation
    • Palma P.N., Rodrigues M.A., Bonifacio A.I., Loureiro A.I., Learmonth D.A., Carrondo M.A., and Soares-Da-Silva P. Comparative study of ortho- and meta-nitrated inhibitors of catechol-O-methyltransferase: interactions with the active site and regioselectivity of O-methylation. Mol. Phamacol. 70 (2006) 143-153
    • (2006) Mol. Phamacol. , vol.70 , pp. 143-153
    • Palma, P.N.1    Rodrigues, M.A.2    Bonifacio, A.I.3    Loureiro, A.I.4    Learmonth, D.A.5    Carrondo, M.A.6    Soares-Da-Silva, P.7
  • 23
    • 0028956315 scopus 로고
    • Universal catalytic domain structure of AdoMet-dependent methyltransferases
    • Schluckebier G., O'Gara M., Saenger W., and Cheng X. Universal catalytic domain structure of AdoMet-dependent methyltransferases. J. Mol. Biol. 247 (1995) 16-20
    • (1995) J. Mol. Biol. , vol.247 , pp. 16-20
    • Schluckebier, G.1    O'Gara, M.2    Saenger, W.3    Cheng, X.4
  • 25
    • 0024478059 scopus 로고
    • Direct Broensted analysis of the restoration of activity to a mutant enzyme by exogenous amines
    • Toney M.D., and Kirsch J.F. Direct Broensted analysis of the restoration of activity to a mutant enzyme by exogenous amines. Science 243 (1989) 1485-1488
    • (1989) Science , vol.243 , pp. 1485-1488
    • Toney, M.D.1    Kirsch, J.F.2
  • 26
    • 0000632912 scopus 로고    scopus 로고
    • Structural aspects in the inhibitor design of catechol-O-methyltransferase
    • Pandi V. (Ed), Marcel Dekker Inc.
    • Vidgren J., and Ovaska M. Structural aspects in the inhibitor design of catechol-O-methyltransferase. In: Pandi V. (Ed). Structure-based Drug Design (1997), Marcel Dekker Inc. 343-363
    • (1997) Structure-based Drug Design , pp. 343-363
    • Vidgren, J.1    Ovaska, M.2
  • 27
    • 0028210328 scopus 로고
    • Crystal structure of catechol-O-methyltransferase
    • Vidgren J., Svenson L.A., and Lijias A. Crystal structure of catechol-O-methyltransferase. Nature 368 (1994) 354-358
    • (1994) Nature , vol.368 , pp. 354-358
    • Vidgren, J.1    Svenson, L.A.2    Lijias, A.3
  • 29
    • 0019321635 scopus 로고
    • Stereochemical course of the transmethylation catalyzed by catechol-O-methyltransferase
    • Woodard R.W., Tsai M.-D., Floss H.G., Crooks P.A., and Coward J.K. Stereochemical course of the transmethylation catalyzed by catechol-O-methyltransferase. J. Biol. Chem. 255 (1980) 9124-9127
    • (1980) J. Biol. Chem. , vol.255 , pp. 9124-9127
    • Woodard, R.W.1    Tsai, M.-D.2    Floss, H.G.3    Crooks, P.A.4    Coward, J.K.5
  • 30
    • 0030767647 scopus 로고    scopus 로고
    • A theoretical examination of the factors controlling the catalytic efficiency of a transmethylation enzyme: catechol-O-methyltransferase
    • Zheng Y.J., and Bruice T.C. A theoretical examination of the factors controlling the catalytic efficiency of a transmethylation enzyme: catechol-O-methyltransferase. J. Am. Chem. Soc. (1997) 8137-8145
    • (1997) J. Am. Chem. Soc. , pp. 8137-8145
    • Zheng, Y.J.1    Bruice, T.C.2
  • 31
    • 0020040983 scopus 로고
    • Rapid and sensitive single-step radiochemical assay for catechol-O-methyltransferase
    • Zücher G., and Da Prada M. Rapid and sensitive single-step radiochemical assay for catechol-O-methyltransferase. J. Neurochem. 38 (1982) 191-195
    • (1982) J. Neurochem. , vol.38 , pp. 191-195
    • Zücher, G.1    Da Prada, M.2


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