메뉴 건너뛰기




Volumn 6, Issue 8, 2011, Pages

Structural mechanism of S-adenosyl methionine binding to catechol O-methyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

APOENZYME; CATECHOL METHYLTRANSFERASE; DIVALENT CATION; HOLOENZYME; METHYL GROUP; S ADENOSYLMETHIONINE;

EID: 80052339060     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0024287     Document Type: Article
Times cited : (32)

References (14)
  • 1
    • 0038287034 scopus 로고    scopus 로고
    • Catechol-O-methyltransferase (COMT): biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors
    • Mannisto PT, Kaakkola S, (1999) Catechol-O-methyltransferase (COMT): biochemistry, molecular biology, pharmacology, and clinical efficacy of the new selective COMT inhibitors. Pharmacol Rev 51: 593-628.
    • (1999) Pharmacol Rev , vol.51 , pp. 593-628
    • Mannisto, P.T.1    Kaakkola, S.2
  • 2
    • 68149091979 scopus 로고    scopus 로고
    • Effects of catechol-O-methyltransferase on normal variation in the cognitive function of children
    • Barnett JH, Heron J, Goldman D, Jones PB, Xu K, (2009) Effects of catechol-O-methyltransferase on normal variation in the cognitive function of children. Am J Psychiatry 166: 909-916.
    • (2009) Am J Psychiatry , vol.166 , pp. 909-916
    • Barnett, J.H.1    Heron, J.2    Goldman, D.3    Jones, P.B.4    Xu, K.5
  • 3
    • 49249134936 scopus 로고    scopus 로고
    • Genetic approaches to addiction: genes and alcohol
    • Ducci F, Goldman D, (2008) Genetic approaches to addiction: genes and alcohol. Addiction 103: 1414-1428.
    • (2008) Addiction , vol.103 , pp. 1414-1428
    • Ducci, F.1    Goldman, D.2
  • 4
    • 19944427292 scopus 로고    scopus 로고
    • Genetic basis for individual variations in pain perception and the development of a chronic pain condition
    • Diatchenko L, Slade GD, Nackley AG, Bhalang K, Sigurdsson A, et al. (2005) Genetic basis for individual variations in pain perception and the development of a chronic pain condition. Hum Mol Genet 14: 135-143.
    • (2005) Hum Mol Genet , vol.14 , pp. 135-143
    • Diatchenko, L.1    Slade, G.D.2    Nackley, A.G.3    Bhalang, K.4    Sigurdsson, A.5
  • 5
    • 44649191697 scopus 로고    scopus 로고
    • Crystal structures of human 108V and 108M catechol O-methyltransferase
    • Rutherford K, Le Trong I, Stenkamp RE, Parson WW, (2008) Crystal structures of human 108V and 108M catechol O-methyltransferase. J Mol Biol 380: 120-130.
    • (2008) J Mol Biol , vol.380 , pp. 120-130
    • Rutherford, K.1    Le Trong, I.2    Stenkamp, R.E.3    Parson, W.W.4
  • 6
    • 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, Melen K, et al. (1995) Kinetics of human soluble and membrane-bound catechol O-methyltransferase: a revised mechanism and description of the thermolabile variant of the enzyme. Biochemistry 34: 4202-4210.
    • (1995) Biochemistry , vol.34 , pp. 4202-4210
    • Lotta, T.1    Vidgren, J.2    Tilgmann, C.3    Ulmanen, I.4    Melen, K.5
  • 7
    • 52049118327 scopus 로고    scopus 로고
    • MedusaScore: an accurate force field-based scoring function for virtual drug screening
    • Yin S, Biedermannova L, Vondrasek J, Dokholyan NV, (2008) MedusaScore: an accurate force field-based scoring function for virtual drug screening. J Chem Inf Model 48: 1656-1662.
    • (2008) J Chem Inf Model , vol.48 , pp. 1656-1662
    • Yin, S.1    Biedermannova, L.2    Vondrasek, J.3    Dokholyan, N.V.4
  • 8
    • 77957237749 scopus 로고    scopus 로고
    • Rapid flexible docking using a stochastic rotamer library of ligands
    • Ding F, Yin S, Dokholyan NV, (2010) Rapid flexible docking using a stochastic rotamer library of ligands. J Chem Inf Model 50: 1623-1632.
    • (2010) J Chem Inf Model , vol.50 , pp. 1623-1632
    • Ding, F.1    Yin, S.2    Dokholyan, N.V.3
  • 9
    • 0032443390 scopus 로고    scopus 로고
    • Discrete molecular dynamics studies of the folding of a protein-like model
    • Dokholyan NV, Buldyrev SV, Stanley HE, Shakhnovich EI, (1998) Discrete molecular dynamics studies of the folding of a protein-like model. Fold Des 3: 577-587.
    • (1998) Fold Des , vol.3 , pp. 577-587
    • Dokholyan, N.V.1    Buldyrev, S.V.2    Stanley, H.E.3    Shakhnovich, E.I.4
  • 10
    • 70449228544 scopus 로고
    • Enzymatic O-methylation of epinephrine and other catechols
    • Axelrod J, Tomchick R, (1958) Enzymatic O-methylation of epinephrine and other catechols. J Biol Chem 233: 702-705.
    • (1958) J Biol Chem , vol.233 , pp. 702-705
    • Axelrod, J.1    Tomchick, R.2
  • 11
    • 58849155679 scopus 로고    scopus 로고
    • Crystal structures of the apo and holo form of rat catechol-O-methyltransferase
    • Tsuji E, Okazaki K, Isaji M, Takeda K, (2009) Crystal structures of the apo and holo form of rat catechol-O-methyltransferase. J Struct Biol 165: 133-139.
    • (2009) J Struct Biol , vol.165 , pp. 133-139
    • Tsuji, E.1    Okazaki, K.2    Isaji, M.3    Takeda, K.4
  • 12
    • 0034701258 scopus 로고    scopus 로고
    • QM-FE and molecular dynamics calculations on catechol O-methyltransferase: free energy of activation in the enzyme and in aqueous solution and regioselectivity of the enzyme-catalyzed reaction
    • Kuhn B, Kollman PA, (2000) QM-FE and molecular dynamics calculations on catechol O-methyltransferase: free energy of activation in the enzyme and in aqueous solution and regioselectivity of the enzyme-catalyzed reaction. J Am Chem Soc 122: 2586-2596.
    • (2000) J Am Chem Soc , vol.122 , pp. 2586-2596
    • Kuhn, B.1    Kollman, P.A.2
  • 13
    • 84961983443 scopus 로고    scopus 로고
    • Theoretical modeling of enzyme catalytic power: analysis of "cratic" and electrostatic factors in catechol O-methyltransferase
    • Roca M, Marti S, Andres J, Moliner V, Tunon I, et al. (2003) Theoretical modeling of enzyme catalytic power: analysis of "cratic" and electrostatic factors in catechol O-methyltransferase. J Am Chem Soc 125: 7726-7737.
    • (2003) J Am Chem Soc , vol.125 , pp. 7726-7737
    • Roca, M.1    Marti, S.2    Andres, J.3    Moliner, V.4    Tunon, I.5
  • 14
    • 25144507259 scopus 로고    scopus 로고
    • Mechanisms for the inhibition of DNA methyltransferases by tea catechins and bioflavonoids
    • Lee WJ, Shim JY, Zhu BT, (2005) Mechanisms for the inhibition of DNA methyltransferases by tea catechins and bioflavonoids. Mol Pharmacol 68: 1018-1030.
    • (2005) Mol Pharmacol , vol.68 , pp. 1018-1030
    • Lee, W.J.1    Shim, J.Y.2    Zhu, B.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.