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Volumn 78, Issue 14, 2010, Pages 2961-2972

Substrate stereo-specificity in tryptophan dioxygenase and indoleamine 2,3-dioxygenase

Author keywords

Affinity; CO; Dioxygenase; IDO; Inhibitors; Molecular dynamics; Oxygen; Structure; TDO

Indexed keywords

CARBON MONOXIDE; INDOLEAMINE 2,3 DIOXYGENASE; OXYGEN; TRYPTOPHAN 2,3 DIOXYGENASE;

EID: 77957934484     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22819     Document Type: Article
Times cited : (37)

References (35)
  • 2
    • 27544499713 scopus 로고    scopus 로고
    • Biochemical and medical aspects of the indoleamine 2 3-dioxygenase-initiated L-tryptophan metabolism
    • Takikawa O. Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism. Biochem Biophys Res Commun 2005;338:12-19.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 12-19
    • Takikawa, O.1
  • 4
    • 33846043574 scopus 로고    scopus 로고
    • Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis
    • Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE. Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry 2007;46:145-155.
    • (2007) Biochemistry , vol.46 , pp. 145-155
    • Zhang, Y.1    Kang, S.A.2    Mukherjee, T.3    Bale, S.4    Crane, B.R.5    Begley, T.P.6    Ealick, S.E.7
  • 5
    • 33644511372 scopus 로고    scopus 로고
    • Crystal structure of human indoleamine 2 3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase
    • Sugimoto H, Oda S-i, Otsuki T, Hino T, Yoshida T, Shiro Y. Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase. Proc Natl Acad Sci USA 2006;103:2611-2616.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2611-2616
    • Sugimoto, H.1    Oda, S.-I.2    Otsuki, T.3    Hino, T.4    Yoshida, T.5    Shiro, Y.6
  • 6
    • 16244408626 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy
    • Muller AJ, DuHadaway JB, Donover PS, Sutanto-Ward E, Prendergast GC. Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Nat Med 2005;11:312-319.
    • (2005) Nat Med , vol.11 , pp. 312-319
    • Muller, A.J.1    DuHadaway, J.B.2    Donover, P.S.3    Sutanto-Ward, E.4    Prendergast, G.C.5
  • 8
    • 0038215374 scopus 로고    scopus 로고
    • Tolerance DCs and tryptophan: much ado about IDO
    • Grohmann U, Fallarino F, Puccetti P. Tolerance, DCs and tryptophan: much ado about IDO. Trends Immunol 2003;24:242-248.
    • (2003) Trends Immunol , vol.24 , pp. 242-248
    • Grohmann, U.1    Fallarino, F.2    Puccetti, P.3
  • 11
    • 37849002571 scopus 로고    scopus 로고
    • Human tryptophan dioxygenase: a comparison to indoleamine 2 3-dioxygenase
    • Batabyal D, Yeh SR. Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase. J Am Chem Soc 2007;129:15690-15701.
    • (2007) J Am Chem Soc , vol.129 , pp. 15690-15701
    • Batabyal, D.1    Yeh, S.R.2
  • 12
    • 70349084620 scopus 로고    scopus 로고
    • Inhibitory substrate binding site of human indoleamine 2 3-dioxygenase
    • Lu C, Lin Y, Yeh S-R. Inhibitory substrate binding site of human indoleamine 2,3-dioxygenase. J Am Chem Soc 2009;131:12866-12867.
    • (2009) J Am Chem Soc , vol.131 , pp. 12866-12867
    • Lu, C.1    Lin, Y.2    Yeh, S.-R.3
  • 14
    • 70350494610 scopus 로고    scopus 로고
    • Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76
    • Batabyal D, Yeh S-R. Substrate-protein interaction in human tryptophan dioxygenase: the critical role of H76. J Am Chem Soc 2009;131:3260-3270.
    • (2009) J Am Chem Soc , vol.131 , pp. 3260-3270
    • Batabyal, D.1    Yeh, S.-R.2
  • 17
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang J, Cieplak P, Kollman PA. How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J Comput Chem 2000;21:1049-1074.
    • (2000) J Comput Chem , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 21
    • 0034212858 scopus 로고    scopus 로고
    • Use of MM-PB/SA in estimating the free energies of proteins: application to native, intermediates, and unfolded villin headpiece
    • Lee MR, Duan Y, Kollman PA. Use of MM-PB/SA in estimating the free energies of proteins: application to native, intermediates, and unfolded villin headpiece. Prot: Struct Funct Bioinf 2000;39:309-316.
    • (2000) Prot: Struct Funct Bioinf , vol.39 , pp. 309-316
    • Lee, M.R.1    Duan, Y.2    Kollman, P.A.3
  • 22
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • Still WC, Tempczyk A, Hawley RC, Hendrickson T. Semianalytical treatment of solvation for molecular mechanics and dynamics. J Am Chem Soc 1990;112:6127-6129.
    • (1990) J Am Chem Soc , vol.112 , pp. 6127-6129
    • Still, W.C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 25
    • 0346885688 scopus 로고    scopus 로고
    • A DFT-Based QM-MM approach designed for the treatment of large molecular systems: application to chorismate mutase
    • Crespo A, Scherlis DA, Marti MA, Ordejon P, Roitberg AE, Estrin DA. A DFT-Based QM-MM approach designed for the treatment of large molecular systems: application to chorismate mutase. J Phys Chem B 2003;107:13728-13736.
    • (2003) J Phys Chem B , vol.107 , pp. 13728-13736
    • Crespo, A.1    Scherlis, D.A.2    Marti, M.A.3    Ordejon, P.4    Roitberg, A.E.5    Estrin, D.A.6
  • 26
    • 4243943295 scopus 로고    scopus 로고
    • Generalized gradient approximation made simple
    • Perdew JP, Burke K, Ernzerhof M. Generalized gradient approximation made simple. Phys Rev Lett 1996;77:3865.
    • (1996) Phys Rev Lett , vol.77 , pp. 3865
    • Perdew, J.P.1    Burke, K.2    Ernzerhof, M.3
  • 27
    • 34250821654 scopus 로고    scopus 로고
    • Oxygen affinity controlled by dynamical distal conformations: the soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
    • Martí MA, Capece L, Bikiel DE, Falcone B, Estrin DA. Oxygen affinity controlled by dynamical distal conformations: the soybean leghemoglobin and the Paramecium caudatum hemoglobin cases. Prot: Struct, Funct, Bioinformatics 2007;68:480-487.
    • (2007) Prot: Struct, Funct, Bioinformatics , vol.68 , pp. 480-487
    • Martí, M.A.1    Capece, L.2    Bikiel, D.E.3    Falcone, B.4    Estrin, D.A.5
  • 29
    • 34547435173 scopus 로고    scopus 로고
    • Molecular docking and spatial coarse graining simulations as tools to investigate substrate recognition, enhancer
    • Macchiarulo A, Nuti R, Bellocchi D, Camaioni E, Pellicciari R. Molecular docking and spatial coarse graining simulations as tools to investigate substrate recognition, enhancer. Biochim Biophys Acta 2007;1774:1058-1068.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1058-1068
    • Macchiarulo, A.1    Nuti, R.2    Bellocchi, D.3    Camaioni, E.4    Pellicciari, R.5
  • 30
    • 77957933059 scopus 로고    scopus 로고
    • The first step in the dioxygenation reaction carried out by tryptophan dioxygenase and indoleamine 2 3-dioxygenase as revealed by QM-MM studies
    • Capece L, Lewis-Ballester A, Batabyal D, Di Russo N, Yeh SR, Estrin DA, Marti MA. The first step in the dioxygenation reaction carried out by tryptophan dioxygenase and indoleamine 2,3-dioxygenase as revealed by QM-MM studies. J Biol Inorg Chem 2010; 15:811-823.
    • (2010) J Biol Inorg Chem , vol.15 , pp. 811-823
    • Capece, L.1    Lewis-Ballester, A.2    Batabyal, D.3    Di Russo, N.4    Yeh, S.R.5    Estrin, D.A.6    Marti, M.A.7
  • 32
    • 0023926018 scopus 로고
    • Mechanism of interferon-gamma action. Characterization of indoleamine 2,3-dioxygenase in cultured human cells induced by interferon-gamma and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity
    • Takikawa O, Kuroiwa T, Yamazaki F, Kido R. Mechanism of interferon-gamma action. Characterization of indoleamine 2,3-dioxygenase in cultured human cells induced by interferon-gamma and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity. J Biol Chem 1988;263:2041-2048.
    • (1988) J Biol Chem , vol.263 , pp. 2041-2048
    • Takikawa, O.1    Kuroiwa, T.2    Yamazaki, F.3    Kido, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.