메뉴 건너뛰기




Volumn 34, Issue 3, 2011, Pages 375-388

Computational screening of novel thiamine-catalyzed decarboxylation reactions of 2-keto acids

Author keywords

Enzyme screening; Molecular modeling; Novel biochemical transformations

Indexed keywords

CARBOXYLATION; MOLECULAR MODELING; QUANTUM THEORY; SUBSTRATES;

EID: 79955939745     PISSN: 16157591     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00449-010-0481-z     Document Type: Article
Times cited : (8)

References (77)
  • 1
    • 33745334012 scopus 로고    scopus 로고
    • The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography
    • Wille G, Meyer D, Steinmetz A, Hinze E, Golbik R, Tittmann K (2006) The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nat Chem Biol 2:390-490
    • (2006) Nat Chem Biol , vol.2 , pp. 390-490
    • Wille, G.1    Meyer, D.2    Steinmetz, A.3    Hinze, E.4    Golbik, R.5    Tittmann, K.6
  • 2
    • 64149099325 scopus 로고    scopus 로고
    • Reaction mechanisms of thiamin diphosphate enzymes: Defining states of ionization and tautomerization of the cofactor at individual steps
    • Nemeria NS, Chakraborty S, Balakrishnan A, Jordan F (2009) Reaction mechanisms of thiamin diphosphate enzymes: defining states of ionization and tautomerization of the cofactor at individual steps. FEBS J 276:2432-2446
    • (2009) FEBS J , vol.276 , pp. 2432-2446
    • Nemeria, N.S.1    Chakraborty, S.2    Balakrishnan, A.3    Jordan, F.4
  • 4
    • 33947672445 scopus 로고    scopus 로고
    • Extending Iterative Protein Redesign and Optimization (IPRO) in protein library design for ligand specificity
    • DOI 10.1529/biophysj.106.096016
    • Fazelinia H, Cirino PC, Maranas CD (2007) Extending iterative protein redesign and optimization (IPRO) in protein library design for ligand specificity. Biophys J 92:2120-2130 (Pubitemid 46495273)
    • (2007) Biophysical Journal , vol.92 , Issue.6 , pp. 2120-2130
    • Fazelinia, H.1    Cirino, P.C.2    Maranas, C.D.3
  • 5
    • 51849142353 scopus 로고    scopus 로고
    • Genome-scale model for Clostridium acetobutylicum: Part I. Metabolic network resolution and analysis
    • Senger RS, Papoutsakis ET (2008) Genome-scale model for Clostridium acetobutylicum: part I. Metabolic network resolution and analysis. Biotechnol Bioeng 101:1036-1052
    • (2008) Biotechnol Bioeng , vol.101 , pp. 1036-1052
    • Senger, R.S.1    Papoutsakis, E.T.2
  • 6
    • 51849157931 scopus 로고    scopus 로고
    • Genome-scale model for Clostridium acetobutylicum: Part II. Development of specific proton flux states and numerically determined sub-systems
    • Senger RS, Papoutsakis ET (2008) Genome-scale model for Clostridium acetobutylicum: part II. Development of specific proton flux states and numerically determined sub-systems. Biotechnol Bioeng 101:1053-1071
    • (2008) Biotechnol Bioeng , vol.101 , pp. 1053-1071
    • Senger, R.S.1    Papoutsakis, E.T.2
  • 7
    • 51849115840 scopus 로고    scopus 로고
    • Genome-scale reconstruction and in silico analysis of the Clostridium acetobutylicum ATCC 824 metabolic network
    • Lee J, Yun H, Feist AM, Palsson BO, Lee SY (2008) Genome-scale reconstruction and in silico analysis of the Clostridium acetobutylicum ATCC 824 metabolic network. Appl Microbiol Biotechnol 80:849-862
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 849-862
    • Lee, J.1    Yun, H.2    Feist, A.M.3    Palsson, B.O.4    Lee, S.Y.5
  • 9
    • 34547809313 scopus 로고    scopus 로고
    • A model-based optimization framework for the inference of regulatory interactions using time-course DNA microarray expression data
    • Thomas R, Paredes CJ, Mehrotra S, Hatzimanikatis V, Papoutsakis ET (2007) A model-based optimization framework for the inference of regulatory interactions using time-course DNA microarray expression data. BMC Bioinformatics 8:228-236
    • (2007) BMC Bioinformatics , vol.8 , pp. 228-236
    • Thomas, R.1    Paredes, C.J.2    Mehrotra, S.3    Hatzimanikatis, V.4    Papoutsakis, E.T.5
  • 10
    • 58149476770 scopus 로고    scopus 로고
    • OptGraft: A computational procedure for transferring a binding site onto an existing protein scaffold
    • Fazelinia H, Cirino PC, Maranas CD (2009) OptGraft: a computational procedure for transferring a binding site onto an existing protein scaffold. Protein Sci 18:180-195
    • (2009) Protein Sci , vol.18 , pp. 180-195
    • Fazelinia, H.1    Cirino, P.C.2    Maranas, C.D.3
  • 11
    • 34347258175 scopus 로고    scopus 로고
    • Quantitative prediction of cellular metabolism with constraint-based models: The COBRA Toolbox
    • DOI 10.1038/nprot.2007.99, PII NPROT.2007.99
    • Becker SA, Feist AM, Mo ML, Hannum G, Palsson BO, Herrgard MJ (2007) Quantitative prediction of cellular metabolism with constraint-based models: the COBRA Toolbox. Nat Protoc 2:727-738 (Pubitemid 47040034)
    • (2007) Nature Protocols , vol.2 , Issue.3 , pp. 727-738
    • Becker, S.A.1    Feist, A.M.2    Mo, M.L.3    Hannum, G.4    Palsson, B.O.5    Herrgard, M.J.6
  • 17
    • 0028727474 scopus 로고
    • Computer generated reaction networks: On-the-fly calculation of species properties using computational quantum chemistry
    • Broadbelt LJ, Stark SM, Klein MT (1994) Computer generated reaction networks: on-the-fly calculation of species properties using computational quantum chemistry. Chem Eng Sci 49:4991-5010
    • (1994) Chem Eng Sci , vol.49 , pp. 4991-5010
    • Broadbelt, L.J.1    Stark, S.M.2    Klein, M.T.3
  • 18
    • 0028410110 scopus 로고
    • Computer-generated pyrolysis modeling - On-the-fly generation of species, reactions, and rates
    • Broadbelt LJ, Stark SM, Klein MT (1994) Computer-generated pyrolysis modeling - on-the-fly generation of species, reactions, and rates. Ind Eng Chem Res 33:790-799
    • (1994) Ind Eng Chem Res , vol.33 , pp. 790-799
    • Broadbelt, L.J.1    Stark, S.M.2    Klein, M.T.3
  • 19
    • 0000670212 scopus 로고
    • Termination of computer-generated reaction-mechanisms - Species rank-based convergence criterion
    • Broadbelt LJ, Stark SM, Klein MT (1995) Termination of computer-generated reaction-mechanisms - species rank-based convergence criterion. Ind Eng Chem Res 34:2566-2573
    • (1995) Ind Eng Chem Res , vol.34 , pp. 2566-2573
    • Broadbelt, L.J.1    Stark, S.M.2    Klein, M.T.3
  • 20
    • 22144436255 scopus 로고    scopus 로고
    • Theoretical considerations and computational analysis of the complexity in polyketide synthesis pathways
    • DOI 10.1021/ja051586y
    • Gonzalez-Lergier J, Broadbelt LJ, Hatzimanikatis V (2005) Theoretical considerations and computational analysis of the complexity in polyketide synthesis pathways. J Am Chem Soc 127:9930-9938 (Pubitemid 40981557)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.27 , pp. 9930-9938
    • Gonzalez-Lergier, J.1    Broadbelt, L.J.2    Hatzimanikatis, V.3
  • 21
    • 77953578214 scopus 로고    scopus 로고
    • Discovery and analysis of novel metabolic pathways for the biosynthesis of industrial chemicals: 3-hydroxypropanoate
    • Henry CS, Broadbelt LJ, Hatzimanikatis V (2010) Discovery and analysis of novel metabolic pathways for the biosynthesis of industrial chemicals: 3-hydroxypropanoate. Biotechnol Bioeng 106:462-473
    • (2010) Biotechnol Bioeng , vol.106 , pp. 462-473
    • Henry, C.S.1    Broadbelt, L.J.2    Hatzimanikatis, V.3
  • 22
    • 2642513030 scopus 로고    scopus 로고
    • Monte Carlo sampling can be used to determine the size and shape of the steady-state flux space
    • DOI 10.1016/j.jtbi.2004.02.006, PII S0022519304000554
    • Wiback SJ, Famili I, Greenberg HJ, Palsson BØ (2004) Monte Carlo sampling can be used to determine the size and shape of the steady-state flux space. J Theor Biol 228:437-447 (Pubitemid 38726066)
    • (2004) Journal of Theoretical Biology , vol.228 , Issue.4 , pp. 437-447
    • Wiback, S.J.1    Famili, I.2    Greenberg, H.J.3    Palsson, B.O.4
  • 24
    • 33847797256 scopus 로고    scopus 로고
    • Thermodynamics-based metabolic flux analysis
    • DOI 10.1529/biophysj.106.093138
    • Henry CS, Broadbelt LJ, Hatzimanikatis V (2007) Thermodynamics-based metabolic flux analysis. Biophys J 92:1792-1805 (Pubitemid 46393490)
    • (2007) Biophysical Journal , vol.92 , Issue.5 , pp. 1792-1805
    • Henry, C.S.1    Broadbelt, L.J.2    Hatzimanikatis, V.3
  • 25
    • 51049107514 scopus 로고    scopus 로고
    • Group contribution method for thermodynamic analysis of complex metabolic networks
    • Jankowski MD, Henry CS, Broadbelt LJ, Hatzimanikatis V (2008) Group contribution method for thermodynamic analysis of complex metabolic networks. Biophys J 95:1487-1499
    • (2008) Biophys J , vol.95 , pp. 1487-1499
    • Jankowski, M.D.1    Henry, C.S.2    Broadbelt, L.J.3    Hatzimanikatis, V.4
  • 26
    • 1542269174 scopus 로고    scopus 로고
    • Acetone butanol ethanol (ABE) production from concentrated substrate: Reduction in substrate inhibition by fed-batch technique and product inhibition by gas stripping
    • DOI 10.1007/s00253-003-1400-x
    • Ezeji TC, Qureshi N, Blaschek HP (2004) Acetone butanol ethanol (ABE) production from concentrated substrate: reduction in substrate inhibition by fed-batch technique and product inhibition by gas stripping. Appl Microbiol Biotechnol 63:653-658 (Pubitemid 38316691)
    • (2004) Applied Microbiology and Biotechnology , vol.63 , Issue.6 , pp. 653-658
    • Ezeji, T.C.1    Qureshi, N.2    Blaschek, H.P.3
  • 27
    • 34249981232 scopus 로고    scopus 로고
    • Bioproduction of butanol from biomass: From genes to bioreactors
    • DOI 10.1016/j.copbio.2007.04.002, PII S0958166907000511, Energy biotechnology / Environmental biotechnology
    • Ezeji TC, Qureshi N, Blaschek HP (2007) Bioproduction of butanol from biomass: from genes to bioreactors. Curr Opin Biotechnol 18:220-227 (Pubitemid 46887658)
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.3 , pp. 220-227
    • Ezeji, T.C.1    Qureshi, N.2    Blaschek, H.P.3
  • 28
    • 2242456844 scopus 로고    scopus 로고
    • Glucose Uptake in Clostridium beijerinckii NCIMB 8052 and the Solvent-Hyperproducing Mutant BA101
    • Lee J, Blaschek HP (2001) Glucose uptake in Clostridium beijerinckii NCIMB 8052 and the solvent-hyperproducing mutant BA101. Appl Environ Microbiol 67:5025-5031 (Pubitemid 33701265)
    • (2001) Applied and Environmental Microbiology , vol.67 , Issue.3-12 , pp. 5025-5031
    • Lee, J.1    Blaschek, H.P.2
  • 29
    • 0034879273 scopus 로고    scopus 로고
    • Review of the enzymes and metabolic pathways (EMP) database
    • DOI 10.1006/mben.2001.0189
    • Burgard AP, Maranas CD (2001) Review of the Enzymes and Metabolic Pathways (EMP) Database. Metab Eng 3:193-194 (Pubitemid 32748162)
    • (2001) Metabolic Engineering , vol.3 , Issue.3 , pp. 193-194
    • Burgard, A.P.1    Maranas, C.D.2
  • 30
    • 64149111838 scopus 로고    scopus 로고
    • Reaction mechanisms of thiamin diphosphate enzymes: Redox reactions
    • Tittmann K (2009) Reaction mechanisms of thiamin diphosphate enzymes: redox reactions. FEBS J 276:2454-2468
    • (2009) FEBS J , vol.276 , pp. 2454-2468
    • Tittmann, K.1
  • 32
    • 0010505580 scopus 로고    scopus 로고
    • Theoretical studies on the decarboxylation reaction in thiamin catalysis
    • Friedemann R, Breitkopf C (1996) Theoretical studies on the decarboxylation reaction in thiamin catalysis. Int J Quantum Chem 57:943-948 (Pubitemid 126534833)
    • (1996) International Journal of Quantum Chemistry , vol.57 , Issue.5 , pp. 943-948
    • Friedemann, R.1    Breitkopf, C.2
  • 33
    • 0037493009 scopus 로고    scopus 로고
    • Ab initio and DFT calculations on the initial step in thiamin catalysis
    • Friedemann R, Naumann S (2003) Ab initio and DFT calculations on the initial step in thiamin catalysis. J Mol Struct Theochem 630:275-281
    • (2003) J Mol Struct Theochem , vol.630 , pp. 275-281
    • Friedemann, R.1    Naumann, S.2
  • 35
    • 56849087272 scopus 로고    scopus 로고
    • Catalyzing separation of carbon dioxide in thiamin diphosphate-promoted decarboxylation
    • Kluger R, Rathgeber S (2008) Catalyzing separation of carbon dioxide in thiamin diphosphate-promoted decarboxylation. FEBS J 275:6089-6100
    • (2008) FEBS J , vol.275 , pp. 6089-6100
    • Kluger, R.1    Rathgeber, S.2
  • 36
    • 77952411134 scopus 로고    scopus 로고
    • Studying enzyme-substrate specificity in silico: A case study of the Escherichia coli glycolysis pathway
    • Kalyanaraman C, Jacobson MP (2010) Studying enzyme-substrate specificity in silico: a case study of the Escherichia coli glycolysis pathway. Biochemistry 49:4003-4005
    • (2010) Biochemistry , vol.49 , pp. 4003-4005
    • Kalyanaraman, C.1    Jacobson, M.P.2
  • 39
    • 3543002852 scopus 로고    scopus 로고
    • Ligand selectivity and competition between enzymes in silico
    • DOI 10.1038/nbt999
    • Macchiarulo A, Nobeli I, Thornton JM (2004) Ligand selectivity and competition between enzymes in silico. Nat Biotechnol 22:1039-1045 (Pubitemid 39014486)
    • (2004) Nature Biotechnology , vol.22 , Issue.8 , pp. 1039-1045
    • Macchiarulo, A.1    Nobeli, I.2    Thornton, J.M.3
  • 47
    • 79955934260 scopus 로고    scopus 로고
    • QSite (2001) Schrodinger Inc, Portland
    • QSite (2001) Schrodinger Inc, Portland
  • 48
    • 79955929670 scopus 로고    scopus 로고
    • Jaguar 5.5
    • Bachrach SM (2004) Jaguar 5.5. J Am Chem Soc 126:5018-5028
    • (2004) J Am Chem Soc , vol.126 , pp. 5018-5028
    • Bachrach, S.M.1
  • 49
    • 79955937260 scopus 로고    scopus 로고
    • IMPACT Schrodinger Inc Portland, OR
    • IMPACT Schrodinger Inc Portland, OR
  • 52
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • DOI 10.1021/ja9621760, PII S0002786396021762
    • Jorgensen WL, Maxwell DS, Tirado-Rives J (1996) Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 118:11225-11236 (Pubitemid 26399746)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 53
    • 0000189651 scopus 로고
    • Density-functional thermochemistry 3. The role of exact exchange
    • Becke AD (1993) Density-functional thermochemistry 3. The role of exact exchange. J Chem Phys 98:5648-5652
    • (1993) J Chem Phys , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 54
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic-behavior
    • Becke AD (1988) Density-functional exchange-energy approximation with correct asymptotic-behavior. Phys Rev A 38: 3098-3100
    • (1988) Phys Rev A , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 55
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron-density
    • Lee CT, Yang WT, Parr RG (1988) Development of the Colle-Salvetti correlation-energy formula into a functional of the electron-density. Phys Rev B 37:785-789
    • (1988) Phys Rev B , vol.37 , pp. 785-789
    • Lee, C.T.1    Yang, W.T.2    Parr, R.G.3
  • 57
    • 84962361532 scopus 로고    scopus 로고
    • Benchmarking the conductor-like polarizable
    • continuum model (CPCM) for aqueous solvation free energies of neutral and ionic organic molecules.
    • Takano Y, Houk KN (2005) Benchmarking the conductor-like polarizable continuum model (CPCM) for aqueous solvation free energies of neutral and ionic organic molecules. J Chem Theory Comput 1:70-77
    • (2005) J Chem Theory Comput , vol.1 , pp. 70-77
    • Takano, Y.1    Houk, K.N.2
  • 58
    • 84962349001 scopus 로고    scopus 로고
    • Energies, structures, and electronic properties of molecules in solution with the C-PCM solvation model
    • Cossi M, Rega N, Scalmani G, Barone V (2003) Energies, structures, and electronic properties of molecules in solution with the C-PCM solvation model. J Comput Chem 24:669-681
    • (2003) J Comput Chem , vol.24 , pp. 669-681
    • Cossi, M.1    Rega, N.2    Scalmani, G.3    Barone, V.4
  • 59
    • 84961985847 scopus 로고    scopus 로고
    • Quantum calculation of molecular energies and energy gradients in solution by a conductor solvent model
    • Barone V, Cossi M (1998) Quantum calculation of molecular energies and energy gradients in solution by a conductor solvent model. J Phys Chem A 102:1995-2001 (Pubitemid 128591338)
    • (1998) Journal of Physical Chemistry A , vol.102 , Issue.11 , pp. 1995-2001
    • Barone, V.1    Cossi, M.2
  • 60
    • 0037898938 scopus 로고    scopus 로고
    • Pyruvate ferredoxin oxidoreductase and its radical intermediate
    • Ragsdale SW (2003) Pyruvate ferredoxin oxidoreductase and its radical intermediate. Chem Rev 103:2333-2346
    • (2003) Chem Rev , vol.103 , pp. 2333-2346
    • Ragsdale, S.W.1
  • 61
    • 26844525476 scopus 로고    scopus 로고
    • Theoretical study toward understanding the catalytic mechanism of pyruvate decarboxylase
    • DOI 10.1021/jp052802s
    • Wang JY, Dong H, Li SH, He HW (2005) Theoretical study toward understanding the catalytic mechanism of pyruvate decarboxylase. J Phys Chem B 109:18664-18672 (Pubitemid 41464201)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.39 , pp. 18664-18672
    • Wang, J.1    Dong, H.2    Li, S.3    He, H.4
  • 62
    • 67649476220 scopus 로고    scopus 로고
    • Recent developments of the quantum chemical cluster approach for modeling enzyme reactions
    • Siegbahn P, Himo F (2009) Recent developments of the quantum chemical cluster approach for modeling enzyme reactions. J Biol Inorg Chem 14:643-651
    • (2009) J Biol Inorg Chem , vol.14 , pp. 643-651
    • Siegbahn, P.1    Himo, F.2
  • 63
    • 67650549945 scopus 로고    scopus 로고
    • S K-edge XAS and DFT calculations on cytochrome P450: Covalent and ionic contributions to the cysteine-Fe bond and their contribution to reactivity
    • Dey A, Jiang Y, Ortiz de Montellano P, Hodgson KO, Hedman B, Solomon EI (2009) S K-edge XAS and DFT calculations on cytochrome P450: covalent and ionic contributions to the cysteine-Fe bond and their contribution to reactivity. J Am Chem Soc 131:7869-7878
    • (2009) J Am Chem Soc , vol.131 , pp. 7869-7878
    • Dey, A.1    Jiang, Y.2    Ortiz De Montellano, P.3    Hodgson, K.O.4    Hedman, B.5    Solomon, E.I.6
  • 64
    • 84962476358 scopus 로고    scopus 로고
    • Solvent effects on electronic structure of active site of azurin by polarizable continuum model
    • Sugimori K, Shuku T, Sugiyama A, Nagao H, Sakurai T, Nishikawa K (2005) Solvent effects on electronic structure of active site of azurin by polarizable continuum model. Polyhedron 24:2671-2675
    • (2005) Polyhedron , vol.24 , pp. 2671-2675
    • Sugimori, K.1    Shuku, T.2    Sugiyama, A.3    Nagao, H.4    Sakurai, T.5    Nishikawa, K.6
  • 65
    • 0035930716 scopus 로고    scopus 로고
    • Crystal structure of the free radical intermediate of pyruvate:ferredoxin oxidoreductase
    • DOI 10.1126/science.1066198
    • Chabriere E, Vernede C, Guigliarelli B, Charon MH, Hatchikian EC, Fontecilla-Camps JC (2001) Crystal structure of the free radical intermediate of pyruvate: ferredoxin oxidoreductase. Science 294:2559-2563 (Pubitemid 34027298)
    • (2001) Science , vol.294 , Issue.5551 , pp. 2559-2563
    • Chabriere, E.1    Vernede, X.2    Guigliarelli, B.3    Charon, M.-H.4    Hatchikian, E.C.5    Fontecilla-Camps, J.C.6
  • 67
    • 0034609527 scopus 로고    scopus 로고
    • Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarum
    • Tittmann K, Golbik R, Ghisla S, Hubner G (2000) Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarum. Biochemistry 39:10747-10754
    • (2000) Biochemistry , vol.39 , pp. 10747-10754
    • Tittmann, K.1    Golbik, R.2    Ghisla, S.3    Hubner, G.4
  • 68
    • 47349102781 scopus 로고    scopus 로고
    • Thiamin diphosphate catalysis: Enzymic and nonenzymic covalent intermediates
    • Kluger R, Tittmann K (2008) Thiamin diphosphate catalysis: enzymic and nonenzymic covalent intermediates. Chem Rev 108:1797-1833
    • (2008) Chem Rev , vol.108 , pp. 1797-1833
    • Kluger, R.1    Tittmann, K.2
  • 69
    • 0034666137 scopus 로고    scopus 로고
    • The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway
    • Furdui C, Ragsdale SW (2000) The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway. J Biol Chem 275:28494-28499
    • (2000) J Biol Chem , vol.275 , pp. 28494-28499
    • Furdui, C.1    Ragsdale, S.W.2
  • 71
    • 0142135980 scopus 로고    scopus 로고
    • Dual Catalytic Apparatus of the Thiamin Diphosphate Coenzyme: Acid-Base via the 1′,4′-Iminopyrimidine Tautomer along with Its Electrophilic Role
    • DOI 10.1021/ja0346126
    • Jordan F, Nemeria NS, Zhang S, Yan Y, Arjunan P, Furey W (2003) Dual catalytic apparatus of the thiamin diphosphate coenzyme: acid-base via the 1′, 4′-iminopyrimidine tautomer along with its electrophilic role. J Am Chem Soc 125:12732-12738 (Pubitemid 37280442)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.42 , pp. 12732-12738
    • Jordan, F.1    Nemeria, N.S.2    Zhang, S.3    Yan, Y.4    Arjunan, P.5    Furey, W.6
  • 72
    • 0032537475 scopus 로고    scopus 로고
    • Theoretical studies on the electronic and energetic properties of the aminopyrimidine part of thiamin diphosphate
    • DOI 10.1016/S0167-4838(98)00072-7, PII S0167483898000727
    • Friedemann R, Neef H (1998) Theoretical studies on the electronic and energetic properties of the aminopyrimidine part of thiamin diphosphate. Biochim Biophys Acta Protein Struct Mol Enzymol 1385:245-250 (Pubitemid 28310792)
    • (1998) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1385 , Issue.2 , pp. 245-250
    • Friedemann, R.1    Neef, H.2
  • 73
    • 0027366618 scopus 로고
    • Decomposition of 2-(1-hydroxybenzyl)thiamin in neutral aqueous solutions: Benzaldehyde and thiamin are not the products
    • DOI 10.1006/bioo.1993.1023
    • Kluger R, Lam JF, Kim CS (1993) Decomposition of 2- (1-hydroxybenzyl) thiamin in neutral aqueous-solutions - benzaldehyde and thiamin are not the products. Bioorg Chem 21:275-283 (Pubitemid 23285425)
    • (1993) Bioorganic Chemistry , vol.21 , Issue.3 , pp. 275-283
    • Kluger, R.1    Lam, J.F.2    Kim, C.-S.3
  • 74
    • 0023719226 scopus 로고
    • Thiamin diphosphate catalysis - Mechanistic divergence as a probe of substrate activation of pyruvate decarboxylase
    • Gish G, Smyth T, Kluger R (1988) Thiamin diphosphate catalysis - mechanistic divergence as a probe of substrate activation of pyruvate decarboxylase. J Am Chem Soc 110:6230-6234
    • (1988) J Am Chem Soc , vol.110 , pp. 6230-6234
    • Gish, G.1    Smyth, T.2    Kluger, R.3
  • 75
    • 38049001166 scopus 로고    scopus 로고
    • Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels
    • Atsumi S, Hanai T, Liao JC (2008) Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels. Nature 451(7174):86-89
    • (2008) Nature , vol.451 , Issue.7174 , pp. 86-89
    • Atsumi, S.1    Hanai, T.2    Liao, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.