메뉴 건너뛰기




Volumn 21, Issue , 2014, Pages 25-33

Catalytic control in terpenoid cyclases: Multiscale modeling of thermodynamic, kinetic, and dynamic effects

Author keywords

[No Author keywords available]

Indexed keywords

ARISTOLOCHENE; CARBENE; PROTON; PYROPHOSPHATE; SQUALENE; TERPENE; TERPENE SYNTHASE; TRANSFERASE;

EID: 84908314966     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2014.03.010     Document Type: Review
Times cited : (59)

References (67)
  • 2
    • 33947476119 scopus 로고
    • Application of the theory of diffusion-controlled reactions to enzyme kinetics
    • Alberty R.A., Hammes G.G. Application of the theory of diffusion-controlled reactions to enzyme kinetics. J Phys Chem 1958, 62:154-159.
    • (1958) J Phys Chem , vol.62 , pp. 154-159
    • Alberty, R.A.1    Hammes, G.G.2
  • 3
    • 79959431109 scopus 로고    scopus 로고
    • Benchmark reaction rates, the stability of biological molecules in water, and the evolution of catalytic power in enzymes
    • Wolfenden R. Benchmark reaction rates, the stability of biological molecules in water, and the evolution of catalytic power in enzymes. Annu Rev Biochem 2011, 80:645-667.
    • (2011) Annu Rev Biochem , vol.80 , pp. 645-667
    • Wolfenden, R.1
  • 5
    • 84912208190 scopus 로고
    • Chemical achievement and hope for the future
    • Pauling L. Chemical achievement and hope for the future. Am Sci 1948, 36:50-58.
    • (1948) Am Sci , vol.36 , pp. 50-58
    • Pauling, L.1
  • 6
    • 0000561390 scopus 로고
    • Role of solvent reorganization energies in the catalytic activity of enzymes
    • Yadav A., Jackson R.M., Holbrook J.J., Warshel A. Role of solvent reorganization energies in the catalytic activity of enzymes. J Am Chem Soc 1991, 113:4800.
    • (1991) J Am Chem Soc , vol.113 , pp. 4800
    • Yadav, A.1    Jackson, R.M.2    Holbrook, J.J.3    Warshel, A.4
  • 7
    • 33748584863 scopus 로고    scopus 로고
    • Mechanisms and free energies of enzymatic reactions
    • Gao J., Ma S., Major D.T., Nam K., Pu J., Truhlar D.G. Mechanisms and free energies of enzymatic reactions. Chem Rev 2006, 106:3188-3209.
    • (2006) Chem Rev , vol.106 , pp. 3188-3209
    • Gao, J.1    Ma, S.2    Major, D.T.3    Nam, K.4    Pu, J.5    Truhlar, D.G.6
  • 8
    • 20444457978 scopus 로고    scopus 로고
    • Why enzymes are proficient catalysts: beyond the Pauling paradigm
    • Zhang X., Houk K.N. Why enzymes are proficient catalysts: beyond the Pauling paradigm. Acc Chem Res 2005, 38:379-385.
    • (2005) Acc Chem Res , vol.38 , pp. 379-385
    • Zhang, X.1    Houk, K.N.2
  • 9
    • 73949083862 scopus 로고    scopus 로고
    • Differential quantum mechanical tunneling in the uncatalyzed and in the Nitroalkane Oxidase proton abstraction of nitroethane
    • Major D.T., Heroux A., Orville A.M., Valley M.P., Fitzpatrick P.F., Gao J. Differential quantum mechanical tunneling in the uncatalyzed and in the Nitroalkane Oxidase proton abstraction of nitroethane. Proc Natl Acad Sci U S A 2009, 106:20734-20739.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20734-20739
    • Major, D.T.1    Heroux, A.2    Orville, A.M.3    Valley, M.P.4    Fitzpatrick, P.F.5    Gao, J.6
  • 10
    • 77955164557 scopus 로고    scopus 로고
    • Enzymatic tunneling and kinetic isotope effects: chemistry at the crossroads
    • Sen A., Kohen A. Enzymatic tunneling and kinetic isotope effects: chemistry at the crossroads. J Phys Org Chem 2010, 23:613-619.
    • (2010) J Phys Org Chem , vol.23 , pp. 613-619
    • Sen, A.1    Kohen, A.2
  • 11
    • 84857515422 scopus 로고    scopus 로고
    • Good vibrations in enzyme-catalysed reactions
    • Hay S., Scrutton N.S. Good vibrations in enzyme-catalysed reactions. Nat Chem 2012, 4:161-168.
    • (2012) Nat Chem , vol.4 , pp. 161-168
    • Hay, S.1    Scrutton, N.S.2
  • 12
    • 11144311139 scopus 로고    scopus 로고
    • Lessons from natural molecules
    • Clardy J., Walsh C. Lessons from natural molecules. Nature 2004, 432:829-837.
    • (2004) Nature , vol.432 , pp. 829-837
    • Clardy, J.1    Walsh, C.2
  • 13
    • 34250785114 scopus 로고    scopus 로고
    • The function of terpene natural products in the natural world
    • Gershenzon J., Dudareva N. The function of terpene natural products in the natural world. Nat Chem Biol 2007, 3:408-414.
    • (2007) Nat Chem Biol , vol.3 , pp. 408-414
    • Gershenzon, J.1    Dudareva, N.2
  • 14
    • 33845282240 scopus 로고
    • Biosynthesis and catabolism of monoterpenoids
    • Croteau R. Biosynthesis and catabolism of monoterpenoids. Chem Rev 1987, 87:929-954.
    • (1987) Chem Rev , vol.87 , pp. 929-954
    • Croteau, R.1
  • 15
    • 0000558630 scopus 로고
    • Enzymatic formation of sesquiterpenes
    • Cane D.E. Enzymatic formation of sesquiterpenes. Chem Rev 1990, 90:1089-1103.
    • (1990) Chem Rev , vol.90 , pp. 1089-1103
    • Cane, D.E.1
  • 16
    • 33748601470 scopus 로고    scopus 로고
    • Structural biology and chemistry of the terpenoid cyclases
    • Christianson D.W. Structural biology and chemistry of the terpenoid cyclases. Chem Rev 2006, 106:3412-3442.
    • (2006) Chem Rev , vol.106 , pp. 3412-3442
    • Christianson, D.W.1
  • 17
    • 34147124870 scopus 로고    scopus 로고
    • Roots of biosynthetic diversity
    • Christianson D.W. Roots of biosynthetic diversity. Science 2007, 316:60-61.
    • (2007) Science , vol.316 , pp. 60-61
    • Christianson, D.W.1
  • 18
    • 52449121215 scopus 로고    scopus 로고
    • Chemical wizardry? The generation of diversity in terpenoid biosynthesis
    • Allemann R.K. Chemical wizardry? The generation of diversity in terpenoid biosynthesis. Pure Appl Chem 2008, 80:1791-1798.
    • (2008) Pure Appl Chem , vol.80 , pp. 1791-1798
    • Allemann, R.K.1
  • 19
    • 43049107992 scopus 로고    scopus 로고
    • Unearthing the roots of the terpenome
    • Christianson D.W. Unearthing the roots of the terpenome. Curr Opin Chem Biol 2008, 12:141-150.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 141-150
    • Christianson, D.W.1
  • 20
    • 70350731753 scopus 로고    scopus 로고
    • Monoterpene and sesquiterpene synthases and the origin of terpene skeletal diversity in plants
    • Degenhardt J., Kollner T.G., Gershenzon J. Monoterpene and sesquiterpene synthases and the origin of terpene skeletal diversity in plants. Phytochemistry 2009, 70:1621-1637.
    • (2009) Phytochemistry , vol.70 , pp. 1621-1637
    • Degenhardt, J.1    Kollner, T.G.2    Gershenzon, J.3
  • 21
    • 0030751628 scopus 로고    scopus 로고
    • Pre-steady-state kinetic analysis of the trichodiene synthase reaction pathway
    • Cane D.E., Chiu H.T., Liang P.H., Anderson K.S. Pre-steady-state kinetic analysis of the trichodiene synthase reaction pathway. Biochemistry 1997, 36:8332-8339.
    • (1997) Biochemistry , vol.36 , pp. 8332-8339
    • Cane, D.E.1    Chiu, H.T.2    Liang, P.H.3    Anderson, K.S.4
  • 22
    • 34250688380 scopus 로고    scopus 로고
    • Following evolution's lead to a single residue switch for diterpene synthase product outcome
    • Xu M., Wilderman P.R., Peters R.J. Following evolution's lead to a single residue switch for diterpene synthase product outcome. Proc Natl Acad Sci U S A 2007, 104:7397-7401.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7397-7401
    • Xu, M.1    Wilderman, P.R.2    Peters, R.J.3
  • 23
    • 84858676944 scopus 로고    scopus 로고
    • Exploration and mining of the bacterial terpenome
    • Cane D.E., Ikeda H. Exploration and mining of the bacterial terpenome. Acc Chem Res 2012, 45:463-472.
    • (2012) Acc Chem Res , vol.45 , pp. 463-472
    • Cane, D.E.1    Ikeda, H.2
  • 24
    • 0030846307 scopus 로고    scopus 로고
    • Creating isoprenoid diversity
    • Sacchettini J.C., Poulter C.D. Creating isoprenoid diversity. Science 1997, 277:1788-1789.
    • (1997) Science , vol.277 , pp. 1788-1789
    • Sacchettini, J.C.1    Poulter, C.D.2
  • 26
    • 84863936069 scopus 로고    scopus 로고
    • The sweet smell of microbes
    • Bomgardner M.M. The sweet smell of microbes. Chem Eng News 2012, 90:25-29.
    • (2012) Chem Eng News , vol.90 , pp. 25-29
    • Bomgardner, M.M.1
  • 28
    • 0038391517 scopus 로고    scopus 로고
    • Engineering a mevalonate pathway in Escherichia coli for production of terpenoids
    • Martin V.J., Pitera D.J., Withers S.T., Newman J.D., Keasling J.D. Engineering a mevalonate pathway in Escherichia coli for production of terpenoids. Nat Biotechnol 2003, 21:796-802.
    • (2003) Nat Biotechnol , vol.21 , pp. 796-802
    • Martin, V.J.1    Pitera, D.J.2    Withers, S.T.3    Newman, J.D.4    Keasling, J.D.5
  • 30
    • 34548757971 scopus 로고    scopus 로고
    • An oxidosqualene cyclase makes numerous products by diverse mechanisms: a challenge to prevailing concepts of triterpene biosynthesis
    • Lodeiro S., Xiong Q., Wilson W.K., Kolesnikova M.D., Onak C.S., Matsuda S.P.T. An oxidosqualene cyclase makes numerous products by diverse mechanisms: a challenge to prevailing concepts of triterpene biosynthesis. J Am Chem Soc 2007, 129:11213-11222.
    • (2007) J Am Chem Soc , vol.129 , pp. 11213-11222
    • Lodeiro, S.1    Xiong, Q.2    Wilson, W.K.3    Kolesnikova, M.D.4    Onak, C.S.5    Matsuda, S.P.T.6
  • 31
    • 84877698856 scopus 로고    scopus 로고
    • High-throughput screening for terpene-synthase-cyclization activity and directed evolution of a terpene synthase
    • Lauchli R., Rabe K.S., Kalbarczyk K.Z., Tata A., Heel T., Kitto R.Z., Arnold F.H. High-throughput screening for terpene-synthase-cyclization activity and directed evolution of a terpene synthase. Angew Chem Int Ed 2013, 52:5571-5574.
    • (2013) Angew Chem Int Ed , vol.52 , pp. 5571-5574
    • Lauchli, R.1    Rabe, K.S.2    Kalbarczyk, K.Z.3    Tata, A.4    Heel, T.5    Kitto, R.Z.6    Arnold, F.H.7
  • 32
    • 84873342812 scopus 로고    scopus 로고
    • Rapid chemical characterization of bacterial terpene synthases
    • Rabe P., Dickschat J.S. Rapid chemical characterization of bacterial terpene synthases. Angew Chem Int Ed 2013, 52:1810-1812.
    • (2013) Angew Chem Int Ed , vol.52 , pp. 1810-1812
    • Rabe, P.1    Dickschat, J.S.2
  • 33
    • 33745631233 scopus 로고    scopus 로고
    • Identifying and manipulating structural determinates linking catalytic specificities in terpene synthases
    • Greenhagen B.T., O'Maille P.E., Noel J.P., Chappell J. Identifying and manipulating structural determinates linking catalytic specificities in terpene synthases. Proc Natl Acad Sci U S A 2006, 103:9826-9831.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9826-9831
    • Greenhagen, B.T.1    O'Maille, P.E.2    Noel, J.P.3    Chappell, J.4
  • 34
    • 33847049467 scopus 로고    scopus 로고
    • X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate
    • Shishova E.Y., Di Costanzo L., Cane D.E., Christianson D.W. X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate. Biochemistry 2007, 46:1941-1951.
    • (2007) Biochemistry , vol.46 , pp. 1941-1951
    • Shishova, E.Y.1    Di Costanzo, L.2    Cane, D.E.3    Christianson, D.W.4
  • 35
    • 79955020478 scopus 로고    scopus 로고
    • Electrostatic effects on (di)terpene synthase product outcome
    • Zhou K., Peters R.J. Electrostatic effects on (di)terpene synthase product outcome. Chem Commun 2011, 47:4074-4080.
    • (2011) Chem Commun , vol.47 , pp. 4074-4080
    • Zhou, K.1    Peters, R.J.2
  • 36
    • 80051584607 scopus 로고    scopus 로고
    • Biosynthesis via carbocations: theoretical studies on terpene formation
    • Tantillo D.J. Biosynthesis via carbocations: theoretical studies on terpene formation. Nat Prod Rep 2011, 28:1035-1053.
    • (2011) Nat Prod Rep , vol.28 , pp. 1035-1053
    • Tantillo, D.J.1
  • 37
    • 0142029089 scopus 로고    scopus 로고
    • Balancing kinetic and thermodynamic control: the mechanism of carbocation cyclization by squalene cyclase
    • Rajamani R., Gao J. Balancing kinetic and thermodynamic control: the mechanism of carbocation cyclization by squalene cyclase. J Am Chem Soc 2003, 125:12768-12781.
    • (2003) J Am Chem Soc , vol.125 , pp. 12768-12781
    • Rajamani, R.1    Gao, J.2
  • 38
    • 35848965918 scopus 로고    scopus 로고
    • Synthetic efficiency in enzyme mechanisms involving carbocations: aristolochene synthase
    • Allemann R.K., Young N.J., Ma S., Truhlar D.G., Gao J. Synthetic efficiency in enzyme mechanisms involving carbocations: aristolochene synthase. J Am Chem Soc 2007, 129:13008-13013.
    • (2007) J Am Chem Soc , vol.129 , pp. 13008-13013
    • Allemann, R.K.1    Young, N.J.2    Ma, S.3    Truhlar, D.G.4    Gao, J.5
  • 39
    • 77952083065 scopus 로고    scopus 로고
    • Challenges posed to bornyl diphosphate synthase: diverging reaction mechanisms in monoterpenes
    • Weitman M., Major D.T. Challenges posed to bornyl diphosphate synthase: diverging reaction mechanisms in monoterpenes. J Am Chem Soc 2010, 132:6349-6360.
    • (2010) J Am Chem Soc , vol.132 , pp. 6349-6360
    • Weitman, M.1    Major, D.T.2
  • 40
    • 84870323486 scopus 로고    scopus 로고
    • Electrostatically guided dynamics-the root of fidelity in a promiscuous terpene synthase?
    • Major D.T., Weitman M. Electrostatically guided dynamics-the root of fidelity in a promiscuous terpene synthase?. J Am Chem Soc 2012, 134:19454-19462.
    • (2012) J Am Chem Soc , vol.134 , pp. 19454-19462
    • Major, D.T.1    Weitman, M.2
  • 41
    • 0017100947 scopus 로고
    • Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Warshel A., Levitt M. Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J Mol Biol 1976, 103:227-249.
    • (1976) J Mol Biol , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 42
    • 33646351072 scopus 로고    scopus 로고
    • Nonclassical carbocations as CH hydrogen bond donors
    • Bojin M.D., Tantillo D.J. Nonclassical carbocations as CH hydrogen bond donors. J Phys Chem A 2006, 110:4810-4816.
    • (2006) J Phys Chem A , vol.110 , pp. 4810-4816
    • Bojin, M.D.1    Tantillo, D.J.2
  • 44
    • 69249168676 scopus 로고    scopus 로고
    • A potential energy surface bifurcation in terpene biosynthesis
    • Hong Y.J., Tantillo D.J. A potential energy surface bifurcation in terpene biosynthesis. Nat Chem 2009, 1:384-389.
    • (2009) Nat Chem , vol.1 , pp. 384-389
    • Hong, Y.J.1    Tantillo, D.J.2
  • 45
    • 82355169264 scopus 로고    scopus 로고
    • Do we fully understand what controls chemical selectivity?
    • Rehbein J., Carpenter B.K. Do we fully understand what controls chemical selectivity?. Phys Chem Chem Phys 2011, 13:20906-20922.
    • (2011) Phys Chem Chem Phys , vol.13 , pp. 20906-20922
    • Rehbein, J.1    Carpenter, B.K.2
  • 46
    • 0037065665 scopus 로고    scopus 로고
    • X-ray crystal structures of D100E trichodiene synthase and its pyrophosphate complex reveal the basis for terpene product diversity
    • Rynkiewicz M.J., Cane D.E., Christianson D.W. X-ray crystal structures of D100E trichodiene synthase and its pyrophosphate complex reveal the basis for terpene product diversity. Biochemistry 2002, 41:1732-1741.
    • (2002) Biochemistry , vol.41 , pp. 1732-1741
    • Rynkiewicz, M.J.1    Cane, D.E.2    Christianson, D.W.3
  • 47
    • 84863651510 scopus 로고    scopus 로고
    • Collective reaction coordinate for hybrid quantum and molecular mechanics simulations: a case study of the hydride transfer in dihydrofolate reductase
    • Doron D., Kohen A., Major D.T. Collective reaction coordinate for hybrid quantum and molecular mechanics simulations: a case study of the hydride transfer in dihydrofolate reductase. J Chem Theory Comput 2012, 8:2484-2496.
    • (2012) J Chem Theory Comput , vol.8 , pp. 2484-2496
    • Doron, D.1    Kohen, A.2    Major, D.T.3
  • 48
    • 25444471816 scopus 로고    scopus 로고
    • Implementation of the bisection sampling method in path integral simulations
    • Major D.T., Gao J.L. Implementation of the bisection sampling method in path integral simulations. J Mol Graph Model 2005, 24:121-127.
    • (2005) J Mol Graph Model , vol.24 , pp. 121-127
    • Major, D.T.1    Gao, J.L.2
  • 49
    • 36148963327 scopus 로고    scopus 로고
    • An integrated path integral and free-energy perturbation-umbrella sampling method for computing kinetic isotope effects of chemical reactions in solution and in enzymes
    • Major D.T., Gao J.L. An integrated path integral and free-energy perturbation-umbrella sampling method for computing kinetic isotope effects of chemical reactions in solution and in enzymes. J Chem Theory Comput 2007, 3:949-960.
    • (2007) J Chem Theory Comput , vol.3 , pp. 949-960
    • Major, D.T.1    Gao, J.L.2
  • 50
    • 33746911013 scopus 로고    scopus 로고
    • Path integral simulations of proton transfer reactions in aqueous solution using combined QM/MM potentials
    • Major D.T., Garcia-Viloca M., Gao J.L. Path integral simulations of proton transfer reactions in aqueous solution using combined QM/MM potentials. J Chem Theory Comput 2006, 2:236-245.
    • (2006) J Chem Theory Comput , vol.2 , pp. 236-245
    • Major, D.T.1    Garcia-Viloca, M.2    Gao, J.L.3
  • 51
    • 80051583624 scopus 로고    scopus 로고
    • Physical constraints on sesquiterpene diversity arising from cyclization of the eudesm-5-yl carbocation
    • Andes Hess B.J., Smentek L., Noel J.P., O'Maille P.E. Physical constraints on sesquiterpene diversity arising from cyclization of the eudesm-5-yl carbocation. J Am Chem Soc 2011, 133:12632-12641.
    • (2011) J Am Chem Soc , vol.133 , pp. 12632-12641
    • Andes Hess, B.J.1    Smentek, L.2    Noel, J.P.3    O'Maille, P.E.4
  • 52
    • 84876731984 scopus 로고    scopus 로고
    • Squalene hopene cyclases: highly promiscuous and evolvable catalysts for stereoselective CC and CX bond formation
    • Hammer S.C., Syren P.-O., Seitz M., Nestl B.M., Hauer B. Squalene hopene cyclases: highly promiscuous and evolvable catalysts for stereoselective CC and CX bond formation. Curr Opin Chem Biol 2013, 17:293-300.
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 293-300
    • Hammer, S.C.1    Syren, P.-O.2    Seitz, M.3    Nestl, B.M.4    Hauer, B.5
  • 53
    • 84870307882 scopus 로고    scopus 로고
    • Catalytic mechanism and product specificity of oxidosqualene-lanosterol cyclase: a QM/MM study
    • Tian B.-X., Eriksson L.A. Catalytic mechanism and product specificity of oxidosqualene-lanosterol cyclase: a QM/MM study. J Phys Chem B 2012, 116:13857-13862.
    • (2012) J Phys Chem B , vol.116 , pp. 13857-13862
    • Tian, B.-X.1    Eriksson, L.A.2
  • 54
    • 2942628424 scopus 로고    scopus 로고
    • Concerted nature of AB ring formation in the enzymatic cyclization of squalene to hopenes
    • Andes Hess B., Smentek J.L. Concerted nature of AB ring formation in the enzymatic cyclization of squalene to hopenes. Org Lett 2004, 6:1717-1720.
    • (2004) Org Lett , vol.6 , pp. 1717-1720
    • Andes Hess, B.1    Smentek, J.L.2
  • 55
    • 78650087420 scopus 로고    scopus 로고
    • Compelling computational evidence for the concerted cyclization of the ABC rings of hopene from protonated squalene
    • Smentek L., Andes Hess B.J. Compelling computational evidence for the concerted cyclization of the ABC rings of hopene from protonated squalene. J Am Chem Soc 2010, 132:17111-17117.
    • (2010) J Am Chem Soc , vol.132 , pp. 17111-17117
    • Smentek, L.1    Andes Hess, B.J.2
  • 56
    • 45749137172 scopus 로고    scopus 로고
    • Stereochemistry of eudesmane cation formation during catalysis by aristolochene synthase from Penicillium roqueforti
    • Miller D.J., Gao J., Truhlar D.G., Young N.J., Gonzaleza V., Allemann R.K. Stereochemistry of eudesmane cation formation during catalysis by aristolochene synthase from Penicillium roqueforti. Org Biomol Chem 2008, 6:2346-2354.
    • (2008) Org Biomol Chem , vol.6 , pp. 2346-2354
    • Miller, D.J.1    Gao, J.2    Truhlar, D.G.3    Young, N.J.4    Gonzaleza, V.5    Allemann, R.K.6
  • 57
    • 84887594651 scopus 로고    scopus 로고
    • Conformational change and ligand binding in the aristolochene synthase catalytic cycle
    • van der Kamp M.W., Sirirak J., Zurek J., Allemann R.K., Mulholland A.J. Conformational change and ligand binding in the aristolochene synthase catalytic cycle. Biochemistry 2013, 52:8094-8105.
    • (2013) Biochemistry , vol.52 , pp. 8094-8105
    • van der Kamp, M.W.1    Sirirak, J.2    Zurek, J.3    Allemann, R.K.4    Mulholland, A.J.5
  • 59
    • 84857705214 scopus 로고    scopus 로고
    • The role of aristolochene synthase in diphosphate activation
    • Faraldos J.A., Gonzalez V., Allemann R.K. The role of aristolochene synthase in diphosphate activation. Chem Commun 2012, 48:3230-3232.
    • (2012) Chem Commun , vol.48 , pp. 3230-3232
    • Faraldos, J.A.1    Gonzalez, V.2    Allemann, R.K.3
  • 60
    • 77957675477 scopus 로고    scopus 로고
    • Quantum chemical dissection of the classic terpinyl/pinyl/bornyl/camphyl cation conundrum-the role of pyrophosphate in manipulating pathways to monoterpenes
    • Hong Y.J., Tantillo D.J. Quantum chemical dissection of the classic terpinyl/pinyl/bornyl/camphyl cation conundrum-the role of pyrophosphate in manipulating pathways to monoterpenes. Org Biomol Chem 2010, 8:4589-4600.
    • (2010) Org Biomol Chem , vol.8 , pp. 4589-4600
    • Hong, Y.J.1    Tantillo, D.J.2
  • 61
    • 55549098582 scopus 로고    scopus 로고
    • Control elements in dynamically determined selectivity on a bifurcating surface
    • Thomas J.B., Waas J.R., Harmata M., Singleton D.A. Control elements in dynamically determined selectivity on a bifurcating surface. J Am Chem Soc 2008, 130:14544-14555.
    • (2008) J Am Chem Soc , vol.130 , pp. 14544-14555
    • Thomas, J.B.1    Waas, J.R.2    Harmata, M.3    Singleton, D.A.4
  • 62
    • 70349630685 scopus 로고    scopus 로고
    • Dynamics and the failure of transition state theory in alkene hydroboration
    • Oyola Y., Singleton D.A. Dynamics and the failure of transition state theory in alkene hydroboration. J Am Chem Soc 2009, 131:3130-3131.
    • (2009) J Am Chem Soc , vol.131 , pp. 3130-3131
    • Oyola, Y.1    Singleton, D.A.2
  • 63
    • 84893021866 scopus 로고    scopus 로고
    • Biosynthetic consequences of multiple sequential post-transition-state bifurcations
    • Hong Y.J., Tantillo D.J. Biosynthetic consequences of multiple sequential post-transition-state bifurcations. Nat Chem 2014, 6:104-111.
    • (2014) Nat Chem , vol.6 , pp. 104-111
    • Hong, Y.J.1    Tantillo, D.J.2
  • 64
    • 84892994558 scopus 로고    scopus 로고
    • It's all downhill from here
    • Hornsby C.E., Paton R.S. It's all downhill from here. Nat Chem 2014, 6:88-89.
    • (2014) Nat Chem , vol.6 , pp. 88-89
    • Hornsby, C.E.1    Paton, R.S.2
  • 66
    • 0032511026 scopus 로고    scopus 로고
    • Monoterpene synthases from common sage (Salvia officinalis)
    • Wise M.L., Savage T.J., Katahira E., Croteau R. Monoterpene synthases from common sage (Salvia officinalis). J Biol Chem 1998, 273:14891-14899.
    • (1998) J Biol Chem , vol.273 , pp. 14891-14899
    • Wise, M.L.1    Savage, T.J.2    Katahira, E.3    Croteau, R.4
  • 67
    • 0035908186 scopus 로고    scopus 로고
    • Stereochemical disposition of the geminal dimethyl groups in the enzymatic cyclization of geranyl diphosphate to (+)-bornyl diphosphate by recombinant (+)-bornyl diphosphate synthase from Salvia officinalis
    • Wise M.L., Pyun H.-J., Helms G., Assink B., Coates R.M., Croteau R.B. Stereochemical disposition of the geminal dimethyl groups in the enzymatic cyclization of geranyl diphosphate to (+)-bornyl diphosphate by recombinant (+)-bornyl diphosphate synthase from Salvia officinalis. Tetrahedron 2001, 57:5327-5334.
    • (2001) Tetrahedron , vol.57 , pp. 5327-5334
    • Wise, M.L.1    Pyun, H.-J.2    Helms, G.3    Assink, B.4    Coates, R.M.5    Croteau, R.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.