메뉴 건너뛰기




Volumn 114, Issue 29, 2010, Pages 9622-9628

Catalytic mechanism of hydroxynitrile lyase from hevea brasiliensis: A theoretical investigation

Author keywords

[No Author keywords available]

Indexed keywords

ACETONE; CATALYSIS; CRYSTAL ATOMIC STRUCTURE; CYANIDES; HYDROGEN BONDS; REACTION KINETICS;

EID: 77954935929     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp100373e     Document Type: Article
Times cited : (14)

References (48)
  • 2
    • 77954923494 scopus 로고
    • Ciba Foundation Symposium; John Wiley and Sons: Chichester, U.K
    • Cyanide Compounds in Biology; Evered, D., Harnett, S., Eds.; Ciba Foundation Symposium 140; John Wiley and Sons: Chichester, U.K., 1988; pp 67 - 91.
    • (1988) Cyanide Compounds in Biology , vol.140 , pp. 67-99
    • Evered, D.1    Harnett, S.2
  • 3
    • 0000966890 scopus 로고
    • Mobilization and Utilization of Cyanogenic Glycosides: The Linustatin Pathway
    • Selmar, D.; Lieberei, R.; Biehl, B. Mobilization and Utilization of Cyanogenic Glycosides: The Linustatin Pathway Plant Physiol. 1988, 86, 711-716
    • (1988) Plant Physiol. , vol.86 , pp. 711-716
    • Selmar, D.1    Lieberei, R.2    Biehl, B.3
  • 4
    • 0002545280 scopus 로고
    • α-Hydroxynitrile Lyase in Hevea brasiliensis and its Significance for Rapid Cyanogenesis
    • Selmar, D.; Lieberei, R.; Biehl, B.; Conn, E. E. α-Hydroxynitrile Lyase in Hevea brasiliensis and its Significance for Rapid Cyanogenesis Physiol. Plant. 1989, 75, 91-101
    • (1989) Physiol. Plant. , vol.75 , pp. 91-101
    • Selmar, D.1    Lieberei, R.2    Biehl, B.3    Conn, E.E.4
  • 5
    • 0024728476 scopus 로고
    • Mandelonitrile Lyase from Ximenia americana L.: Stereospecificity and Lack of Flavin Prosthetic Group
    • Kuroki, G. W.; Conn, E. E. Mandelonitrile Lyase from Ximenia americana L.: Stereospecificity and Lack of Flavin Prosthetic Group Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 6978-6981
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 6978-6981
    • Kuroki, G.W.1    Conn, E.E.2
  • 7
    • 0030441331 scopus 로고    scopus 로고
    • Hydroxynitrile Lyases: Functions and Properties
    • Hickel, A.; Hasslacher, M.; Griengl, H. Hydroxynitrile Lyases: Functions and Properties Physiol. Plant. 1996, 98, 891-898
    • (1996) Physiol. Plant. , vol.98 , pp. 891-898
    • Hickel, A.1    Hasslacher, M.2    Griengl, H.3
  • 8
    • 0029909939 scopus 로고    scopus 로고
    • Hydroxynitrile Lyases of Higher Plants
    • Wajant, H.; Effenberger, F. Hydroxynitrile Lyases of Higher Plants Biol. Chem. 1996, 377, 611-617
    • (1996) Biol. Chem. , vol.377 , pp. 611-617
    • Wajant, H.1    Effenberger, F.2
  • 9
    • 0002123773 scopus 로고
    • Metabolization of Cyanogenic Glucosides in Hevea brasiliensis
    • Lieberei, R.; Selmar, D.; Biehl, B. Metabolization of Cyanogenic Glucosides in Hevea brasiliensis Plant Syst. Evol. 1985, 150, 49-63
    • (1985) Plant Syst. Evol. , vol.150 , pp. 49-63
    • Lieberei, R.1    Selmar, D.2    Biehl, B.3
  • 10
    • 0000713888 scopus 로고
    • Apoplastic Occurrence of Cyanogenic Beta-Glucosidases and Consequences for the Metabolism of Cyanogenic Glucosides
    • Selmar, D. Apoplastic Occurrence of Cyanogenic Beta-Glucosidases and Consequences for the Metabolism of Cyanogenic Glucosides ACS Symp. Ser. 1993, 13, 191-204
    • (1993) ACS Symp. Ser. , vol.13 , pp. 191-204
    • Selmar, D.1
  • 11
    • 33748215202 scopus 로고
    • Synthesis and Reactions of Optically Active Cyanohydrins
    • Effenberger, F. Synthesis and Reactions of Optically Active Cyanohydrins Angew. Chem., Int. Ed. Engl. 1994, 33, 1555-1564
    • (1994) Angew. Chem., Int. Ed. Engl. , vol.33 , pp. 1555-1564
    • Effenberger, F.1
  • 13
    • 0027325846 scopus 로고
    • Aliphatic (S)-Cyanohydrins by Enzyme Catalyzed Synthesis
    • Klempier, N.; Griengl, H.; Hayn, M. Aliphatic (S)-Cyanohydrins by Enzyme Catalyzed Synthesis Tetrahedron Lett. 1993, 34, 4769-4772
    • (1993) Tetrahedron Lett. , vol.34 , pp. 4769-4772
    • Klempier, N.1    Griengl, H.2    Hayn, M.3
  • 14
    • 0028964103 scopus 로고
    • Synthesis of α/β-Unsaturated (S)-Cyanohydrins Using the Oxynitrilase from Hevea brasiliensis
    • Klempier, N.; Pichler, U.; Griengl, H. Synthesis of α/β- Unsaturated (S)-Cyanohydrins Using the Oxynitrilase from Hevea brasiliensis Tetrahedron: Asymmetry 1995, 6, 845-848
    • (1995) Tetrahedron: Asymmetry , vol.6 , pp. 845-848
    • Klempier, N.1    Pichler, U.2    Griengl, H.3
  • 16
    • 21644433892 scopus 로고    scopus 로고
    • Hydroxynitrile Lyase: At the Interface of Biology and Chemistry
    • Sharma, M.; Sharma, N. N.; Bhalla, T. C. Hydroxynitrile Lyase: At the Interface of Biology and Chemistry Enzyme Microb. Technol. 2005, 37, 279-294
    • (2005) Enzyme Microb. Technol. , vol.37 , pp. 279-294
    • Sharma, M.1    Sharma, N.N.2    Bhalla, T.C.3
  • 17
    • 34547168548 scopus 로고    scopus 로고
    • Hydroxynitrile Lyase-Catalyzed Enzymatic Nitroaldol (Henry) Reaction
    • Khadjawi, M. G.; Parkarthofer, T.; Skranc, W.; Griengl, H. Hydroxynitrile Lyase-Catalyzed Enzymatic Nitroaldol (Henry) Reaction Adv. Synth. Catal. 2007, 349, 1445-1450
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1445-1450
    • Khadjawi, M.G.1    Parkarthofer, T.2    Skranc, W.3    Griengl, H.4
  • 18
    • 52049088539 scopus 로고    scopus 로고
    • Atomic Resolution Crystal Structure and Quantum Chemistry Meet to Reveal Subtleties of Hydroxynitrile Lyase Catalysis
    • Schmidt, A.; Gruber, K.; Kratky, C.; Lamzin, V. S. Atomic Resolution Crystal Structure and Quantum Chemistry Meet to Reveal Subtleties of Hydroxynitrile Lyase Catalysis J. Biol. Chem. 2008, 283, 21827-21836
    • (2008) J. Biol. Chem. , vol.283 , pp. 21827-21836
    • Schmidt, A.1    Gruber, K.2    Kratky, C.3    Lamzin, V.S.4
  • 19
    • 2442485744 scopus 로고    scopus 로고
    • Reaction Mechanism of Hydroxynitrile Lyases of the α/β- Hydrolase Superfamily
    • Gruber, K.; Gartler, G.; Krammer, B.; Schwab, H.; Kratky, C. Reaction Mechanism of Hydroxynitrile Lyases of the α/β-Hydrolase Superfamily J. Biol. Chem. 2004, 279, 20501-20510
    • (2004) J. Biol. Chem. , vol.279 , pp. 20501-20510
    • Gruber, K.1    Gartler, G.2    Krammer, B.3    Schwab, H.4    Kratky, C.5
  • 20
    • 0030586027 scopus 로고    scopus 로고
    • Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis
    • DOI 10.1016/S0969-2126(96)00088-3
    • Wagner, U. G.; Hasslacher, M.; Griengl, H.; Schwab, H.; Kratky, C. Mechanism of Cyanogenesis: the Crystal Structure of Hydroxynitrile Lyase from Hevea brasiliensis Structure 1996, 4, 811-822 (Pubitemid 26312365)
    • (1996) Structure , vol.4 , Issue.7 , pp. 811-822
    • Wagner, U.G.1    Hasslacher, M.2    Griengl, H.3    Schwab, H.4    Kratky, C.5
  • 21
    • 0029955020 scopus 로고    scopus 로고
    • Identification of Potential Active-Site Residues in the Hydroxynitrile Lyase from Manihot esculenta by Site-Sirected Mutagenesis
    • Wajant, H.; Pfizenmaier, K. Identification of Potential Active-Site Residues in the Hydroxynitrile Lyase from Manihot esculenta by Site-Sirected Mutagenesis J. Biol. Chem. 1996, 271, 25830-25834
    • (1996) J. Biol. Chem. , vol.271 , pp. 25830-25834
    • Wajant, H.1    Pfizenmaier, K.2
  • 22
    • 0029978870 scopus 로고    scopus 로고
    • Molecular Cloning of the Full-Length cDNA of (S)-Hydroxynitrile Lyase from Hevea brasiliensis
    • Hasslacher, M.; Schall, M.; Hayn, M.; Griengl, H.; Kohlwein, S. D.; Schwab, H. Molecular Cloning of the Full-Length cDNA of (S)-Hydroxynitrile Lyase from Hevea brasiliensis J. Biol. Chem. 1996, 271, 5884-5891
    • (1996) J. Biol. Chem. , vol.271 , pp. 5884-5891
    • Hasslacher, M.1    Schall, M.2    Hayn, M.3    Griengl, H.4    Kohlwein, S.D.5    Schwab, H.6
  • 24
    • 0030057585 scopus 로고    scopus 로고
    • Purification and Characterization of Hydroxynitrile Lyase from Hevea brasillensis
    • Wajant, H.; Foerster, S. Purification and Characterization of Hydroxynitrile Lyase from Hevea brasillensis Plant Sci. 1996, 115, 25-31
    • (1996) Plant Sci. , vol.115 , pp. 25-31
    • Wajant, H.1    Foerster, S.2
  • 26
    • 0032852375 scopus 로고    scopus 로고
    • Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis
    • Zuegg, J.; Gruber, K.; Gugganig, M.; Wagner, U. G.; Kratky, C. Three-Dimensional Structures of Enzyme-Substrate Complexes of the Hydroxynitrile Lyase from Hevea brasiliensis Protein Sci. 1999, 8, 1990-2000 (Pubitemid 29489926)
    • (1999) Protein Science , vol.8 , Issue.10 , pp. 1990-2000
    • Zuegg, J.1    Gruber, K.2    Gugganig, M.3    Wagner, U.G.4    Kratky, C.5
  • 27
    • 0035400446 scopus 로고    scopus 로고
    • Elucidation of the Mode of Substrate Binding to Hydroxynitrile Lyase from Hevea brasiliensis
    • Gruber, K. Elucidation of the Mode of Substrate Binding to Hydroxynitrile Lyase from Hevea brasiliensis Proteins: Struct., Funct., Genet. 2001, 44, 26-31
    • (2001) Proteins: Struct., Funct., Genet. , vol.44 , pp. 26-31
    • Gruber, K.1
  • 28
    • 18444364203 scopus 로고    scopus 로고
    • Methyl Transfer in Glycine N -Methyltransferase. A Theoretical Study
    • Velichkova, P.; Himo, F. Methyl Transfer in Glycine N -Methyltransferase. A Theoretical Study J. Phys. Chem. B 2005, 109, 8216-8219
    • (2005) J. Phys. Chem. B , vol.109 , pp. 8216-8219
    • Velichkova, P.1    Himo, F.2
  • 29
    • 84962459998 scopus 로고    scopus 로고
    • Theoretical Study of General Base-Catalyzed Hydrolysis of Aryl Esters and Implications for Enzymatic Reactions
    • Xie, D. Q.; Xu, D. G.; Zhang, L. D.; Guo, H. Theoretical Study of General Base-Catalyzed Hydrolysis of Aryl Esters and Implications for Enzymatic Reactions J. Phys. Chem. B 2005, 109, 5259-5266
    • (2005) J. Phys. Chem. B , vol.109 , pp. 5259-5266
    • Xie, D.Q.1    Xu, D.G.2    Zhang, L.D.3    Guo, H.4
  • 30
    • 51349146401 scopus 로고    scopus 로고
    • Density Functional Theory Study of the Reaction Mechanism of the DNA Repairing Enzyme Alkylguanine Alkyltransferase
    • Georgieva, P.; Himo, F. Density Functional Theory Study of the Reaction Mechanism of the DNA Repairing Enzyme Alkylguanine Alkyltransferase Chem. Phys. Let. 2008, 463, 214-218
    • (2008) Chem. Phys. Let. , vol.463 , pp. 214-218
    • Georgieva, P.1    Himo, F.2
  • 31
    • 26844493581 scopus 로고    scopus 로고
    • Density-Functional Study of Mechanisms for the Cofactor-Free Decarboxylation Performed by Uroporphyrinogen III Decarboxylase
    • Silva, P. J.; Ramos, M. J. Density-Functional Study of Mechanisms for the Cofactor-Free Decarboxylation Performed by Uroporphyrinogen III Decarboxylase J. Phys. Chem. B 2005, 109, 18195-18200
    • (2005) J. Phys. Chem. B , vol.109 , pp. 18195-18200
    • Silva, P.J.1    Ramos, M.J.2
  • 32
    • 33646376220 scopus 로고    scopus 로고
    • Catalytic Mechanism of 6-Phosphogluconate Dehydrogenase: A Theoretical Investigation
    • Wang, J. Y.; Li, S. H. Catalytic Mechanism of 6-Phosphogluconate Dehydrogenase: A Theoretical Investigation J. Phys. Chem. B 2006, 110, 7029-7035
    • (2006) J. Phys. Chem. B , vol.110 , pp. 7029-7035
    • Wang, J.Y.1    Li, S.H.2
  • 33
    • 16244414333 scopus 로고    scopus 로고
    • Theoretical Insights into the Mechanism of Acetylcholinesterase-Catalyzed Acylation of Acetylcholine
    • Manojkumar, T. K.; Cui, C. Z.; Kim, K. S. Theoretical Insights into the Mechanism of Acetylcholinesterase-Catalyzed Acylation of Acetylcholine J. Comput. Chem. 2005, 26, 606-611
    • (2005) J. Comput. Chem. , vol.26 , pp. 606-611
    • Manojkumar, T.K.1    Cui, C.Z.2    Kim, K.S.3
  • 34
    • 33748532821 scopus 로고    scopus 로고
    • Theoretical study of the full reaction mechanism of human soluble epoxide hydrolase
    • DOI 10.1002/chem.200501519
    • Hopmann, K. H.; Himo, F. Theoretical Study of the Full Reaction Mechanism of Human Soluble Epoxide Hydrolase Chem. - Eur. J. 2006, 12, 6898-6909 (Pubitemid 44369222)
    • (2006) Chemistry - A European Journal , vol.12 , Issue.26 , pp. 6898-6909
    • Hopmann, K.H.1    Himo, F.2
  • 35
    • 0037950581 scopus 로고    scopus 로고
    • Theoretical Studies on the Mechanism of Inhibition of Ribonucleotide Reductase by (E)-2′-Fluoromethylene-2′-Deoxycitidine-5′- Diphosphate
    • Fernandes, P. A.; Ramos, M. J. Theoretical Studies on the Mechanism of Inhibition of Ribonucleotide Reductase by (E)-2′-Fluoromethylene-2′- Deoxycitidine-5′-Diphosphate J. Am. Chem. Soc. 2003, 125, 6311-6322
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6311-6322
    • Fernandes, P.A.1    Ramos, M.J.2
  • 36
    • 33947398730 scopus 로고    scopus 로고
    • Oxime-Induced Reactivation of Sarin-Inhibited AChE: A Theoretical Mechanisms Study
    • Wang, J.; Gu, J. D.; Leszczynski, J.; Feliks, M.; Sokalski, W. A. Oxime-Induced Reactivation of Sarin-Inhibited AChE: A Theoretical Mechanisms Study J. Phys. Chem. B 2007, 111, 2404-2408
    • (2007) J. Phys. Chem. B , vol.111 , pp. 2404-2408
    • Wang, J.1    Gu, J.D.2    Leszczynski, J.3    Feliks, M.4    Sokalski, W.A.5
  • 37
    • 0000189651 scopus 로고
    • Density-Functional Thermochemistry. III. The Role of Exact Exchange
    • Beck, A. D. Density-Functional Thermochemistry. III. The Role of Exact Exchange J. Chem. Phys. 1993, 98, 5648-5652
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Beck, A.D.1
  • 38
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti Correlation-Energy Formula into a Functional of the Electron Density
    • Lee, C.; Yang, W.; Parr, R. G. Development of the Colle-Salvetti Correlation-Energy Formula into a Functional of the Electron Density Phys. Rev. B 1988, 37, 785-789
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 39
    • 0038596731 scopus 로고
    • Results Obtained with the Correlation Energy Density Functionals of Becke and Lee, Yang and Parr
    • Miehlich, B.; Savin, A.; Stoll, H.; Preuss, H. Results Obtained with the Correlation Energy Density Functionals of Becke and Lee, Yang and Parr Chem. Phys. Lett. 1989, 157, 200-206
    • (1989) Chem. Phys. Lett. , vol.157 , pp. 200-206
    • Miehlich, B.1    Savin, A.2    Stoll, H.3    Preuss, H.4
  • 41
    • 36549103221 scopus 로고
    • Natural Localized Molecular Orbitals
    • Reed, A. E.; Weinhold, F. Natural Localized Molecular Orbitals J. Chem. Phys. 1985, 83, 1736-1740
    • (1985) J. Chem. Phys. , vol.83 , pp. 1736-1740
    • Reed, A.E.1    Weinhold, F.2
  • 42
    • 0011083499 scopus 로고
    • Intermolecular Interactions from a Natural Bond Orbital, Donor-Acceptor Viewpoint
    • Reed, A. E.; Curtiss, L. A.; Weinhold, F. Intermolecular Interactions from a Natural Bond Orbital, Donor-Acceptor Viewpoint Chem. Rev. 1988, 88, 899-926
    • (1988) Chem. Rev. , vol.88 , pp. 899-926
    • Reed, A.E.1    Curtiss, L.A.2    Weinhold, F.3
  • 43
    • 0031209054 scopus 로고    scopus 로고
    • A New Integral Equation Formalism for the Polarizable Continuum Model: Theoretical Background and Applications to Isotropic and Anisotropic Dielectrics
    • Cancès, M. T.; Mennucci, B.; Tomasi, J. A New Integral Equation Formalism for the Polarizable Continuum Model: Theoretical Background and Applications to Isotropic and Anisotropic Dielectrics J. Chem. Phys. 1997, 107, 3032-3041
    • (1997) J. Chem. Phys. , vol.107 , pp. 3032-3041
    • Cancès, M.T.1    Mennucci, B.2    Tomasi, J.3
  • 44
    • 84961979198 scopus 로고    scopus 로고
    • Continuum Solvation Models: A New Approach to the Problem of Solutes Charge Distribution and Cavity Boundaries
    • Mennucci, B.; Tomasi, J. Continuum Solvation Models: A New Approach to the Problem of Solutes Charge Distribution and Cavity Boundaries J. Chem. Phys. 1997, 106, 5151-5158
    • (1997) J. Chem. Phys. , vol.106 , pp. 5151-5158
    • Mennucci, B.1    Tomasi, J.2
  • 45
    • 84962359221 scopus 로고    scopus 로고
    • Ab initio Study of Solvated Molecules: A New Implementation of the Polarizable Continuum Model
    • Cossi, M.; Barone, V.; Mennucci, B.; Tomasi, J. Ab initio Study of Solvated Molecules: A New Implementation of the Polarizable Continuum Model Chem. Phys. Lett. 1996, 255, 327-335
    • (1996) Chem. Phys. Lett. , vol.255 , pp. 327-335
    • Cossi, M.1    Barone, V.2    Mennucci, B.3    Tomasi, J.4
  • 46
    • 1542378733 scopus 로고    scopus 로고
    • Quantum Chemical Studies of Intermediates and Reaction Pathways in Selected Enzymes and Catalytic Synthetic Systems
    • Noodleman, L.; Lovell, T.; Han, W. G.; Li, J.; Himo, F. Quantum Chemical Studies of Intermediates and Reaction Pathways in Selected Enzymes and Catalytic Synthetic Systems Chem. Rev. 2004, 104, 459-508
    • (2004) Chem. Rev. , vol.104 , pp. 459-508
    • Noodleman, L.1    Lovell, T.2    Han, W.G.3    Li, J.4    Himo, F.5
  • 47
    • 15544366274 scopus 로고    scopus 로고
    • Benchmark Database of Barrier Heights for Heavy Atom Transfer, Nucleophilic Substitution, Association, and Unimolecular Reactions and Its Use to Test Theoretical Methods
    • Zhao, Y.; García, N. G.; Truhlar, D. G. Benchmark Database of Barrier Heights for Heavy Atom Transfer, Nucleophilic Substitution, Association, and Unimolecular Reactions and Its Use to Test Theoretical Methods J. Phys. Chem. A 2005, 109, 2012-2018
    • (2005) J. Phys. Chem. A , vol.109 , pp. 2012-2018
    • Zhao, Y.1    García, N.G.2    Truhlar, D.G.3
  • 48
    • 0002545280 scopus 로고
    • α-Hydroxynitrile Lyase in Hevea brasiliensis and its Significance for Rapid Cyanogenesis
    • Selmar, R.; Lieberei, R.; Biehl, B.; Conn, E. E. α-Hydroxynitrile Lyase in Hevea brasiliensis and its Significance for Rapid Cyanogenesis Physiol. Plant. 1989, 75, 97-101
    • (1989) Physiol. Plant. , vol.75 , pp. 97-101
    • Selmar, R.1    Lieberei, R.2    Biehl, B.3    Conn, E.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.