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Volumn 1844, Issue 12, 2014, Pages 2059-2067

Structural and functional analysis of hydroxynitrile lyase from Baliospermum montanum with crystal structure, molecular dynamics and enzyme kinetics

Author keywords

Broad substrate specificity; Crystal structure; Enzyme kinetics; High benzyl affinity; Hydroxynitrile lyase; Molecular dynamics simulation

Indexed keywords

BENZENE; HYDROLASE; HYDROXYNITRILE LYASE; NITRILE;

EID: 84907646046     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.09.004     Document Type: Article
Times cited : (21)

References (37)
  • 1
    • 0000140586 scopus 로고    scopus 로고
    • Cyanohydrins in nature and the laboratory: Biology, preparations, and synthetic applications
    • R.J. Gregory Cyanohydrins in nature and the laboratory: biology, preparations, and synthetic applications Chem. Rev. 99 1999 3649 3682
    • (1999) Chem. Rev. , vol.99 , pp. 3649-3682
    • Gregory, R.J.1
  • 2
    • 80052468032 scopus 로고    scopus 로고
    • Hydroxynitrile lyases: Insights into biochemistry, discovery, and engineering
    • M. Dadashipour, and Y. Asano Hydroxynitrile lyases: insights into biochemistry, discovery, and engineering ACS Catal. 1 2011 1121 1149
    • (2011) ACS Catal. , vol.1 , pp. 1121-1149
    • Dadashipour, M.1    Asano, Y.2
  • 3
    • 65249128570 scopus 로고    scopus 로고
    • Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity
    • I. Dreveny, A.S. Andryushkova, A. Glieder, K. Gruber, and C. Kratky Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity Biochemistry 48 2009 3370 3377
    • (2009) Biochemistry , vol.48 , pp. 3370-3377
    • Dreveny, I.1    Andryushkova, A.S.2    Glieder, A.3    Gruber, K.4    Kratky, C.5
  • 4
    • 0031051520 scopus 로고    scopus 로고
    • Molecular cloning of acetone cyanohydrin lyase from flax (Linum usitatissimum). Definition of a novel class of hydroxynitrile lyases
    • K. Trummler, and H. Wajant Molecular cloning of acetone cyanohydrin lyase from flax (Linum usitatissimum). Definition of a novel class of hydroxynitrile lyases J. Biol. Chem. 272 1997 4770 4774
    • (1997) J. Biol. Chem. , vol.272 , pp. 4770-4774
    • Trummler, K.1    Wajant, H.2
  • 5
    • 65949118468 scopus 로고    scopus 로고
    • Enantioselective enzyme-catalysed synthesis of cyanohydrins
    • J. Holt, and U. Hanefeld Enantioselective enzyme-catalysed synthesis of cyanohydrins Curr. Org. Synth. 6 2009 15 37
    • (2009) Curr. Org. Synth. , vol.6 , pp. 15-37
    • Holt, J.1    Hanefeld, U.2
  • 6
    • 34547131285 scopus 로고    scopus 로고
    • Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry
    • T. Purkarthofer, W. Skranc, C. Schuster, and H. Griengl Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry Appl. Microbiol. Biotechnol. 76 2007 309 320
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 309-320
    • Purkarthofer, T.1    Skranc, W.2    Schuster, C.3    Griengl, H.4
  • 8
    • 45849118262 scopus 로고    scopus 로고
    • Expression of hydroxynitrile lyase from Manihot esculenta in yeast and its application in (S)-mandelonitrile production using an immobilized enzyme reactor
    • H. Semba, Y. Dobashi, and T. Matsui Expression of hydroxynitrile lyase from Manihot esculenta in yeast and its application in (S)-mandelonitrile production using an immobilized enzyme reactor Biosci. Biotechnol. Biochem. 72 2008 1457 1463
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1457-1463
    • Semba, H.1    Dobashi, Y.2    Matsui, T.3
  • 9
    • 77956938375 scopus 로고    scopus 로고
    • Efficient production of active form recombinant cassava hydroxynitrile lyase using Escherichia coli in low-temperature culture
    • H. Semba, E. Ichige, T. Imanaka, H. Atomi, and H. Aoyagi Efficient production of active form recombinant cassava hydroxynitrile lyase using Escherichia coli in low-temperature culture Methods Mol. Biol. 643 2010 133 144
    • (2010) Methods Mol. Biol. , vol.643 , pp. 133-144
    • Semba, H.1    Ichige, E.2    Imanaka, T.3    Atomi, H.4    Aoyagi, H.5
  • 11
    • 79960321967 scopus 로고    scopus 로고
    • Functional expression of a plant hydroxynitrile lyase in Escherichia coli by directed evolution: Creation and characterization of highly in vivo soluble mutants
    • Y. Asano, M. Dadashipour, M. Yamazaki, N. Doi, and H. Komeda Functional expression of a plant hydroxynitrile lyase in Escherichia coli by directed evolution: creation and characterization of highly in vivo soluble mutants Protein Eng. Des. Sel. 24 2011 607 616
    • (2011) Protein Eng. Des. Sel. , vol.24 , pp. 607-616
    • Asano, Y.1    Dadashipour, M.2    Yamazaki, M.3    Doi, N.4    Komeda, H.5
  • 12
    • 52049088539 scopus 로고    scopus 로고
    • Atomic resolution crystal structures and quantum chemistry meet to reveal subtleties of hydroxynitrile lyase catalysis
    • A. Schmidt, K. Gruber, C. Kratky, and V.S. Lamzin Atomic resolution crystal structures and quantum chemistry meet to reveal subtleties of hydroxynitrile lyase catalysis J. Biol. Chem. 283 2008 21827 21836
    • (2008) J. Biol. Chem. , vol.283 , pp. 21827-21836
    • Schmidt, A.1    Gruber, K.2    Kratky, C.3    Lamzin, V.S.4
  • 13
    • 33947124469 scopus 로고    scopus 로고
    • Structural determinants of the enantioselectivity of the hydroxynitrile lyase from Hevea brasiliensis
    • G. Gartler, C. Kratky, and K. Gruber Structural determinants of the enantioselectivity of the hydroxynitrile lyase from Hevea brasiliensis J. Biotechnol. 129 2007 87 97
    • (2007) J. Biotechnol. , vol.129 , pp. 87-97
    • Gartler, G.1    Kratky, C.2    Gruber, K.3
  • 14
    • 0036136695 scopus 로고    scopus 로고
    • Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta
    • H. Lauble, B. Miehlich, S. Forster, C. Kobler, H. Wajant, and F. Effenberger Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta Protein Sci. 11 2002 65 71
    • (2002) Protein Sci. , vol.11 , pp. 65-71
    • Lauble, H.1    Miehlich, B.2    Forster, S.3    Kobler, C.4    Wajant, H.5    Effenberger, F.6
  • 15
    • 0035128239 scopus 로고    scopus 로고
    • Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: Implications for the mechanism of cyanogenesis
    • H. Lauble, S. Forster, B. Miehlich, H. Wajant, and F. Effenberger Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis Acta Crystallogr. D 57 2001 194 200
    • (2001) Acta Crystallogr. D , vol.57 , pp. 194-200
    • Lauble, H.1    Forster, S.2    Miehlich, B.3    Wajant, H.4    Effenberger, F.5
  • 16
    • 2442485744 scopus 로고    scopus 로고
    • Reaction mechanism of hydroxynitrile lyases of the alpha/beta-hydrolase superfamily - The three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of LYS236
    • K. Gruber, G. Gartler, B. Krammer, H. Schwab, and C. Kratky Reaction mechanism of hydroxynitrile lyases of the alpha/beta-hydrolase superfamily - the three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of LYS236 J. Biol. Chem. 279 2004 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
  • 17
    • 77954935929 scopus 로고    scopus 로고
    • Catalytic mechanism of hydroxynitrile lyase from Hevea brasiliensis: A theoretical investigation
    • F.C. Cui, X.L. Pan, and J.Y. Liu Catalytic mechanism of hydroxynitrile lyase from Hevea brasiliensis: a theoretical investigation J. Phys. Chem. B 114 2010 9622 9628
    • (2010) J. Phys. Chem. B , vol.114 , pp. 9622-9628
    • Cui, F.C.1    Pan, X.L.2    Liu, J.Y.3
  • 18
    • 21044452029 scopus 로고    scopus 로고
    • Inversion of stereoselectivity by applying mutants of the hydroxynitrile lyase from Manihot esculenta
    • H. Buhler, B. Miehlich, and F. Effenberger Inversion of stereoselectivity by applying mutants of the hydroxynitrile lyase from Manihot esculenta Chembiochem 6 2005 711 717
    • (2005) Chembiochem , vol.6 , pp. 711-717
    • Buhler, H.1    Miehlich, B.2    Effenberger, F.3
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Method Enzymol. 276 1997 307 326
    • (1997) Method Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • A. Vagin, and A. Teplyakov MOLREP: an automated program for molecular replacement J. Appl. Crystallogr. 30 1997 1022 1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 21
    • 0037208360 scopus 로고    scopus 로고
    • An overview of the CCP4 project in protein crystallography: An example of a collaborative project
    • M.D. Winn An overview of the CCP4 project in protein crystallography: an example of a collaborative project J. Synchrotron Radiat. 10 2003 23 25
    • (2003) J. Synchrotron Radiat. , vol.10 , pp. 23-25
    • Winn, M.D.1
  • 23
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D 53 1997 240 255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 25
    • 84855757480 scopus 로고    scopus 로고
    • 10, in: C.C.G. Inc. (Ed.)Montreal, QC, Canada
    • Molecular Operating Environment (MOE), 2012.10, in: C.C.G. Inc. (Ed.)Montreal, QC, Canada.
    • (2012) Molecular Operating Environment (MOE)
  • 28
    • 48749148224 scopus 로고
    • Rattle: A "velocity" version of the shake algorithm for molecular dynamics calculations
    • H.C. Andersen Rattle: a "velocity" version of the shake algorithm for molecular dynamics calculations J. Comput. Phys. 52 1983 24 34
    • (1983) J. Comput. Phys. , vol.52 , pp. 24-34
    • Andersen, H.C.1
  • 29
    • 84898650507 scopus 로고    scopus 로고
    • Binding of NAD+ and L-threonine induces stepwise structural and flexibility changes in Cupriavidus necator L-threonine dehydrogenase
    • S. Nakano, S. Okazaki, H. Tokiwa, and Y. Asano Binding of NAD+ and L-threonine induces stepwise structural and flexibility changes in Cupriavidus necator L-threonine dehydrogenase J. Biol. Chem. 289 2014 10445 10454
    • (2014) J. Biol. Chem. , vol.289 , pp. 10445-10454
    • Nakano, S.1    Okazaki, S.2    Tokiwa, H.3    Asano, Y.4
  • 30
    • 35748935079 scopus 로고    scopus 로고
    • Wordom: A program for efficient analysis of molecular dynamics simulations
    • M. Seeber, M. Cecchini, F. Rao, G. Settanni, and A. Caflisch Wordom: a program for efficient analysis of molecular dynamics simulations Bioinformatics 23 2007 2625 2627
    • (2007) Bioinformatics , vol.23 , pp. 2625-2627
    • Seeber, M.1    Cecchini, M.2    Rao, F.3    Settanni, G.4    Caflisch, A.5
  • 33
    • 84865568695 scopus 로고    scopus 로고
    • Hydroxynitrile lyases with alpha/beta-hydrolase fold: Two enzymes with almost identical 3D structures but opposite enantioselectivities and different reaction mechanisms
    • J.N. Andexer, N. Staunig, T. Eggert, C. Kratky, M. Pohl, and K. Gruber Hydroxynitrile lyases with alpha/beta-hydrolase fold: two enzymes with almost identical 3D structures but opposite enantioselectivities and different reaction mechanisms Chembiochem 13 2012 1932 1939
    • (2012) Chembiochem , vol.13 , pp. 1932-1939
    • Andexer, J.N.1    Staunig, N.2    Eggert, T.3    Kratky, C.4    Pohl, M.5    Gruber, K.6
  • 35
    • 0032546782 scopus 로고    scopus 로고
    • Pi-Stacking interactions. Alive and well in proteins
    • G.B. McGaughey, M. Gagne, and A.K. Rappe pi-Stacking interactions. Alive and well in proteins J. Biol. Chem. 273 1998 15458 15463
    • (1998) J. Biol. Chem. , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappe, A.K.3
  • 36
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • N. Tokuriki, and D.S. Tawfik Protein dynamism and evolvability Science 324 2009 203 207
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 37
    • 84907668884 scopus 로고    scopus 로고
    • Increasing the reaction rate of hydroxynitrile lyase from Hevea brasiliensis toward mandelonitrile by copying active site residues from an esterase that accepts aromatic esters
    • J. von Langermann, D.M. Nedrud, and R.J. Kazlauskas Increasing the reaction rate of hydroxynitrile lyase from Hevea brasiliensis toward mandelonitrile by copying active site residues from an esterase that accepts aromatic esters Chembiochem 15 2014 1931 1938
    • (2014) Chembiochem , vol.15 , pp. 1931-1938
    • Von Langermann, J.1    Nedrud, D.M.2    Kazlauskas, R.J.3


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