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Volumn 153, Issue 3-4, 2011, Pages 100-110

S-selective hydroxynitrile lyase from a plant Baliospermum montanum: Molecular characterization of recombinant enzyme

Author keywords

Alanine scanning; Characterization; Homology modeling; Molecular cloning; S selective hydroxynitrile lyase; Substrate specificity

Indexed keywords

ALANINE SCANNING; HOMOLOGY MODELING; HYDROXYNITRILE LYASES; MOLECULAR CLONING; SUBSTRATE SPECIFICITY;

EID: 79955781277     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.02.004     Document Type: Article
Times cited : (37)

References (47)
  • 3
    • 0033524351 scopus 로고    scopus 로고
    • Kinetic studies on the enzyme (S)-hydroxynitrile lyase from Hevea brasiliensis using initial rate methods and progress curve analysis
    • Bauer M., Griengl H., Steiner W. Kinetic studies on the enzyme (S)-hydroxynitrile lyase from Hevea brasiliensis using initial rate methods and progress curve analysis. Biotechnol. Bioeng. 1999, 62:20-29.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 20-29
    • Bauer, M.1    Griengl, H.2    Steiner, W.3
  • 4
    • 0032946807 scopus 로고    scopus 로고
    • Parameters influencing stability and activity of a S-hydroxynitrile lyase from Hevea brasiliensis in two-phase systems
    • Bauer M., Griengl H., Steiner W. Parameters influencing stability and activity of a S-hydroxynitrile lyase from Hevea brasiliensis in two-phase systems. Enzyme Microbiol. Technol. 1999, 24:514-522.
    • (1999) Enzyme Microbiol. Technol. , vol.24 , pp. 514-522
    • Bauer, M.1    Griengl, H.2    Steiner, W.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding
    • Bradford M.M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 51249169259 scopus 로고
    • A simple and efficient method for isolating RNA from pine trees
    • Chang Sh., Puryear J., Cairney J. A simple and efficient method for isolating RNA from pine trees. Plant Mol. Biol. Rep. 1993, 11:113-116.
    • (1993) Plant Mol. Biol. Rep. , vol.11 , pp. 113-116
    • Chang, S.1    Puryear, J.2    Cairney, J.3
  • 7
    • 0030588303 scopus 로고    scopus 로고
    • Properties of alpha-hydroxynitrile lyase from the petiole of cassava (Manihot esculenta Crantz)
    • Chueskul S., Chulavatnatol M. Properties of alpha-hydroxynitrile lyase from the petiole of cassava (Manihot esculenta Crantz). Arch. Biochem. Biophys. 1996, 334:401-405.
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 401-405
    • Chueskul, S.1    Chulavatnatol, M.2
  • 8
    • 84955409681 scopus 로고    scopus 로고
    • Enzymatic synthesis of cyanohydrins
    • Wiley-VCH, Weinheim, K. Drauz, H. Waldmann (Eds.)
    • Fechter M.H., Griengl H. Enzymatic synthesis of cyanohydrins. Enzyme catalysis in organic synthesis 2002, 974-989. Wiley-VCH, Weinheim. K. Drauz, H. Waldmann (Eds.).
    • (2002) Enzyme catalysis in organic synthesis , pp. 974-989
    • Fechter, M.H.1    Griengl, H.2
  • 9
    • 33748630895 scopus 로고    scopus 로고
    • The first recombinant hydroxynitrile lyase and its application in the synthesis of (S)-cyanohydrins
    • Foerster S., Roos J., Effenburger F., Wajant H., Sprauer A. The first recombinant hydroxynitrile lyase and its application in the synthesis of (S)-cyanohydrins. Angew. Chem. Int. Ed. 1996, 35:437-439.
    • (1996) Angew. Chem. Int. Ed. , vol.35 , pp. 437-439
    • Foerster, S.1    Roos, J.2    Effenburger, F.3    Wajant, H.4    Sprauer, A.5
  • 10
    • 4644302352 scopus 로고    scopus 로고
    • The first hydroxynitrile lyase catalysed cyanohydrin formation in ionic liquids
    • Gaisberger R.P., Fechter M.H., Griengl H. The first hydroxynitrile lyase catalysed cyanohydrin formation in ionic liquids. Tetrahedron: Asymmetry 2004, 15:2959-2963.
    • (2004) Tetrahedron: Asymmetry , vol.15 , pp. 2959-2963
    • Gaisberger, R.P.1    Fechter, M.H.2    Griengl, H.3
  • 11
    • 0000140586 scopus 로고    scopus 로고
    • Cyanohydrins in nature and the laboratory: biology, preparations, and synthetic applications
    • Gregory R.J.H. Cyanohydrins in nature and the laboratory: biology, preparations, and synthetic applications. Chem. Rev. 1999, 99:3649-3682.
    • (1999) Chem. Rev. , vol.99 , pp. 3649-3682
    • Gregory, R.J.H.1
  • 12
    • 2442485744 scopus 로고    scopus 로고
    • Reaction mechanism of hydroxynitrile lyases of the α/β-hydrolase superfamily. The 3-D structure of the transient enzyme-substrate complex certifies the crucial role of Lys236
    • Gruber K., Gartler G., Krammer B., Schwab H., Kratky Ch. Reaction mechanism of hydroxynitrile lyases of the α/β-hydrolase superfamily. The 3-D structure of the transient enzyme-substrate complex certifies the crucial role of Lys236. 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
  • 15
    • 0035846964 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry, circular dichroism and SAXS studies of the (S)-hydroxynitrile lyase from Hevea brasiliensis.Biochem
    • Hanefeld U., Stranzl G., Straathof A.J.J., Heijnen J.J., Bergmann A., Mittelbach R., Glatter O., Kratky C. Electrospray ionization mass spectrometry, circular dichroism and SAXS studies of the (S)-hydroxynitrile lyase from Hevea brasiliensis.Biochem. Biophys. Acta 2001, 1544:133-142.
    • (2001) Biophys. Acta , vol.1544 , pp. 133-142
    • Hanefeld, U.1    Stranzl, G.2    Straathof, A.J.J.3    Heijnen, J.J.4    Bergmann, A.5    Mittelbach, R.6    Glatter, O.7    Kratky, C.8
  • 16
    • 0029978870 scopus 로고    scopus 로고
    • Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis: functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue
    • 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: functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue. 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
  • 17
    • 65949118468 scopus 로고    scopus 로고
    • Enantioselective enzyme-catalysed synthesis of cyanohydrins
    • Holt J., Hanefeld U. Enantioselective enzyme-catalysed synthesis of cyanohydrins. Curr. Org. Synth. 2009, 6:15-37.
    • (2009) Curr. Org. Synth. , vol.6 , pp. 15-37
    • Holt, J.1    Hanefeld, U.2
  • 18
    • 31444439996 scopus 로고    scopus 로고
    • Construction of a fully active truncated alternansucrase partially deleted of its carboxy-terminal domain
    • Joucla G., Pizzut S., Monsan P., Remaud-Simeon M. Construction of a fully active truncated alternansucrase partially deleted of its carboxy-terminal domain. FEBS Lett. 2006, 580:763-768.
    • (2006) FEBS Lett. , vol.580 , pp. 763-768
    • Joucla, G.1    Pizzut, S.2    Monsan, P.3    Remaud-Simeon, M.4
  • 19
    • 0030000714 scopus 로고    scopus 로고
    • (R)- and (S)-cyanohydrins using oxynitrilases in whole cells
    • Kiljunen E., Kanerva L.T. (R)- and (S)-cyanohydrins using oxynitrilases in whole cells. Tetrahedron: Asymmetry 1996, 7:1105-1116.
    • (1996) Tetrahedron: Asymmetry , vol.7 , pp. 1105-1116
    • Kiljunen, E.1    Kanerva, L.T.2
  • 20
    • 46449091126 scopus 로고    scopus 로고
    • A novel D-stereo selective amino acid esterase from Brevibacterium iodinum: gene cloning, expression and characterization
    • Komeda H., Asano Y. A novel D-stereo selective amino acid esterase from Brevibacterium iodinum: gene cloning, expression and characterization. Enzyme Microb. Technol. 2008, 43:276-283.
    • (2008) Enzyme Microb. Technol. , vol.43 , pp. 276-283
    • Komeda, H.1    Asano, Y.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0036136695 scopus 로고    scopus 로고
    • Structural determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta
    • Lauble H., Miehlich B., Förster S., Kolber Ch., Wajant H., Effenberger F. Structural determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta. Protein Sci. 2002, 11:65-71.
    • (2002) Protein Sci. , vol.11 , pp. 65-71
    • Lauble, H.1    Miehlich, B.2    Förster, S.3    Kolber, C.4    Wajant, H.5    Effenberger, F.6
  • 24
    • 0037044299 scopus 로고    scopus 로고
    • Crystal structure of hydroxynitrile lyase from Sorghum bicolor in complex with the inhibitor benzoic acid: a novel cyanogenic enzyme
    • Lauble H., Miehlich B., Förster S., Wajant H., Effenberger F. Crystal structure of hydroxynitrile lyase from Sorghum bicolor in complex with the inhibitor benzoic acid: a novel cyanogenic enzyme. Biochemistry 2002, 41:12043-12050.
    • (2002) Biochemistry , vol.41 , pp. 12043-12050
    • Lauble, H.1    Miehlich, B.2    Förster, S.3    Wajant, H.4    Effenberger, F.5
  • 25
    • 0028795264 scopus 로고
    • Cyanogenesis in cassava (Manihot esculenta Crantz)
    • McMahon J., White W., Sayre R.T. Cyanogenesis in cassava (Manihot esculenta Crantz). J. Exp. Bot. 1995, 46:731-741.
    • (1995) J. Exp. Bot. , vol.46 , pp. 731-741
    • McMahon, J.1    White, W.2    Sayre, R.T.3
  • 26
    • 26844476418 scopus 로고    scopus 로고
    • A new (R)-hydroxynitrile lyase from Prunus mume: asymmetric synthesis of cyanohydrins
    • Nanda S., Kato Y., Asano Y. A new (R)-hydroxynitrile lyase from Prunus mume: asymmetric synthesis of cyanohydrins. Tetrahedron 2005, 61:10908-10916.
    • (2005) Tetrahedron , vol.61 , pp. 10908-10916
    • Nanda, S.1    Kato, Y.2    Asano, Y.3
  • 27
    • 33645752823 scopus 로고    scopus 로고
    • PmHNL-catalyzed synthesis of (R)-cyanohydrins derived from aliphatic aldehydes
    • Nanda S., Kato Y., Asano Y. PmHNL-catalyzed synthesis of (R)-cyanohydrins derived from aliphatic aldehydes. Tetrahedron: Asymmetry 2006, 17:735-741.
    • (2006) Tetrahedron: Asymmetry , vol.17 , pp. 735-741
    • Nanda, S.1    Kato, Y.2    Asano, Y.3
  • 28
    • 0032784276 scopus 로고    scopus 로고
    • α/β hydrolase fold enzymes: the family keeps growing
    • Nardini M., Dijkstra B.W. α/β hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol. 1999, 9:732-737.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 29
    • 0001676723 scopus 로고
    • Enzyme-catalyzed synthesis of (S)-cyanohydrins
    • Niedermyer U., Kula M.R. Enzyme-catalyzed synthesis of (S)-cyanohydrins. Angew. Chem. 1990, 102:423-425.
    • (1990) Angew. Chem. , vol.102 , pp. 423-425
    • Niedermyer, U.1    Kula, M.R.2
  • 30
    • 34547131285 scopus 로고    scopus 로고
    • Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry
    • Purkarthofer T., Skranc W., Schuster Ch., Griengl H. Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry. Appl. Microbiol. Biotechnol. 2007, 76:309-320.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 309-320
    • Purkarthofer, T.1    Skranc, W.2    Schuster, C.3    Griengl, H.4
  • 33
    • 0342409343 scopus 로고    scopus 로고
    • Optimized methods for the preparation of (S)-2-hydroxy-2-phenylpropanenitrile exploiting R-selective oxynitrilase in almond meal
    • Rotčenkovs G., Kanerva L.T. Optimized methods for the preparation of (S)-2-hydroxy-2-phenylpropanenitrile exploiting R-selective oxynitrilase in almond meal. J. Mol. Catal. B: Enzym. 2000, 11:37-43.
    • (2000) J. Mol. Catal. B: Enzym. , vol.11 , pp. 37-43
    • Rotčenkovs, G.1    Kanerva, L.T.2
  • 36
  • 37
    • 0030053212 scopus 로고    scopus 로고
    • Preparation of optically active cyanohydrins using the S-selective hydroxynitrile lyase from Hevea brasiliensis
    • Schmidt M., Hervé S., Klempier N., Griengl H. Preparation of optically active cyanohydrins using the S-selective hydroxynitrile lyase from Hevea brasiliensis. Tetrahedron 1996, 52:7833-7840.
    • (1996) Tetrahedron , vol.52 , pp. 7833-7840
    • Schmidt, M.1    Hervé, S.2    Klempier, N.3    Griengl, H.4
  • 39
    • 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
    • Semba H., Dobashi Y., Matsui T. Expression of hydroxynitrile lyase from Manihot esculenta in yeast and its application in (S)-mandelonitrile production using an immobilized enzyme reactor. Biosci. Biotechnol. Biochem. 2008, 72:1457-1463.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1457-1463
    • Semba, H.1    Dobashi, Y.2    Matsui, T.3
  • 41
    • 0031051520 scopus 로고    scopus 로고
    • Molecular cloning of acetone cyanohydrin lyase from Flax (Linum usitatissimum)
    • Trummler K., Wajant H. Molecular cloning of acetone cyanohydrin lyase from Flax (Linum usitatissimum). J. Biol. Chem. 1997, 272:4770-4774.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4770-4774
    • Trummler, K.1    Wajant, H.2
  • 42
    • 45949097361 scopus 로고    scopus 로고
    • Purification and characterization of a novel (R)-hydroxynitrile lyase from Eribotrya japonica
    • Ueatrongchit T., Kayo A., Komeda H., Asano Y., H-Kittikun A. Purification and characterization of a novel (R)-hydroxynitrile lyase from Eribotrya japonica. Biosci. Biotechnol. Biochem. 2008, 72:1513-1522.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1513-1522
    • Ueatrongchit, T.1    Kayo, A.2    Komeda, H.3    Asano, Y.4    H-Kittikun, A.5
  • 43
    • 58249087170 scopus 로고    scopus 로고
    • Parameters influencing asymmetric synthesis of (R)-mandelonitrile by a novel (R)-hydroxynitrile lyase from Eriobotrya japonica
    • Ueatrongchit T., Komeda H., Asano Y., H-Kittikun A. Parameters influencing asymmetric synthesis of (R)-mandelonitrile by a novel (R)-hydroxynitrile lyase from Eriobotrya japonica. J. Mol. Catal. B: Enzym. 2009, 56:208-214.
    • (2009) J. Mol. Catal. B: Enzym. , vol.56 , pp. 208-214
    • Ueatrongchit, T.1    Komeda, H.2    Asano, Y.3    H-Kittikun, A.4
  • 44
    • 0029955020 scopus 로고    scopus 로고
    • Identification of potential active-site residues of the hydroxynitrile lyase from Manihot esculenta by site-directed mutagenesis
    • Wajant H., Pfizenmaier K. Identification of potential active-site residues of the hydroxynitrile lyase from Manihot esculenta by site-directed mutagenesis. J. Biol. Chem. 1996, 271:25830-25834.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25830-25834
    • Wajant, H.1    Pfizenmaier, K.2
  • 45
    • 0000532033 scopus 로고
    • Hydroxynitrile lyase from Sorghum bicolor: a glycoprotein heterotetramer
    • Wajant H., Mundry K.W. Hydroxynitrile lyase from Sorghum bicolor: a glycoprotein heterotetramer. Plant Sci. 1993, 89:127-133.
    • (1993) Plant Sci. , vol.89 , pp. 127-133
    • Wajant, H.1    Mundry, K.W.2
  • 47
    • 0032852375 scopus 로고    scopus 로고
    • Three-dimensional structure of enzyme-substrate complex of HNL from Hevea brasiliensis
    • Zuegg J., Gruber K., Gugganig M., Wagner U.G., Kratky C. Three-dimensional structure of enzyme-substrate complex of HNL from Hevea brasiliensis. Protein Sci. 1999, 8:1990-2000.
    • (1999) Protein Sci. , vol.8 , pp. 1990-2000
    • Zuegg, J.1    Gruber, K.2    Gugganig, M.3    Wagner, U.G.4    Kratky, C.5


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