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Volumn 18, Issue 6, 2000, Pages 252-256

The synthesis of chiral cyanohydrins by oxynitrilases

Author keywords

[No Author keywords available]

Indexed keywords

AGRICULTURAL CHEMICAL; ALDEHYDE; CYANOHYDRIN; INDUSTRIAL CHEMICAL; KETONE; NITRILASE; ORGANIC SOLVENT; OXYNITRILASE; UNCLASSIFIED DRUG;

EID: 0034213036     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-7799(00)01452-9     Document Type: Review
Times cited : (115)

References (57)
  • 1
    • 0001516109 scopus 로고
    • Durch Enzyme bewirkte asymmetrische Synthesen
    • Rosenthaler L. Durch Enzyme bewirkte asymmetrische Synthesen. Biochem. Z. 14:1908;238-253.
    • (1908) Biochem. Z. , vol.14 , pp. 238-253
    • Rosenthaler, L.1
  • 3
    • 0342483001 scopus 로고
    • Über die synthetisierende Wirkung des Emulsin
    • Albers H., Hamann K. Über die synthetisierende Wirkung des Emulsin. Biochem. Z. 255:1932;44-65.
    • (1932) Biochem. Z. , vol.255 , pp. 44-65
    • Albers, H.1    Hamann, K.2
  • 4
    • 0343788128 scopus 로고
    • Über die Kinetik der durch Emulsin beschleunigten Synthese des (+)-Mandelsäurenitrils
    • Albers H., Hamann K. Über die Kinetik der durch Emulsin beschleunigten Synthese des (+)-Mandelsäurenitrils. Biochem. Z. 269:1934;14-25.
    • (1934) Biochem. Z. , vol.269 , pp. 14-25
    • Albers, H.1    Hamann, K.2
  • 5
    • 73649184344 scopus 로고
    • Cyanohydrin synthesis: Purification and properties of oxynitrilase of bitter almonds
    • Becker W.et al. Cyanohydrin synthesis: purification and properties of oxynitrilase of bitter almonds. Biochem. Z. 337:1963;156-166.
    • (1963) Biochem. Z. , vol.337 , pp. 156-166
    • Becker, W.1
  • 6
    • 0001509373 scopus 로고
    • Über das Flavinenzym D-Oxynitrilase
    • Becker W., Pfeil E. Über das Flavinenzym D-Oxynitrilase. Biochem. Z. 346:1966;301-321.
    • (1966) Biochem. Z. , vol.346 , pp. 301-321
    • Becker, W.1    Pfeil, E.2
  • 7
    • 85027475595 scopus 로고
    • Stereospecific synthesis of D-hydroxy nitriles and optically active ethanolamines
    • Becker W.et al. Stereospecific synthesis of D-hydroxy nitriles and optically active ethanolamines. Angew. Chem., Int. Ed. Engl. 4:1965;1079.
    • (1965) Angew. Chem., Int. Ed. Engl. , vol.4 , pp. 1079
    • Becker, W.1
  • 8
    • 0000018247 scopus 로고
    • Continuous synthesis of optically active α-hydroxynitriles
    • Becker W., Pfeil E. Continuous synthesis of optically active α-hydroxynitriles. J. Am. Chem. Soc. 88:1966;4299-4300.
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 4299-4300
    • Becker, W.1    Pfeil, E.2
  • 9
    • 84985534669 scopus 로고
    • Enzyme-catalysed cyanohydrin preparation in organic solvents
    • Effenberger F.et al. Enzyme-catalysed cyanohydrin preparation in organic solvents. Angew. Chem., Int. Ed. Engl. 26:1987;458-460.
    • (1987) Angew. Chem., Int. Ed. Engl. , vol.26 , pp. 458-460
    • Effenberger, F.1
  • 10
    • 0025637249 scopus 로고
    • Engineering aspects of enzyme engineering: Continuous asymmetric carbon-carbon bond formation in an enzyme-membrane reactor
    • Kragl U.et al. Engineering aspects of enzyme engineering: continuous asymmetric carbon-carbon bond formation in an enzyme-membrane reactor. Ann. New York Acad. Sci. 613:1990;167-175.
    • (1990) Ann. New York Acad. Sci. , vol.613 , pp. 167-175
    • Kragl, U.1
  • 12
    • 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.et al. 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. 271:1996;5884-5891.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5884-5891
    • Hasslacher, M.1
  • 13
    • 33748630895 scopus 로고    scopus 로고
    • The first recombinant hydroxynitrile lyase and its application in the synthesis of (S)-cyanohydrins
    • Förster S.et al. The first recombinant hydroxynitrile lyase and its application in the synthesis of (S)-cyanohydrins. Angew. Chem., Int. Ed. Engl. 35:1996;437-438.
    • (1996) Angew. Chem., Int. Ed. Engl. , vol.35 , pp. 437-438
    • Förster, S.1
  • 14
    • 0030441331 scopus 로고    scopus 로고
    • Hydroxynitrile lyases: Functions and properties
    • Hickel A.et al. Hydroxynitrile lyases: functions and properties. Physiol. Plant. 98:1996;891-898.
    • (1996) Physiol. Plant. , vol.98 , pp. 891-898
    • Hickel, A.1
  • 15
    • 0000234676 scopus 로고    scopus 로고
    • Oxynitrilases: From cyanogenesis to asymmetric synthesis
    • Schmidt M., Griengl H. Oxynitrilases: from cyanogenesis to asymmetric synthesis. Top. Curr. Chem. 200:1999;193-226.
    • (1999) Top. Curr. Chem. , vol.200 , pp. 193-226
    • Schmidt, M.1    Griengl, H.2
  • 18
    • 0018787705 scopus 로고
    • Mechanism of catalysis by the flavoenzyme oxynitrilase
    • Jorns M.S. Mechanism of catalysis by the flavoenzyme oxynitrilase. J. Biol. Chem. 254:1979;12145-12152.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12145-12152
    • Jorns, M.S.1
  • 19
    • 0030975258 scopus 로고    scopus 로고
    • Hydroxynitrile lyase from Hevea brasiliensis: Molecular characterization and mechanism of enzyme catalysis
    • Hasslacher M.et al. Hydroxynitrile lyase from Hevea brasiliensis: molecular characterization and mechanism of enzyme catalysis. Proteins Struct. Funct. Genet. 27:1997;438-449.
    • (1997) Proteins Struct. Funct. Genet. , vol.27 , pp. 438-449
    • Hasslacher, M.1
  • 20
    • 0025254459 scopus 로고
    • Synthesis of optically active silyl protected cyanohydrins
    • Brussee J.et al. Synthesis of optically active silyl protected cyanohydrins. Tetrahedron. 46:1990;979-986.
    • (1990) Tetrahedron , vol.46 , pp. 979-986
    • Brussee, J.1
  • 21
    • 0026707341 scopus 로고
    • Enzyme-catalysed synthesis of optically active aliphatic cyanohydrins
    • Huuhtanen T.T., Kanerva L.T. Enzyme-catalysed synthesis of optically active aliphatic cyanohydrins. Tetrahedron Asymmetry. 3:1992;1223-1226.
    • (1992) Tetrahedron Asymmetry , vol.3 , pp. 1223-1226
    • Huuhtanen, T.T.1    Kanerva, L.T.2
  • 22
    • 0025760153 scopus 로고
    • Enzyme-catalysed synthesis of (R)-ketone cyanohydrins and their hydrolysis to (R)-α-hydroxy-α-methyl carboxylic acids
    • Effenberger F.et al. Enzyme-catalysed synthesis of (R)-ketone cyanohydrins and their hydrolysis to (R)-α-hydroxy-α-methyl carboxylic acids. Tetrahedron Lett. 32:1991;2605-2608.
    • (1991) Tetrahedron Lett. , vol.32 , pp. 2605-2608
    • Effenberger, F.1
  • 23
    • 84981988615 scopus 로고
    • Improved purification of an (R)-oxynitrilase from Linum usitatissimum (flax) and investigation of the substrate range
    • Albrecht J.et al. Improved purification of an (R)-oxynitrilase from Linum usitatissimum (flax) and investigation of the substrate range. Biotechnol. Appl. Biochem. 17:1993;191-203.
    • (1993) Biotechnol. Appl. Biochem. , vol.17 , pp. 191-203
    • Albrecht, J.1
  • 24
    • 0031041041 scopus 로고    scopus 로고
    • Stereoselective synthesis of thienyl and furyl analogues of ephedrine
    • Effenberger F., Eichhorn J. Stereoselective synthesis of thienyl and furyl analogues of ephedrine. Tetrahedron Asymmetry. 8:1997;469-476.
    • (1997) Tetrahedron Asymmetry , vol.8 , pp. 469-476
    • Effenberger, F.1    Eichhorn, J.2
  • 25
    • 0030053212 scopus 로고    scopus 로고
    • Preparation of optically active cyanohydrins using the (S)-hydroxynitrile lyase from Hevea brasiliensis
    • Schmidt M.et al. Preparation of optically active cyanohydrins using the (S)-hydroxynitrile lyase from Hevea brasiliensis. Tetrahedron. 52:1996;7833-7840.
    • (1996) Tetrahedron , vol.52 , pp. 7833-7840
    • Schmidt, M.1
  • 26
    • 0032569785 scopus 로고    scopus 로고
    • Enzyme catalysed formation of (S)-cyanohydrins derived from aldehydes and ketones in a biphasic solvent system
    • Griengl H.et al. Enzyme catalysed formation of (S)-cyanohydrins derived from aldehydes and ketones in a biphasic solvent system. Tetrahedron. 54:1998;14477-14486.
    • (1998) Tetrahedron , vol.54 , pp. 14477-14486
    • Griengl, H.1
  • 27
    • 0030586027 scopus 로고    scopus 로고
    • Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis
    • Wagner U.G.et al. Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Structure. 4:1996;811-822.
    • (1996) Structure , vol.4 , pp. 811-822
    • Wagner, U.G.1
  • 28
    • 0028247273 scopus 로고
    • Purification, characterization, and cloning of α-hydroxynitrile lyase from cassava (Manihot esculenta Crantz)
    • Hughes J.et al. Purification, characterization, and cloning of α-hydroxynitrile lyase from cassava (Manihot esculenta Crantz). Arch. Biochem. Biophys. 311:1994;496-502.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 496-502
    • Hughes, J.1
  • 29
    • 0031553672 scopus 로고    scopus 로고
    • Production and characterization of a plant α-hydroxynitrile lyase in Escherichia coli
    • Hughes J.et al. Production and characterization of a plant α-hydroxynitrile lyase in Escherichia coli. Biotechnol. Bioeng. 53:1997;332-338.
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 332-338
    • Hughes, J.1
  • 30
    • 0031051520 scopus 로고    scopus 로고
    • Molecular cloning of acetone cyanohydrine lyase from flax (Linum usitatissimum): Definition of a novel class of hydroxynitrile lyases
    • Trummler K., Wajant H. Molecular cloning of acetone cyanohydrine 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
  • 31
    • 0033545520 scopus 로고    scopus 로고
    • Cloning and expression of (R)-hydroxynitrile lyase from Linum usitatissimum (flax)
    • Breithaupt H.et al. Cloning and expression of (R)-hydroxynitrile lyase from Linum usitatissimum (flax). J. Mol. Catal. B: Enzymatic. 6:1999;315-332.
    • (1999) J. Mol. Catal. B: Enzymatic , vol.6 , pp. 315-332
    • Breithaupt, H.1
  • 32
    • 0342471685 scopus 로고
    • Purification and protein characterization of hydroxynitrile lyases from sorghum and almond
    • Jansen J.et al. Purification and protein characterization of hydroxynitrile lyases from sorghum and almond. Biotechnol. Appl. Biochem. 15:1992;90-99.
    • (1992) Biotechnol. Appl. Biochem. , vol.15 , pp. 90-99
    • Jansen, J.1
  • 33
    • 84987189245 scopus 로고
    • Hydroxynitrile lyases from almond and sorghum as biocatalysts
    • Smitskamp-Wilms E.et al. Hydroxynitrile lyases from almond and sorghum as biocatalysts. Rev. Trav. Chim. Pays-Bas. 110:1991;208-215.
    • (1991) Rev. Trav. Chim. Pays-Bas , vol.110 , pp. 208-215
    • Smitskamp-Wilms, E.1
  • 34
    • 0028519028 scopus 로고
    • Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.): Homologies to serine carboxypeptidases
    • Wajant H.et al. Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.): homologies to serine carboxypeptidases. Plant Mol. Biol. 26:1994;735-746.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 735-746
    • Wajant, H.1
  • 35
    • 0025143773 scopus 로고
    • Extraction of proteins from biological raw material using aqueous polyethylene-glycol-citrate phase systems
    • Vernan J., Kula M.R. Extraction of proteins from biological raw material using aqueous polyethylene-glycol-citrate phase systems. Biotechnol. Appl. Biochem. 12:1990;397-404.
    • (1990) Biotechnol. Appl. Biochem. , vol.12 , pp. 397-404
    • Vernan, J.1    Kula, M.R.2
  • 36
    • 0025915417 scopus 로고
    • Synthesis of optically active cyanohydrins using almond meal
    • Zandbergen P.et al. Synthesis of optically active cyanohydrins using almond meal. Synth. Commun. 21:1991;1387-1391.
    • (1991) Synth. Commun. , vol.21 , pp. 1387-1391
    • Zandbergen, P.1
  • 37
    • 0030952277 scopus 로고    scopus 로고
    • Novel (R)-oxynitrilase sources for the synthesis of (R)-cyanohydrins in diisopropyl ether
    • Kiljunen E., Kanerva L.T. Novel (R)-oxynitrilase sources for the synthesis of (R)-cyanohydrins in diisopropyl ether. Tetrahedron Asymmetry. 8:1997;1225-1234.
    • (1997) Tetrahedron Asymmetry , vol.8 , pp. 1225-1234
    • Kiljunen, E.1    Kanerva, L.T.2
  • 38
    • 0032424214 scopus 로고    scopus 로고
    • New sources of (R)-oxynitrilase: Capulin (Prunus capuli) and mamey (Mammea Americana)
    • Solis A.et al. New sources of (R)-oxynitrilase: capulin (Prunus capuli) and mamey (Mammea Americana). Biotechnol. Lett. 20:1998;1183-1185.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 1183-1185
    • Solis, A.1
  • 39
    • 0032529605 scopus 로고    scopus 로고
    • Genomic organization and structure of α-hydroxynitrile lyase in cassava (Manihot esculenta Crantz)
    • Hughes J.et al. Genomic organization and structure of α-hydroxynitrile lyase in cassava (Manihot esculenta Crantz). Arch. Biochem. Biophys. 356:1998;107-116.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 107-116
    • Hughes, J.1
  • 40
    • 0029158010 scopus 로고
    • Characterization of a rice gene induced by Pseudomonas syringae pv. syringae: Requirement for the bacterial lemA gene function
    • Reimmann C.et al. Characterization of a rice gene induced by Pseudomonas syringae pv. syringae: requirement for the bacterial lemA gene function. Physiol. Mol. Plant Pathol. 46:1995;71-81.
    • (1995) Physiol. Mol. Plant Pathol. , vol.46 , pp. 71-81
    • Reimmann, C.1
  • 41
    • 0032523910 scopus 로고    scopus 로고
    • The defense-related rice gene pir7b encodes an α/β hydrolase fold protein exhibiting esterase activity towards naphthol AS esters
    • Wäspi U.et al. The defense-related rice gene pir7b encodes an α/β hydrolase fold protein exhibiting esterase activity towards naphthol AS esters. Eur. J. Biochem. 254:1998;32-37.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 32-37
    • Wäspi, U.1
  • 42
    • 0026540411 scopus 로고
    • The α/β hydrolase fold
    • Ollis D.I.et al. The α/β hydrolase fold. Protein Eng. 5:1992;197-211.
    • (1992) Protein Eng. , vol.5 , pp. 197-211
    • Ollis, D.I.1
  • 43
    • 0031259717 scopus 로고    scopus 로고
    • High level intracellular expression of hydroxynitrile lyase from the tropical rubber tree Hevea brasiliensis in microbial host
    • 11
    • Hasslacher M.et al. High level intracellular expression of hydroxynitrile lyase from the tropical rubber tree Hevea brasiliensis in microbial host. Protein Expres. Purif. 11 61-71:1997.
    • (1997) Protein Expres. Purif. , vol.6171
    • Hasslacher, M.1
  • 44
    • 0030771126 scopus 로고    scopus 로고
    • The PROSITE database, its status in 1997
    • Bairoch A.et al. The PROSITE database, its status in 1997. Nucleic Acids Res. 25:1997;217-221.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 217-221
    • Bairoch, A.1
  • 45
    • 15444377148 scopus 로고
    • Yeast systems for the commercial production of heterologous proteins
    • Buckholz R.G., Gleeson M.A.G. Yeast systems for the commercial production of heterologous proteins. Biotechnology. 9:1991;1067-1072.
    • (1991) Biotechnology , vol.9 , pp. 1067-1072
    • Buckholz, R.G.1    Gleeson, M.A.G.2
  • 46
    • 0031869393 scopus 로고    scopus 로고
    • Chromosomal DNA patterns and gene stability of Pichia pastoris
    • Ohi H.et al. Chromosomal DNA patterns and gene stability of Pichia pastoris. Yeast. 14:1998;895-902.
    • (1998) Yeast , vol.14 , pp. 895-902
    • Ohi, H.1
  • 47
    • 0001176770 scopus 로고
    • Electrophilic amination of acyl anion equivalents: Mild oxidation of aldehyes to amides via O-(trimethylsilyl)- aldehyde cyanohydrin anions
    • Boche G.et al. Electrophilic amination of acyl anion equivalents: mild oxidation of aldehyes to amides via O-(trimethylsilyl)- aldehyde cyanohydrin anions. Tetrahedron Lett. 23:1982;3255-3256.
    • (1982) Tetrahedron Lett. , vol.23 , pp. 3255-3256
    • Boche, G.1
  • 48
    • 0029955020 scopus 로고    scopus 로고
    • Identification of potential active-site residues in the hydroxynitrile lyase from Manihot esculenta by site-directed mutagenesis
    • Wajant H., Pfizenmaier K. Identification of potential active-site residues in the hydroxynitrile lyase from Manihot esculenta by site-directed mutagenesis. J. Biol. Chem. 271:1996;25830-25834.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25830-25834
    • Wajant, H.1    Pfizenmaier, K.2
  • 49
    • 0032852375 scopus 로고    scopus 로고
    • 3D structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis
    • Zuegg J.et al. 3D structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis. Protein Sci. 8:1999;1990-2000.
    • (1999) Protein Sci. , vol.8 , pp. 1990-2000
    • Zuegg, J.1
  • 50
    • 0025700661 scopus 로고
    • Formation of carbon-carbon bonds by mandelonitrile lyase in organic solvents
    • Whetje E.et al. Formation of carbon-carbon bonds by mandelonitrile lyase in organic solvents. Biotechnol. Bioeng. 36:1990;39-46.
    • (1990) Biotechnol. Bioeng. , vol.36 , pp. 39-46
    • Whetje, E.1
  • 51
    • 0033180037 scopus 로고    scopus 로고
    • Hydroxynitrile-lyase-catalysed synthesis of cyanohydrins in organic solvents: Parameters influencing activity and enantiospecificity
    • Costes D.et al. Hydroxynitrile-lyase-catalysed synthesis of cyanohydrins in organic solvents: parameters influencing activity and enantiospecificity. Enzyme Microb. Technol. 25:1999;384-391.
    • (1999) Enzyme Microb. Technol. , vol.25 , pp. 384-391
    • Costes, D.1
  • 52
    • 0032946807 scopus 로고    scopus 로고
    • Parameters influencing stability and activity of S-hydroxynitrile lyase from Hevea brasiliensis in two-phase systems
    • Bauer M.et al. Parameters influencing stability and activity of S-hydroxynitrile lyase from Hevea brasiliensis in two-phase systems. Enzyme Microb. Technol. 24:1999;514-522.
    • (1999) Enzyme Microb. Technol. , vol.24 , pp. 514-522
    • Bauer, M.1
  • 53
    • 0028836960 scopus 로고
    • Synthesis of optically active cyanohydrins using R-oxynitrilase in a liquid-liquid biphasic system
    • Loos W.T.et al. Synthesis of optically active cyanohydrins using R-oxynitrilase in a liquid-liquid biphasic system. Biocatal. Biotransform. 12:1995;255-266.
    • (1995) Biocatal. Biotransform. , vol.12 , pp. 255-266
    • Loos, W.T.1
  • 54
    • 0000446906 scopus 로고
    • Bioorganic synthesis of optically active cyanohydrins and acyloins
    • Brussee J.et al. Bioorganic synthesis of optically active cyanohydrins and acyloins. Tetrahedron Lett. 29:1988;4485-4488.
    • (1988) Tetrahedron Lett. , vol.29 , pp. 4485-4488
    • Brussee, J.1
  • 55
    • 84989568771 scopus 로고
    • A convenient route to (R)-α-hydroxy carboxylic acids and (2R)-1-amino-2-alkanols from (R)-cyanohydrins
    • Ziegler T.et al. A convenient route to (R)-α-hydroxy carboxylic acids and (2R)-1-amino-2-alkanols from (R)-cyanohydrins. Synthesis. 1990;575-578.
    • (1990) Synthesis , pp. 575-578
    • Ziegler, T.1
  • 56
    • 21644489778 scopus 로고
    • Preparation of chiral cyanohydrins by an oxynitrilase-mediated transcyanation
    • Ognyanov V.I.et al. Preparation of chiral cyanohydrins by an oxynitrilase-mediated transcyanation. J. Am. Chem. Soc. 113:1991;6992-6996.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6992-6996
    • Ognyanov, V.I.1
  • 57
    • 0343341144 scopus 로고    scopus 로고
    • Preparation of optically active cyanohydrins using oxynitrilase from almond meal
    • S.M. Roberts. Wiley
    • Zandbergen P.et al. Preparation of optically active cyanohydrins using oxynitrilase from almond meal. Roberts S.M. Preparative Biotransformations. 1997;1-6 Wiley.
    • (1997) Preparative Biotransformations , pp. 1-6
    • Zandbergen, P.1


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