메뉴 건너뛰기




Volumn 98, Issue 4, 1996, Pages 891-898

Hydroxynitrile lyases: Functions and properties

Author keywords

Biochemical properties; Enzyme mechanism; Function; Hydroxynitrile lyase; Industrial application

Indexed keywords

EUPHORBIA; EUPHORBIACEAE; LINACEAE; MAGNOLIOPHYTA; OLACACEAE; POACEAE; ROSACEAE;

EID: 0030441331     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-3054.1996.tb06700.x     Document Type: Article
Times cited : (100)

References (63)
  • 1
    • 84981988615 scopus 로고
    • Improved purification of an (R)-oxynitrilase from Linum usitatissimum (flax) and investigation of the substrate range
    • Albrecht, J., Jansen, I. & Kula, M.-R. 1993. Improved purification of an (R)-oxynitrilase from Linum usitatissimum (flax) and investigation of the substrate range. - Biotechnol. Appl. Biochem. 17: 191-203.
    • (1993) Biotechnol. Appl. Biochem. , vol.17 , pp. 191-203
    • Albrecht, J.1    Jansen, I.2    Kula, M.-R.3
  • 2
    • 0014815902 scopus 로고
    • Auftrennung und Charakterisierung der Isoenzyme von D-Hydroxynitril-Lyase (D-Oxynitrilase) aus Mandeln
    • Aschoff, H.-J. & Pfeil, E. 1970. Auftrennung und Charakterisierung der Isoenzyme von D-Hydroxynitril-Lyase (D-Oxynitrilase) aus Mandeln. - Z. Physiol. Chem. 351: 818-826.
    • (1970) Z. Physiol. Chem. , vol.351 , pp. 818-826
    • Aschoff, H.-J.1    Pfeil, E.2
  • 3
    • 0001509373 scopus 로고
    • Über das Flavinenzym D-Oxynitrilase
    • Becker, W. & Pfeil, E. 1966. Über das Flavinenzym D-Oxynitrilase. - Biochem. Z. 346: 301-321.
    • (1966) Biochem. Z. , vol.346 , pp. 301-321
    • Becker, W.1    Pfeil, E.2
  • 4
    • 0142173061 scopus 로고
    • Zur Kenntnis der Cyanhydrinsynthese II
    • _, Benthin, U., Eschenhof, E. & Pfeil, E. 1963. Zur Kenntnis der Cyanhydrinsynthese II. - Biochem. Z. 337: 156-166.
    • (1963) Biochem. Z. , vol.337 , pp. 156-166
    • Benthin, U.1    Eschenhof, E.2    Pfeil, E.3
  • 5
    • 0009421603 scopus 로고
    • Metabolism of aromatic compounds in higher plants
    • Bové, C. & Conn, E. E. 1961. Metabolism of aromatic compounds in higher plants. - J. Biol. Chem. 236: 207-210.
    • (1961) J. Biol. Chem. , vol.236 , pp. 207-210
    • Bové, C.1    Conn, E.E.2
  • 6
    • 0027131001 scopus 로고
    • Cloning of cDNA of Prunus serotina (R)-(+)-mandelonitrile lyase and identification of a putative FAD-binding site
    • Cheng, I.-P. & Poulton, J. E. 1993. Cloning of cDNA of Prunus serotina (R)-(+)-mandelonitrile lyase and identification of a putative FAD-binding site. - Plant Cell Physiol. 34: 1139-1143.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 1139-1143
    • Cheng, I.-P.1    Poulton, J.E.2
  • 7
    • 0004149428 scopus 로고
    • The biochemistry of plants: A comprehensive treatise
    • P. K. Stumpf and E. E. Conn, eds, Academic Press, New York, NY. ISBN 0-12-675407-1
    • Conn, E. E. 1981. The biochemistry of plants: A comprehensive treatise. - In Secondary Plant Products, Vol. 7 (P. K. Stumpf and E. E. Conn, eds), pp. 479-500. Academic Press, New York, NY. ISBN 0-12-675407-1.
    • (1981) Secondary Plant Products , vol.7 , pp. 479-500
    • Conn, E.E.1
  • 8
    • 0000710861 scopus 로고
    • Synthese und Reaktionen optisch aktiver Cyanhydrine
    • Effenberger, F. 1994. Synthese und Reaktionen optisch aktiver Cyanhydrine. - Angew. Chem. 106: 1609-1619.
    • (1994) Angew. Chem. , vol.106 , pp. 1609-1619
    • Effenberger, F.1
  • 9
    • 0010315131 scopus 로고
    • Enzymkatalysierte Cyanhydrin-Synthese in organischen Lösungsmitteln
    • _, Ziegler, T. & Förster, S. 1987. Enzymkatalysierte Cyanhydrin-Synthese in organischen Lösungsmitteln. - Angew. Chem. 99: 491-192.
    • (1987) Angew. Chem. , vol.99 , pp. 491-1192
    • Ziegler, T.1    Förster, S.2
  • 10
    • 0025034596 scopus 로고
    • Enzyme-catalyzed synthesis of (S)-cyanohydrins and subsequent hydrolysis to (S)-a-hydroxy-carboxylic acids
    • _, Hörsch, B., Förster, S. & Ziegler, T. 1990. Enzyme-catalyzed synthesis of (S)-cyanohydrins and subsequent hydrolysis to (S)-a-hydroxy-carboxylic acids. - Tetrahedron Lett. 3: 1249-1252.
    • (1990) Tetrahedron Lett. , vol.3 , pp. 1249-1252
    • Hörsch, B.1    Förster, S.2    Ziegler, T.3
  • 11
    • 0343552862 scopus 로고    scopus 로고
    • Über die erste rekombinante Hydroxynitril-Lyase und ihre Anwendungen in der Synthese von (S)-Cyanhydrinen
    • Förster, S., Roos, J., Effenberger, F., Wajant, H. & Sprauer, A. 1996. Über die erste rekombinante Hydroxynitril-Lyase und ihre Anwendungen in der Synthese von (S)-Cyanhydrinen. - Angew. Chem. 108: 493-494.
    • (1996) Angew. Chem. , vol.108 , pp. 493-494
    • Förster, S.1    Roos, J.2    Effenberger, F.3    Wajant, H.4    Sprauer, A.5
  • 12
    • 0016651075 scopus 로고
    • Eine neue Mandelsäurenitril-Lyase (D-Oxynitrilase) aus Prunus laurocerasus (Kirschlorbeer)
    • Gerstner, E. & Kiel, U. 1975. Eine neue Mandelsäurenitril-Lyase (D-Oxynitrilase) aus Prunus laurocerasus (Kirschlorbeer).- Z. Physiol. Chem. 356: 1853-1857.
    • (1975) Z. Physiol. Chem. , vol.356 , pp. 1853-1857
    • Gerstner, E.1    Kiel, U.2
  • 13
    • 0015310231 scopus 로고
    • Zur Kenntnis des Flavineazyms Hydroxynitril-Lyase (D-Oxynitrilase)
    • _ & Pfeil, E. 1972. Zur Kenntnis des Flavineazyms Hydroxynitril-Lyase (D-Oxynitrilase). - Z. Physiol. Chem. 353: 271-286.
    • (1972) Z. Physiol. Chem. , vol.353 , pp. 271-286
    • Pfeil, E.1
  • 14
    • 0028253967 scopus 로고
    • Compartmentation of cyanogenic glycosides and their degrading enzymes
    • Gruhnert, C., Biehl, B. & Selmar, D. 1994. Compartmentation of cyanogenic glycosides and their degrading enzymes. - Planta 195: 36-42.
    • (1994) Planta , vol.195 , pp. 36-42
    • Gruhnert, C.1    Biehl, B.2    Selmar, D.3
  • 15
    • 0029978870 scopus 로고    scopus 로고
    • Molecular cloning of the full-length cDNA of (5)-hydroxynitrile lyase from Hevea brasiliense
    • Hasslacher, M., Schall, M., Hayn, M., Griengl, H., Kohlwein, S. D. & Schwab, H. 1996. Molecular cloning of the full-length cDNA of (5)-hydroxynitrile lyase from Hevea brasiliense. - J. Biol. Chem. 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
  • 16
    • 0026005904 scopus 로고
    • Thiol proteases and aldehyde dehydrogenases: Evolution from a common thiolesterase precursor?
    • Hempel, J., Nicholas, H. & Jörnvall, H. 1991. Thiol proteases and aldehyde dehydrogenases: Evolution from a common thiolesterase precursor? - Proteins 11: 176-183.
    • (1991) Proteins , vol.11 , pp. 176-183
    • Hempel, J.1    Nicholas, H.2    Jörnvall, H.3
  • 17
    • 0028247273 scopus 로고
    • Purification, characterization, and cloning of α-hydroxynitrile lyase from cassava (Manihot esculenta Crantz)
    • Hughes, J., De Carvalho, F. J. P. & Hughes, M. A. 1994. Purification, characterization, and cloning of α-hydroxynitrile lyase from cassava (Manihot esculenta Crantz). - Arch. Biochem. Biophys. 311: 496-502.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 496-502
    • Hughes, J.1    De Carvalho, F.J.P.2    Hughes, M.A.3
  • 18
    • 0021764990 scopus 로고
    • Chemical modification of hydroxynitrile lyase by selective reaction of an essential cysteine-SH group with α,β-unsaturated propiophenones as pseudo-substrates
    • Jaenicke, L. & Preuti, J. 1984. Chemical modification of hydroxynitrile lyase by selective reaction of an essential cysteine-SH group with α,β-unsaturated propiophenones as pseudo-substrates. - Eur. J. Biochem. 138: 319-325.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 319-325
    • Jaenicke, L.1    Preuti, J.2
  • 19
    • 0342471685 scopus 로고
    • Purification and protein characterization of hydroxynitrile lyases from Sorghum and Almond
    • Jansen, I., Woker, R. & Kula, M.-R. 1992. Purification and protein characterization of hydroxynitrile lyases from Sorghum and Almond. - Biotechnol. Appl. Biochem. 15: 90-99.
    • (1992) Biotechnol. Appl. Biochem. , vol.15 , pp. 90-99
    • Jansen, I.1    Woker, R.2    Kula, M.-R.3
  • 20
    • 0018787705 scopus 로고
    • Mechanism of catalysis by the flavoenzyme oxynitrilase
    • Jorns, M. S. 1979. Mechanism of catalysis by the flavoenzyme oxynitrilase. - J. Biol. Chem. 254: 12145-12152.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12145-12152
    • Jorns, M.S.1
  • 21
    • 0018813784 scopus 로고
    • Studies on the kinetics of cyanhydrin synthesis and cleavage by the flavoenzyme oxynitrile lyase
    • _ 1980. Studies on the kinetics of cyanhydrin synthesis and cleavage by the flavoenzyme oxynitrile lyase. - Biochim. Biophys. Acta 613: 203-209.
    • (1980) Biochim. Biophys. Acta , vol.613 , pp. 203-209
  • 22
    • 0022425392 scopus 로고
    • Comments on: 'Chemical modification of hydroxynitrile lyase by selective reaction of an essential cysteine-SH group with alpha, beta-unsaturated propiophenones as pseudo-substrates' by L. Jaenicke and J. Preun
    • _ 1985. Comments on: 'Chemical modification of hydroxynitrile lyase by selective reaction of an essential cysteine-SH group with alpha, beta-unsaturated propiophenones as pseudo-substrates' by L. Jaenicke and J. Preun [letter]. - Eur. J. Biochem. 146: 481-482.
    • (1985) Eur. J. Biochem. , vol.146 , pp. 481-482
  • 23
    • 0000225005 scopus 로고
    • Linamarase and other β-glucosidases are present in the cell wall of Trifolium repens L. leaves
    • Kakes, P. 1985. Linamarase and other β-glucosidases are present in the cell wall of Trifolium repens L. leaves. - Planta 166: 156-160.
    • (1985) Planta , vol.166 , pp. 156-160
    • Kakes, P.1
  • 24
    • 0008301655 scopus 로고
    • Is there rhodanese activity in plants?
    • _ & Hakvoort, H. 1992. Is there rhodanese activity in plants? - Phytochemistry 31: 1501-1505.
    • (1992) Phytochemistry , vol.31 , pp. 1501-1505
    • Hakvoort, H.1
  • 25
    • 0027325846 scopus 로고
    • Aliphatic (S)-cyanhydrins by enzyme catalysed synthesis
    • Klempier, N., Griengl, H. & Hayn, M. 1993. Aliphatic (S)-cyanhydrins by enzyme catalysed synthesis. - Tetrahedron Lett. 34: 4769-4772.
    • (1993) Tetrahedron Lett. , vol.34 , pp. 4769-4772
    • Klempier, N.1    Griengl, H.2    Hayn, M.3
  • 26
    • 0028964103 scopus 로고
    • Synthesis of aα,β-unsaturated (S)-cyanohydrins using the oxynitrilase from Hevea brasiliensis
    • _, Pichler, U. & Griengl, H. 1995. Synthesis of aα,β-unsaturated (S)-cyanohydrins using the oxynitrilase from Hevea brasiliensis. - Tetrahedron: Asymmetry 6: 845-848.
    • (1995) Tetrahedron: Asymmetry , vol.6 , pp. 845-848
    • Pichler, U.1    Griengl, H.2
  • 27
    • 0000297833 scopus 로고
    • Tissue distributions of dhurrin and of enzymes involved in its metabolism in leaves of Sorghum bicolor
    • Kojima, N., Poulton, J. E., Thayer, S. S. & Conn, E. E. 1979. Tissue distributions of dhurrin and of enzymes involved in its metabolism in leaves of Sorghum bicolor. - Plant Physiol. 63: 1022-1028.
    • (1979) Plant Physiol. , vol.63 , pp. 1022-1028
    • Kojima, N.1    Poulton, J.E.2    Thayer, S.S.3    Conn, E.E.4
  • 28
    • 0002968804 scopus 로고
    • Chiral cyanohydnns - Their manufacture and utility as chiral building blocks
    • John Wiley & Sons Ltd. Chichester. ISBN 0-471-93595-6
    • Kruse, C. G. 1992. Chiral cyanohydnns - their manufacture and utility as chiral building blocks. - In Chirality in Industry. John Wiley & Sons Ltd. Chichester. pp. 279-299. ISBN 0-471-93595-6.
    • (1992) Chirality in Industry , pp. 279-299
    • Kruse, C.G.1
  • 29
    • 0024728476 scopus 로고
    • Mandelonitrile lyase from Ximenia americana L.: Slereospecificity and lack of flavin prosthetic group
    • Kuroki, G. W. & Conn, E. E. 1989. Mandelonitrile lyase from Ximenia americana L.: Slereospecificity and lack of flavin prosthetic group. - Proc. Natl. Acad. Sci. USA 86: 6978-6981.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6978-6981
    • Kuroki, G.W.1    Conn, E.E.2
  • 31
    • 0002123773 scopus 로고
    • Metabolization of cyanogenic glucosides in Hevea brasiliensis
    • Lieberei, R., Selmar, D. & Biehl, B. 1985. Metabolization of cyanogenic glucosides in Hevea brasiliensis. - Plant Syst. Evol. 150: 49-63.
    • (1985) Plant Syst. Evol. , vol.150 , pp. 49-63
    • Lieberei, R.1    Selmar, D.2    Biehl, B.3
  • 32
    • 0025694677 scopus 로고
    • Purification and characterization of an α-hydroxynitrile lyase from the haemolymph of the larvae of Zygaena trifolii
    • Müller, E. & Nahrsted, A. 1990. Purification and characterization of an α-hydroxynitrile lyase from the haemolymph of the larvae of Zygaena trifolii. - Planta Med. 56: 612.
    • (1990) Planta Med. , vol.56 , pp. 612
    • Müller, E.1    Nahrsted, A.2
  • 33
    • 0002140025 scopus 로고
    • Cyanogenic compounds as protecting agents for organisms
    • Nahrstedt, A. 1985. Cyanogenic compounds as protecting agents for organisms. - Plant Syst. Evol. 150: 35-47.
    • (1985) Plant Syst. Evol. , vol.150 , pp. 35-47
    • Nahrstedt, A.1
  • 34
    • 0001676723 scopus 로고
    • Enzymkatalysierte Synthese von (S)-Cyanhydrinen
    • Niedermeyer, U. & Kula, M.-R. 1990. Enzymkatalysierte Synthese von (S)-Cyanhydrinen. - Angew. Chem. 102: 423-424.
    • (1990) Angew. Chem. , vol.102 , pp. 423-424
    • Niedermeyer, U.1    Kula, M.-R.2
  • 35
    • 85064432185 scopus 로고
    • Catalytic asymmetric cyanhydrin synthesis
    • North, M. 1993. Catalytic asymmetric cyanhydrin synthesis. - Synlett. 807-820.
    • (1993) Synlett. , pp. 807-820
    • North, M.1
  • 36
    • 0000700061 scopus 로고
    • Diurnal variation of cyanogenic slucosides, thiocyanate and rhodanese in cassava
    • Okolie, P. N. & Obasi, B. N. 1993. Diurnal variation of cyanogenic slucosides, thiocyanate and rhodanese in cassava. - Phytochemistry 33: 775-778.
    • (1993) Phytochemistry , vol.33 , pp. 775-778
    • Okolie, P.N.1    Obasi, B.N.2
  • 38
    • 0028269037 scopus 로고
    • Transient inactivation of almond mandelonitrile tyase by 3-methyleneoxindole: A photooxidation product of the natural plant hormone indole-3-acetic acid
    • Petrounia, I. P., Goldberg, J. & Brush, E. J. 1994. Transient inactivation of almond mandelonitrile tyase by 3-methyleneoxindole: A photooxidation product of the natural plant hormone indole-3-acetic acid - Biochemistry 33: 2891-2899.
    • (1994) Biochemistry , vol.33 , pp. 2891-2899
    • Petrounia, I.P.1    Goldberg, J.2    Brush, E.J.3
  • 39
    • 0024259550 scopus 로고
    • Localization and catabolism of cyanogenic glycosides
    • Ciba Foundation Symposium No. 140, John Wiley & Sons Ltd, Chichester. ISBN 0-471-91904-7
    • Poulton, J. E. 1988. Localization and catabolism of cyanogenic glycosides. - In Cyanide Compounds in Biology. Ciba Foundation Symposium No. 140, pp. 67-91. John Wiley & Sons Ltd, Chichester. ISBN 0-471-91904-7.
    • (1988) Cyanide Compounds in Biology , pp. 67-91
    • Poulton, J.E.1
  • 40
    • 0005789287 scopus 로고
    • Enzymology of cyanogenesis in rosaceous stone fruits
    • _ 1993. Enzymology of cyanogenesis in rosaceous stone fruits. - ACS Symp. Ser. 12: 170-190.
    • (1993) ACS Symp. Ser. , vol.12 , pp. 170-190
  • 41
    • 0001213299 scopus 로고
    • The presence of the cyanogenic slycoside dhurrin in isolated vacuoles from Sorghum
    • Saunders, J. A. & Conn, E. E. 1978. The presence of the cyanogenic slycoside dhurrin in isolated vacuoles from Sorghum. - Plant Physiol. 61: 154-157.
    • (1978) Plant Physiol. , vol.61 , pp. 154-157
    • Saunders, J.A.1    Conn, E.E.2
  • 42
    • 0009830610 scopus 로고
    • Subcellular localization of the cyanogenic glycosides of Sorghum by autoradiography
    • _, Conn, E. E., Lin, C. H. & Stocking, C. R. 1977. Subcellular localization of the cyanogenic glycosides of Sorghum by autoradiography. - Plant Physiol. 59: 647-652.
    • (1977) Plant Physiol. , vol.59 , pp. 647-652
    • Conn, E.E.1    Lin, C.H.2    Stocking, C.R.3
  • 43
    • 0014011418 scopus 로고
    • The metabolism of aromatic compounds in higher plants
    • Seely, M. K., Criddle, R. S. & Conn, E. E. 1966. The metabolism of aromatic compounds in higher plants. - J. Biol. Chem. 241: 4457-4462.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4457-4462
    • Seely, M.K.1    Criddle, R.S.2    Conn, E.E.3
  • 44
    • 0000713888 scopus 로고
    • Apoplastic occurrence of cyanogenic β-glucosidases and consequences for the metabolism of cyanogenic glucosides
    • Selmar, D. 1993. Apoplastic occurrence of cyanogenic β-glucosidases and consequences for the metabolism of cyanogenic glucosides. - ACS Symp. Ser. 13: 191-204.
    • (1993) ACS Symp. Ser. , vol.13 , pp. 191-204
    • Selmar, D.1
  • 45
    • 0000966890 scopus 로고
    • Mobilization and utilization of cyanogenic glycosides
    • _, Lieberei, R. & Biehl, B. 1988. Mobilization and utilization of cyanogenic glycosides. - Plant Physiol. 86: 711-716.
    • (1988) Plant Physiol. , vol.86 , pp. 711-716
    • Lieberei, R.1    Biehl, B.2
  • 46
    • 0002545280 scopus 로고
    • α-Hydoxynitrile lyase in Hevea brasiliensis and its significance for rapid cyanogenesis
    • _, Lieberei, R., Biehl, B. & Conn, E. E. 1989. α-Hydoxynitrile lyase in Hevea brasiliensis and its significance for rapid cyanogenesis. - Physiol. Plant. 75: 97-101.
    • (1989) Physiol. Plant , vol.75 , pp. 97-101
    • Lieberei, R.1    Biehl, B.2    Conn, E.E.3
  • 48
    • 0038142491 scopus 로고
    • Development of the potential for cyanogenesis in maturing black cherry (Prunus serotina Ehrh.) fruits
    • Swain, E., Li, C. P. & Poulton, J. E. 1992a. Development of the potential for cyanogenesis in maturing black cherry (Prunus serotina Ehrh.) fruits. - Plant Physiol. 98: 1423-1428.
    • (1992) Plant Physiol. , vol.98 , pp. 1423-1428
    • Swain, E.1    Li, C.P.2    Poulton, J.E.3
  • 49
    • 0001059769 scopus 로고
    • Tissue and subcellular localization of enzymes catabolizins (R)-amygdalin in mature Prunus serolina seeds
    • _, Li, C. P. & Poulton, J. E. 1992b. Tissue and subcellular localization of enzymes catabolizins (R)-amygdalin in mature Prunus serolina seeds. - Plant Physiol. 100: 291-300.
    • (1992) Plant Physiol. , vol.100 , pp. 291-300
    • Li, C.P.1    Poulton, J.E.2
  • 50
    • 0000480371 scopus 로고
    • Subcellular localization of dhurrin β-glucosidase and hydroxynitrile lyase in the mesophyll cells of Sorghum leaf blades
    • Thayer, S. & Conn, E. E. 1981. Subcellular localization of dhurrin β-glucosidase and hydroxynitrile lyase in the mesophyll cells of Sorghum leaf blades. - Plant Physiol. 67: 617-622.
    • (1981) Plant Physiol. , vol.67 , pp. 617-622
    • Thayer, S.1    Conn, E.E.2
  • 51
    • 0002961690 scopus 로고
    • The potential of (R)- and (S)-oxynitriIases for the enzymatic synthesis of optically active cyanhydrins
    • van Scharrenburg, G. J. M., Sloothaak, J. B., Kruse, C. G., Smitskamp-Wilms, E. & Brussee, J. 1993. The potential of (R)- and (S)-oxynitriIases for the enzymatic synthesis of optically active cyanhydrins. - Ind. J. Chem. 32B: 16-19.
    • (1993) Ind. J. Chem. , vol.32 B , pp. 16-19
    • Van Scharrenburg, G.J.M.1    Sloothaak, J.B.2    Kruse, C.G.3    Smitskamp-Wilms, E.4    Brussee, J.5
  • 52
    • 0030586027 scopus 로고    scopus 로고
    • The crystal structure of the hydroxynitrile lyase from rubber tree Hevea brasiliensis suggests that the enzyme is structurally and mechanistically related to α/β hydrolases
    • Wagner, U., Hasslacher, M., Griengl, H., Schwab, H. & Kratky, C. 1996. The crystal structure of the hydroxynitrile lyase from rubber tree Hevea brasiliensis suggests that the enzyme is structurally and mechanistically related to α/β hydrolases. - Structure 4: 811-822.
    • (1996) Structure , vol.4 , pp. 811-822
    • Wagner, U.1    Hasslacher, M.2    Griengl, H.3    Schwab, H.4    Kratky, C.5
  • 53
    • 0000532033 scopus 로고
    • Hydroxynitrile lyase from Sorghum bicolor: A glycoprotein heterotetramer
    • Wajant, H. & Mundry, K.-W. 1993. Hydroxynitrile lyase from Sorghum bicolor: A glycoprotein heterotetramer. - Plant Sci. 89: 127-133.
    • (1993) Plant Sci. , vol.89 , pp. 127-133
    • Wajant, H.1    Mundry, K.-W.2
  • 54
    • 0011956437 scopus 로고
    • Purification of hydroxynitrile lyase from Sorghum bicolor L. (sorghum) by affinity chromatography using monoclonal antibodies
    • H.
    • _, H., Böttinger, H. & Mundry, K.-W. 1993. Purification of hydroxynitrile lyase from Sorghum bicolor L. (sorghum) by affinity chromatography using monoclonal antibodies. -Biotechnol. Appl. Biochem. 18: 75-82.
    • (1993) Biotechnol. Appl. Biochem. , vol.18 , pp. 75-82
    • Böttinger, H.1    Mundry, K.-W.2
  • 55
    • 0028519028 scopus 로고
    • Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.). Homologies to serine carboxypeptidase
    • _, Mundry, K.-W. & Pfizenmaier, K. 1994a. Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.). Homologies to serine carboxypeptidase. - Plant Mol. Biol 26: 735-746.
    • (1994) Plant Mol. Biol , vol.26 , pp. 735-746
    • Mundry, K.-W.1    Pfizenmaier, K.2
  • 56
    • 0028190831 scopus 로고
    • Immunocytological localization of hydroxynitrile lyase from Sorghum bicolor L. and Linum usitatissimum L
    • _, Riedel, D., Benz, S. & Mundry, K.-W. 1994b. Immunocytological localization of hydroxynitrile lyase from Sorghum bicolor L. and Linum usitatissimum L. - Plant Sci. 103: 145-154.
    • (1994) Plant Sci. , vol.103 , pp. 145-154
    • Riedel, D.1    Benz, S.2    Mundry, K.-W.3
  • 57
    • 0029164138 scopus 로고
    • Acetone cyanohydrin lyase from Manihot esculenta (cassava) is serologically distinct from other hydroxynitrile lyases
    • _, Förster, S., Böttinger, H., Effenberger, F. & Pfizenmaier, K. 1995a. Acetone cyanohydrin lyase from Manihot esculenta (cassava) is serologically distinct from other hydroxynitrile lyases. - Plant Sci. 103: 1-11.
    • (1995) Plant Sci. , vol.103 , pp. 1-11
    • Förster, S.1    Böttinger, H.2    Effenberger, F.3    Pfizenmaier, K.4
  • 58
    • 0029188401 scopus 로고
    • Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum
    • _, Förster, S., Selmar, D., Effenberger, F. & Pfizenmaier, K. 1995b. Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum. - Plant Physiol. 109: 1231-1238.
    • (1995) Plant Physiol. , vol.109 , pp. 1231-1238
    • Förster, S.1    Selmar, D.2    Effenberger, F.3    Pfizenmaier, K.4
  • 59
    • 0344095956 scopus 로고
    • Immunocytochemical localization of mandelonitrile lyase in mature black cherry (Prunus serotina Ehrh.) seeds
    • Wu, H.-C. & Poulton, J. E. 1991. Immunocytochemical localization of mandelonitrile lyase in mature black cherry (Prunus serotina Ehrh.) seeds. - Plant Physiol. 96: 1329-1337.
    • (1991) Plant Physiol. , vol.96 , pp. 1329-1337
    • Wu, H.-C.1    Poulton, J.E.2
  • 60
    • 0022809152 scopus 로고
    • Purification and characterization of mandelonitrile lyase from Prunus lyonii
    • Xu, L.-L., Singh, B. K. & Conn, E. E. 1986. Purification and characterization of mandelonitrile lyase from Prunus lyonii. - Arch. Biochem. Biophys. 250: 322-328.
    • (1986) Arch. Biochem. Biophys. , vol.250 , pp. 322-328
    • Xu, L.-L.1    Singh, B.K.2    Conn, E.E.3
  • 61
    • 0024022058 scopus 로고
    • Purification and characterization of acetone cyanohydrin lyase from Linum usitatissimum
    • _, Singh, B. K. & Conn, E. E. 1988. Purification and characterization of acetone cyanohydrin lyase from Linum usitatissimum. - Arch. Biochem. Biophys. 263: 256-263.
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 256-263
    • Singh, B.K.1    Conn, E.E.2
  • 62
    • 0022725311 scopus 로고
    • Isolation and characterization of multiple forms of mandelonitrile lyase from mature black cherry (Prunus serotina Ehrh.) seeds
    • Yemm, R. S. & Poulton, J. E. 1986. Isolation and characterization of multiple forms of mandelonitrile lyase from mature black cherry (Prunus serotina Ehrh.) seeds. - Arch. Biochem. Biophys. 247: 440-445.
    • (1986) Arch. Biochem. Biophys. , vol.247 , pp. 440-445
    • Yemm, R.S.1    Poulton, J.E.2
  • 63
    • 84989568771 scopus 로고
    • Ein einfacher Zugang zu (R)-α-Hydroxycarbonsauren und (R)-1-Amino-2-alkoholen aus (R)-Cyanhydrinen
    • Ziegler, T., Hörsch, B. & Effenberger, F. 1990. Ein einfacher Zugang zu (R)-α-Hydroxycarbonsauren und (R)-1-Amino-2-alkoholen aus (R)-Cyanhydrinen. - Synthesis 575-578.
    • (1990) Synthesis , pp. 575-578
    • Ziegler, T.1    Hörsch, B.2    Effenberger, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.