메뉴 건너뛰기




Volumn 53, Issue 3, 1997, Pages 332-338

Production and characterization of a plant α-hydroxynitrile lyase in Escherichia coli

Author keywords

hydroxynitrile lyase; cassava; cyanogenesis; cyanohydrin; Escherichia coli expression vector

Indexed keywords

BACTERIA; BIOASSAY; BIOSYNTHESIS; CHARACTERIZATION; DNA SEQUENCES; PLANTS (BOTANY); PROTEINS; SPECTROSCOPY;

EID: 0031553672     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19970205)53:3<332::AID-BIT12>3.0.CO;2-M     Document Type: Article
Times cited : (24)

References (25)
  • 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
  • 3
    • 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
  • 4
    • 33748215202 scopus 로고
    • Synthesis and reactions of optically active cyanohydrins
    • Effenberger, F. 1994. Synthesis and reactions of optically active cyanohydrins. Angew. Chem. Int. Ed. Engl. 33: 1555-1564.
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 1555-1564
    • Effenberger, F.1
  • 5
    • 0025034596 scopus 로고
    • Enzyme catalysed synthesis of (S)-cyanohydrins and subsequent hydrolysis to (S)-α-hydroxy-carboxylic acids
    • Effenberger, F., Hörsch, B., Förster, S., Zeigler, T. 1990. Enzyme catalysed synthesis of (S)-cyanohydrins and subsequent hydrolysis to (S)-α-hydroxy-carboxylic acids. Tetrahedr. Lett. 31: 1249-1252.
    • (1990) Tetrahedr. Lett. , vol.31 , pp. 1249-1252
    • Effenberger, F.1    Hörsch, B.2    Förster, S.3    Zeigler, T.4
  • 6
    • 0028247273 scopus 로고
    • Purification, characterisation and cloning of α-hydroxynitrile lyase from cassava (Manihot esculenta Crantz)
    • Hughes, J., Carvalho, F. J. P. de C., Hughes, M. A. 1994. Purification, characterisation 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    Carvalho, F.J.P.D.C.2    Hughes, M.A.3
  • 7
    • 0027325846 scopus 로고
    • Aliphatic (S)-cyanohydrins by enzyme catalysed synthesis
    • Klempier, N., Griengl, H. 1993. Aliphatic (S)-cyanohydrins by enzyme catalysed synthesis. Tetrahedr. Lett. 34: 4769-4772.
    • (1993) Tetrahedr. Lett. , vol.34 , pp. 4769-4772
    • Klempier, N.1    Griengl, H.2
  • 8
    • 0024728476 scopus 로고
    • Mandelonitrile lyase from Ximenia americana L.: Steriospecificity and lack of flavin prosthetic group
    • Kuroki, G. W., Conn, E. E. 1989. Mandelonitrile lyase from Ximenia americana L.: Steriospecificity and lack of flavin prosthetic group. Proc. Nati. Acad. Sci. USA 86: 6978-6981.
    • (1989) Proc. Nati. Acad. Sci. USA , vol.86 , pp. 6978-6981
    • Kuroki, G.W.1    Conn, E.E.2
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 10
    • 33847800895 scopus 로고
    • Stable reagents for colorimetric determination of cyanide by modified König reactions
    • Lambert, J. L., Ramasamy, J., Paukstelis, J. 1975. Stable reagents for colorimetric determination of cyanide by modified König reactions. Anal. Chem. 47: 916-919.
    • (1975) Anal. Chem. , vol.47 , pp. 916-919
    • Lambert, J.L.1    Ramasamy, J.2    Paukstelis, J.3
  • 11
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesised in Escherichia coli
    • Marston, F. A. O. 1986. The purification of eukaryotic polypeptides synthesised in Escherichia coli. Biochem. J. 240: 1-12.
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.O.1
  • 12
    • 21644489778 scopus 로고
    • Preparation of chiral cyanohydrins by an oxynitrilase-mediated transcyanation
    • Ognyanov, V. I., Datcheva, V. K., Kyler, K. S. 1991. Preparation of chiral cyanohydrins by an oxynitrilase-mediated transcyanation. J. Am. Chem. Soc. 113: 6992-6996.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6992-6996
    • Ognyanov, V.I.1    Datcheva, V.K.2    Kyler, K.S.3
  • 13
    • 0000026228 scopus 로고
    • Cyanpgenesis in plants
    • Poulton, J. E. 1990. Cyanpgenesis in plants. Plant Physiol. 94: 401-405.
    • (1990) Plant Physiol. , vol.94 , pp. 401-405
    • Poulton, J.E.1
  • 14
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S. W., Glockner, J. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20: 33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 15
    • 0001895061 scopus 로고
    • Expression and purification of maltose binding protein fusions. Unit 16.6
    • Wiley, New York
    • Riggs, P. 1994. Expression and purification of maltose binding protein fusions. Unit 16.6. In: Current protocols in molecular biology. Wiley, New York.
    • (1994) Current Protocols in Molecular Biology
    • Riggs, P.1
  • 16
    • 0000828332 scopus 로고
    • Cyanogenic glycosides lipids: Structural types and distribution
    • B. Vennesland, E. F., Conn, C. J. Knowles, J. Westley, and F. Wissing (eds.), Academic Press, London
    • Seigler, D. S. 1981. Cyanogenic glycosides lipids: Structural types and distribution. In: B. Vennesland, E. F., Conn, C. J. Knowles, J. Westley, and F. Wissing (eds.), Cyanide in Biology. Academic Press, London.
    • (1981) Cyanide in Biology
    • Seigler, D.S.1
  • 17
    • 0023428155 scopus 로고
    • A colorimetric assay for α-hydroxynitrile lyase
    • Selmar, D., Carvalho, F. J. P. de C., Conn, E. E. 1987. A colorimetric assay for α-hydroxynitrile lyase. Anal. Biochem. 166: 208-211.
    • (1987) Anal. Biochem. , vol.166 , pp. 208-211
    • Selmar, D.1    Carvalho, F.J.P.D.C.2    Conn, E.E.3
  • 18
    • 0002545280 scopus 로고
    • α-Hydroxynitrile lyase in Hevea braziliensis and its significance for rapid cyanogenesis
    • Selmar, D., Lieberei, R., Biehl, B., Conn, E. E. 1989. α-Hydroxynitrile lyase in Hevea braziliensis and its significance for rapid cyanogenesis. Physiol. Plant. 75: 97-101.
    • (1989) Physiol. Plant. , vol.75 , pp. 97-101
    • Selmar, D.1    Lieberei, R.2    Biehl, B.3    Conn, E.E.4
  • 20
    • 0028519028 scopus 로고
    • Molecular cloning of hydroxynitrile lyase from Sorghum, bicolor (L). Homologies to serine carboxypeptidases
    • Wajant, H., Mundry, K-W., Pfizenmaier, K. 1994a. Molecular cloning of hydroxynitrile lyase from Sorghum, bicolor (L). Homologies to serine carboxypeptidases. Plant Mol. Biol. 26: 735-746.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 735-746
    • Wajant, H.1    Mundry, K.-W.2    Pfizenmaier, K.3
  • 21
    • 0028190831 scopus 로고
    • Immunocytological localisation of hydroxynitrile lyases from Sorgum bicolor L. and Linum usitatissimum L
    • Wajant, H., Riedel, D., Benz, S., Mundry, K-W. 1994b. Immunocytological localisation of hydroxynitrile lyases from Sorgum bicolor L. and Linum usitatissimum L. Plant Sci. 103: 145-154.
    • (1994) Plant Sci. , vol.103 , pp. 145-154
    • Wajant, H.1    Riedel, D.2    Benz, S.3    Mundry, K.-W.4
  • 22
    • 0029164138 scopus 로고
    • Acetone cyanohydrin lyase from Manihot esculenta (cassava) is serologically distinct from other hydroxynitrile lyases
    • Wajant, H., 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. 108: 1-11.
    • (1995) Plant Sci. , vol.108 , pp. 1-11
    • Wajant, H.1    Förster, S.2    Böttinger, H.3    Effenberger, F.4    Pfizenmaier, K.5
  • 23
    • 0029188401 scopus 로고
    • Purification and characterisation of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum
    • Wajant, H., Förster, S., Selmar, D., Effenberger, F., Pfizenmaier, K. 1995b. Purification and characterisation of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum. Plant Physiol. 109: 1231-1238.
    • (1995) Plant Physiol. , vol.109 , pp. 1231-1238
    • Wajant, H.1    Förster, S.2    Selmar, D.3    Effenberger, F.4    Pfizenmaier, K.5
  • 24
    • 0002329558 scopus 로고
    • Regulation of cyanogenesis in cassava
    • White, W. L. B., McMahon, J. M., Sayre, R. T. 1994. Regulation of cyanogenesis in cassava. Acta Hort. 375: 69-78.
    • (1994) Acta Hort. , vol.375 , pp. 69-78
    • White, W.L.B.1    McMahon, J.M.2    Sayre, R.T.3
  • 25
    • 0024022058 scopus 로고
    • Purification and characterisation of acetone cyanohydrin lysse from Linum usitatissimum
    • Xu, L-L., Singh, B. K., Conn, E. E. 1988. Purification and characterisation of acetone cyanohydrin lysse from Linum usitatissimum. Arch. Biochem. Biophys. 266: 256-263.
    • (1988) Arch. Biochem. Biophys. , vol.266 , pp. 256-263
    • Xu, L.-L.1    Singh, B.K.2    Conn, E.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.