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Volumn 11, Issue 1, 1997, Pages 61-71

High-level intracellular expression of hydroxynitrile lyase from the tropical rubber tree Hevea brasiliensis in microbial hosts

Author keywords

[No Author keywords available]

Indexed keywords

HEVEA BRASILIENSIS;

EID: 0031259717     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1997.0765     Document Type: Article
Times cited : (116)

References (41)
  • 1
    • 0002968804 scopus 로고
    • Chiral cyanohydrins - Their manufacture and utility as chiral building blocks
    • (Collins, A. N., Sheldrake, G. N., and Crosby, J., Eds.), Wiley, New York
    • 1. Kruse, C. G. (1992) Chiral cyanohydrins - Their manufacture and utility as chiral building blocks, in "Chirality in Industry" (Collins, A. N., Sheldrake, G. N., and Crosby, J., Eds.), pp. 279-299, Wiley, New York.
    • (1992) Chirality in Industry , pp. 279-299
    • Kruse, C.G.1
  • 3
    • 0015310231 scopus 로고
    • Zur kenntnis des flavinenzyms hydroxynitril-lyase (D-oxynitrilase)
    • 3. Gerstner, E., and Pfeil, E. (1972) Zur kenntnis des flavinenzyms hydroxynitril-lyase (D-oxynitrilase). Hoppe-Seyler's Z. Physiol. Chem. 353, 271-286.
    • (1972) Hoppe-Seyler's Z. Physiol. Chem. , vol.353 , pp. 271-286
    • Gerstner, E.1    Pfeil, E.2
  • 4
    • 0016651075 scopus 로고
    • Eine neue mandelsäurenitrillyase (D-oxynitrilase) aus Prunus laurocerasus (Kirschlorbeer)
    • 4. Gerstner, E., and Kiel, U. (1975) Eine neue mandelsäurenitrillyase (D-oxynitrilase) aus Prunus laurocerasus (Kirschlorbeer). Hoppe-Seyler's Z. Physiol. Chem. 356, 1853-1857.
    • (1975) Hoppe-Seyler's Z. Physiol. Chem. , vol.356 , pp. 1853-1857
    • Gerstner, E.1    Kiel, U.2
  • 5
    • 0027325846 scopus 로고
    • Aliphatic (S)-cyanohydrins by enzyme-catalyzed synthesis
    • 5. Kiempier, N., Griengl, H., and Hayn, M. (1993) Aliphatic (S)-cyanohydrins by enzyme-catalyzed synthesis. Tetrahedron Lett. 34, 4769-4772.
    • (1993) Tetrahedron Lett. , vol.34 , pp. 4769-4772
    • Kiempier, N.1    Griengl, H.2    Hayn, M.3
  • 6
    • 0028964103 scopus 로고
    • Synthesis of α/ β-unsaturated (S)-cyanohydrins using oxynitrilase from Hevea brasiliensis
    • 6. Kiempier, N., Pichier, U., and Griengl, H. (1995) Synthesis of α/ β-unsaturated (S)-cyanohydrins using oxynitrilase from Hevea brasiliensis. Tetrahedron: Asymmetry 6, 845-848.
    • (1995) Tetrahedron: Asymmetry , vol.6 , pp. 845-848
    • Kiempier, N.1    Pichier, U.2    Griengl, H.3
  • 8
    • 0029978870 scopus 로고    scopus 로고
    • Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis
    • 8. Hasslacher, M., Schall, M., Hayn, M., Griengl, H., Kohlwein, S. D., and Schwab, H. (1996) Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis. 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
  • 9
    • 0030975258 scopus 로고    scopus 로고
    • Hydroxynitrile lyase from Hevea brasiliensis: Molecular characterization and mechanism of enzyme catalysis
    • 9. Hasslacher, M., Kratky, C., Griengl, H., Schwab, H., and Kohlwein, S. D. (1997) Hydroxynitrile lyase from Hevea brasiliensis: Molecular characterization and mechanism of enzyme catalysis. Proteins 27, 438-449.
    • (1997) Proteins , vol.27 , pp. 438-449
    • Hasslacher, M.1    Kratky, C.2    Griengl, H.3    Schwab, H.4    Kohlwein, S.D.5
  • 10
    • 0030586027 scopus 로고    scopus 로고
    • Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis
    • 10. Wagner, U. G., Hasslacher, M., Griengl, H., Schwab, H., and Kratky, C. (1996) Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Structure 4, 811-822.
    • (1996) Structure , vol.4 , pp. 811-822
    • Wagner, U.G.1    Hasslacher, M.2    Griengl, H.3    Schwab, H.4    Kratky, C.5
  • 11
    • 0028247273 scopus 로고
    • Purification, characterization, and cloning of α-hydroxynitrile lyase from cassava (Manihot esculenta crantz)
    • 11. Hughes, J., Decarvalho, J., and 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    Decarvalho, J.2    Hughes, M.A.3
  • 12
    • 0028519028 scopus 로고
    • Molecular-cloning of hydroxynitrile lyase from Sorghum bicolor (L) - Homologies to serine carboxypeptidases
    • 12. Wajant, H., Mundry, K. W., and Pfizenmaier, K. (1994) 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
  • 13
    • 0025351553 scopus 로고
    • Enhanced translational efficiency with two-cistron expression systems
    • 13. Schoner, B. E., Belagaje, R. M., and Schoner, R. (1990) Enhanced translational efficiency with two-cistron expression systems. Meth. Enzymol. 185, 94-103.
    • (1990) Meth. Enzymol. , vol.185 , pp. 94-103
    • Schoner, B.E.1    Belagaje, R.M.2    Schoner, R.3
  • 14
    • 0022781503 scopus 로고
    • Yeast/E. coli shuttle vector with multiple unique restriction sites
    • 14. Hill, J. E., Myers, A. M., Koerner, T. J., and Tzagloff, A. (1986) Yeast/E. coli shuttle vector with multiple unique restriction sites. Yeast 2, 163-167.
    • (1986) Yeast , vol.2 , pp. 163-167
    • Hill, J.E.1    Myers, A.M.2    Koerner, T.J.3    Tzagloff, A.4
  • 15
    • 0025365144 scopus 로고
    • High-efficiency yeast expression vectors based on the promoter of the phosphoglycerate kinase gene
    • 15. Kingsman, S. M., Cousens, D., Stanway, C. A., Chambers, A., Wilson, M., and Kingsman, A. J. (1990) High-efficiency yeast expression vectors based on the promoter of the phosphoglycerate kinase gene. Meth. Enzymol. 185, 329-341.
    • (1990) Meth. Enzymol. , vol.185 , pp. 329-341
    • Kingsman, S.M.1    Cousens, D.2    Stanway, C.A.3    Chambers, A.4    Wilson, M.5    Kingsman, A.J.6
  • 18
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • 18. Sanger, F., Niklen, S., and Coulsen, A. R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Niklen, S.2    Coulsen, A.R.3
  • 19
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • 19. Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983) Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 22
    • 0002111298 scopus 로고
    • The purification of eucaryontic polypeptides expressed in E. coli
    • (Glover, D. M., Ed.), IRL Press, Oxford
    • 22. Martson, F. A. O. (1987) The purification of eucaryontic polypeptides expressed in E. coli, in "DNA Cloning: A Practical Approach" (Glover, D. M., Ed.), pp. 59-88, IRL Press, Oxford.
    • (1987) DNA Cloning: A Practical Approach , pp. 59-88
    • Martson, F.A.O.1
  • 25
    • 0021019879 scopus 로고
    • Vectors bearing a hybrid trp-lac promoter seful for regulated expression of cloned genes in Escherichia coli
    • 25. Amann, E., Brosius, J., and Ptashne, M. (1983) Vectors bearing a hybrid trp-lac promoter seful for regulated expression of cloned genes in Escherichia coli. Gene 25, 167-178.
    • (1983) Gene , vol.25 , pp. 167-178
    • Amann, E.1    Brosius, J.2    Ptashne, M.3
  • 26
    • 0028533566 scopus 로고
    • Recent developments in heterologous protein production in Escherichia coli
    • 26. Hockney, R. C. (1994) Recent developments in heterologous protein production in Escherichia coli. Trends Biotechnol. 12, 456-463.
    • (1994) Trends Biotechnol. , vol.12 , pp. 456-463
    • Hockney, R.C.1
  • 27
    • 0023892436 scopus 로고
    • Formation of recombinant protein in E. coli is favored by lower growth temperature
    • 27. Schein, C. H., and Noteborn, M. H. M. (1988) Formation of recombinant protein in E. coli is favored by lower growth temperature. Bio/Technology 6, 291-294.
    • (1988) Bio/Technology , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, M.H.M.2
  • 28
    • 0025737589 scopus 로고
    • Higher culture pH is preferable for inclusion body formation of recombinant salmon growth-hormone in Escherichia coli
    • 28. Sugimoto, S., Yokoo, Y., Hatakeyama, N., Yotsuji, A., Teshiba, S., and Hagino, H. (1991) Higher culture pH is preferable for inclusion body formation of recombinant salmon growth-hormone in Escherichia coli. Biotechnol. Lett. 13, 385-388.
    • (1991) Biotechnol. Lett. , vol.13 , pp. 385-388
    • Sugimoto, S.1    Yokoo, Y.2    Hatakeyama, N.3    Yotsuji, A.4    Teshiba, S.5    Hagino, H.6
  • 29
    • 0027584038 scopus 로고
    • Overcoming inclusion body formation in a high-level expression system
    • 29. Moore, J. T., Uppal, A., Maley, F., and Maley, G. F. (1993) Overcoming inclusion body formation in a high-level expression system. Protein Expression Purif. 4, 160-163.
    • (1993) Protein Expression Purif. , vol.4 , pp. 160-163
    • Moore, J.T.1    Uppal, A.2    Maley, F.3    Maley, G.F.4
  • 30
    • 0006553715 scopus 로고
    • Expression in yeast
    • Academic Press, San Diego
    • 30. Goeddel, D. V. (Ed.) (1990) Expression in yeast in "Methods in Enzymology," pp. 231-484, Academic Press, San Diego.
    • (1990) Methods in Enzymology , pp. 231-484
    • Goeddel, D.V.1
  • 31
    • 0026778048 scopus 로고
    • Foreign gene expression in yeast
    • 31. Romanos, M. A., Scorer, C. A., and Clare, J. J. (1992) Foreign gene expression in yeast. Yeast 8, 423-488.
    • (1992) Yeast , vol.8 , pp. 423-488
    • Romanos, M.A.1    Scorer, C.A.2    Clare, J.J.3
  • 33
    • 0346490297 scopus 로고
    • The production of interferon in bacteria and yeast
    • (Birke, D. C., and Morris, A., Ed.), Cambridge University Press, Cambridge, UK
    • 33. Kingsman, S. M., and Kingsman, A. J. (1983) The production of interferon in bacteria and yeast, in "Interferons, Society for General Microbiology Symp." (Birke, D. C., and Morris, A., Ed.), pp. 211-254, Cambridge University Press, Cambridge, UK.
    • (1983) Interferons, Society for General Microbiology Symp. , pp. 211-254
    • Kingsman, S.M.1    Kingsman, A.J.2
  • 35
    • 0025168284 scopus 로고
    • Fermentation development of recombinant Pichia pastoris expressing the heterologous gene: Bovine lysozyme
    • 35. Brierley, R. A., Bussineau, C., Kosson, R., Melton, A., and Siegel, R. S. (1990) Fermentation development of recombinant Pichia pastoris expressing the heterologous gene: Bovine lysozyme. Ann. NY Acad. Sci. 589, 350-362.
    • (1990) Ann. NY Acad. Sci. , vol.589 , pp. 350-362
    • Brierley, R.A.1    Bussineau, C.2    Kosson, R.3    Melton, A.4    Siegel, R.S.5
  • 36
    • 0024701067 scopus 로고
    • Methylotrophic yeast Pichia pastoris produced in high-cell-density fermentations with high cell yields as vehicle for recombinant protein production
    • 36. Siegel, R. S., and Brierley, R. A. (1989) Methylotrophic yeast Pichia pastoris produced in high-cell-density fermentations with high cell yields as vehicle for recombinant protein production. Biotechnol. Bioeng. 34, 403-404.
    • (1989) Biotechnol. Bioeng. , vol.34 , pp. 403-404
    • Siegel, R.S.1    Brierley, R.A.2
  • 37
    • 0023234256 scopus 로고
    • High-level expression and efficient assembly of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris
    • 37. Cregg, J. M., et al. (1987) High-level expression and efficient assembly of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris. Bio/Technology 5, 479-485.
    • (1987) Bio/Technology , vol.5 , pp. 479-485
    • Cregg, J.M.1
  • 38
    • 0023693630 scopus 로고
    • High level expression, purification and characterization of human tumor necrosis factor synthesized in the methylotrophic yeast Pichia pastoris
    • 38. Sreekrishna, K., et al. (1989) High level expression, purification and characterization of human tumor necrosis factor synthesized in the methylotrophic yeast Pichia pastoris. J. Basic Microbiol. 28, 265-278.
    • (1989) J. Basic Microbiol. , vol.28 , pp. 265-278
    • Sreekrishna, K.1
  • 39
    • 14744271884 scopus 로고
    • High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene
    • 39. Clare, J. J., Rayment, F. B., Ballantine, S. P., Sreekrishna, K., and Romanos, M. A. (1991) High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene. Bio/Technology 9, 455-460.
    • (1991) Bio/Technology , vol.9 , pp. 455-460
    • Clare, J.J.1    Rayment, F.B.2    Ballantine, S.P.3    Sreekrishna, K.4    Romanos, M.A.5
  • 40
    • 0025285067 scopus 로고
    • Cotranslational amino-terminal processing
    • 40. Kendall, R. L., Yamada, R., and Bradshaw, R. A. (1990) Cotranslational amino-terminal processing. Meth. Enzymol. 185, 398-407.
    • (1990) Meth. Enzymol. , vol.185 , pp. 398-407
    • Kendall, R.L.1    Yamada, R.2    Bradshaw, R.A.3
  • 41
    • 14744299579 scopus 로고
    • Recent advances in expression of foreign genes in Pichia pastoris
    • 41. Cregg, J. M., Vedvick, T. S., and Rascke, W. C. (1993) Recent advances in expression of foreign genes in Pichia pastoris. Biol Technology 11, 905-910.
    • (1993) Bio/Technology , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Rascke, W.C.3


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