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Volumn 178, Issue 1, 1996, Pages 301-305

Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; BACTERIAL ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; RECOMBINANT PROTEIN;

EID: 0030046289     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.1.301-305.1996     Document Type: Article
Times cited : (54)

References (22)
  • 2
    • 0023777735 scopus 로고
    • Tightly regulated tac promoters useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann, E., B. Ochs, and K. J. Abel. 1988. Tightly regulated tac promoters useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 3
    • 0026969319 scopus 로고
    • --dependent alcohol dehydrogenase from Sulfolobus solfataricus: Gene and protein sequence determination and relationship to other alcohol dehydrogenases
    • --dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases Biochemistry 31: 12514-12523.
    • (1992) Biochemistry , vol.31 , pp. 12514-12523
    • Ammendola, S.1    Raia, C.A.2    Caruso, C.3    Camardella, L.4    D'Auria, S.5    De Rosa, M.6    Rossi, M.7
  • 5
    • 0019586165 scopus 로고
    • Mechanism of action of the lexA gene product
    • Brent, R., and M. Ptashne. 1981 Mechanism of action of the lexA gene product Proc. Natl. Acad Sci. USA 78:4204-4208.
    • (1981) Proc. Natl. Acad Sci. USA , vol.78 , pp. 4204-4208
    • Brent, R.1    Ptashne, M.2
  • 7
    • 0026469488 scopus 로고
    • The enzymes from extreme thermophiles: Bacterial sources, thermostabilities and industrial relevance
    • Coolbear, T., R. M. Daniel, and H. W. Morgan. 1992. The enzymes from extreme thermophiles: bacterial sources, thermostabilities and industrial relevance Adv Biochem. Eng. Biotechnol. 45:57-98.
    • (1992) Adv Biochem. Eng. Biotechnol. , vol.45 , pp. 57-98
    • Coolbear, T.1    Daniel, R.M.2    Morgan, H.W.3
  • 8
    • 0026733875 scopus 로고
    • Enzymes from thermophilic archaebacteria: Current and future application in biotechnology
    • Cowan, D. A. 1992. Enzymes from thermophilic archaebacteria: current and future application in biotechnology Biochem. Soc. Symp. 58:149-169.
    • (1992) Biochem. Soc. Symp. , vol.58 , pp. 149-169
    • Cowan, D.A.1
  • 9
    • 77956844355 scopus 로고
    • Archaeal hyperthermophile genes
    • M Kates, D. J. Kushner, and A. T. Matheson (ed.). Elsevier Science Publishers B.V., Amsterdam
    • Dalgaard, J. Z., and R. A. Garrett. 1993. Archaeal hyperthermophile genes. p. 535-563. In M Kates, D. J. Kushner, and A. T. Matheson (ed.), The biochemistry of Archaea (archaebacteria) Elsevier Science Publishers B.V., Amsterdam.
    • (1993) The Biochemistry of Archaea (Archaebacteria) , pp. 535-563
    • Dalgaard, J.Z.1    Garrett, R.A.2
  • 10
    • 0028961231 scopus 로고
    • The purification, cloning and high level expression of a glutaredoxin-like protein from the hyperthermophilic archaeon Pyrococcus furiosus
    • Guagliardi, A., D. de Pascale, R. Cannio, V. Nobile, S. Bartolucci, and M. Rossi. 1995. The purification, cloning and high level expression of a glutaredoxin-like protein from the hyperthermophilic archaeon Pyrococcus furiosus J. Biol. Chem. 270:5748-5755.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5748-5755
    • Guagliardi, A.1    De Pascale, D.2    Cannio, R.3    Nobile, V.4    Bartolucci, S.5    Rossi, M.6
  • 11
    • 0026768866 scopus 로고
    • Element of an archaeal promoter defined by mutational analysis
    • Hain, J., W.-D. Reiter, U. Hüdepohl, and W. Zillig. 1992. Element of an archaeal promoter defined by mutational analysis Nucleic Acids Res. 20: 5423-5428.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5423-5428
    • Hain, J.1    Reiter, W.-D.2    Hüdepohl, U.3    Zillig, W.4
  • 12
    • 85005697480 scopus 로고
    • Dehydrogenases for the synthesis of chiral compounds
    • Hummel, W., and M. R. Kula. 1989. Dehydrogenases for the synthesis of chiral compounds. Eur. J. Biochem. 184:1-13.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 1-13
    • Hummel, W.1    Kula, M.R.2
  • 14
    • 0018234248 scopus 로고
    • Subunit conformation of yeast alcohol dehydrogenase
    • Jörnvall, H., H. Eklund, and C. I. Brändén. 1978. Subunit conformation of yeast alcohol dehydrogenase. J. Biol. Chem. 253:8414-8419.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8414-8419
    • Jörnvall, H.1    Eklund, H.2    Brändén, C.I.3
  • 15
    • 0023411028 scopus 로고
    • Characteristics of alcohol/ polyol dehydrogenases
    • Jornvall, H., B. Persson, and J. Jeffery. 1987 Characteristics of alcohol/ polyol dehydrogenases. Eur. J. Biochem. 167:195-201.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 195-201
    • Jornvall, H.1    Persson, B.2    Jeffery, J.3
  • 16
    • 0021918946 scopus 로고
    • Prediction of chain flexibility in proteins. A tool for the selection of peptide antigens
    • Karplus, P. A., and G. E. Schulz. 1985. Prediction of chain flexibility in proteins. A tool for the selection of peptide antigens. Naturwissenschaften 72:212-213.
    • (1985) Naturwissenschaften , vol.72 , pp. 212-213
    • Karplus, P.A.1    Schulz, G.E.2
  • 17
    • 0001209395 scopus 로고
    • +-dependent alcohol dehydrogenase from Sulfolobus solfataricus: Structural arid functional features
    • +-dependent alcohol dehydrogenase from Sulfolobus solfataricus: structural arid functional features. Biocatalysis 11:143-150.
    • (1994) Biocatalysis , vol.11 , pp. 143-150
    • Raia, C.A.1    H'Auria, S.2    Rossi, M.3
  • 18
    • 77956810681 scopus 로고
    • The structure, function and evolution of archaeal ribosomes
    • M. Kates, D. J. Kushner, and A. T. Matheson (ed.). Elsevier Science Publishers B.V., Amsterdam
    • Ramìrez, C., A. K. E. Köpke, D.-C. Yang, T. Boeckh, and A. T. Matheson. 1993. The structure, function and evolution of archaeal ribosomes, p. 439-466 In M. Kates, D. J. Kushner, and A. T. Matheson (ed.), The biochemistry of Archaea (archaebacteria). Elsevier Science Publishers B.V., Amsterdam.
    • (1993) The Biochemistry of Archaea (Archaebacteria) , pp. 439-466
    • Ramìrez, C.1    Köpke, A.K.E.2    Yang, D.-C.3    Boeckh, T.4    Matheson, A.T.5
  • 19
    • 0025630439 scopus 로고
    • Mutational analysis of an archaebacterial promoter, essential role of a TATA box for transcription efficiency and start site selection in vitro
    • Reiter, W.-D., U. Hüdepohl, and W. Zillig. 1990. Mutational analysis of an archaebacterial promoter, essential role of a TATA box for transcription efficiency and start site selection in vitro. Proc. Natl. Acad. Sci. USA 87: 9509-9513.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9509-9513
    • Reiter, W.-D.1    Hüdepohl, U.2    Zillig, W.3
  • 21
    • 0002437098 scopus 로고
    • Amplification of genomic DNA
    • M A. Innis, D. A. Gelfand, J. J. Sninski, and T. J. White (ed). Academic Press, Inc., San Diego, Calif.
    • Saiki, R. K. 1990. Amplification of genomic DNA, p. 13-20. In M A. Innis, D. A. Gelfand, J. J. Sninski, and T. J. White (ed), PCR protocols. A guide to methods and applications. Academic Press, Inc., San Diego, Calif.
    • (1990) PCR Protocols. A Guide to Methods and Applications , pp. 13-20
    • Saiki, R.K.1


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