메뉴 건너뛰기




Volumn 64, Issue 6, 1998, Pages 2152-2157

Enzymological characteristics of the hyperthermostable NAD-dependent glutamate dehydrogenase from the archaeon Pyrobaculum islandicum and effects of denaturants and organic solvents

Author keywords

[No Author keywords available]

Indexed keywords

ACETONITRILE; GUANIDINE; SOLVENT;

EID: 0031744984     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.6.2152-2157.1998     Document Type: Article
Times cited : (59)

References (24)
  • 1
    • 0027487614 scopus 로고
    • Enzymes and proteins from organisms that grow near and above 100°C
    • Adams, M. W. W. 1993. Enzymes and proteins from organisms that grow near and above 100°C. Annu. Rev. Microbiol. 47:627-658.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 627-658
    • Adams, M.W.W.1
  • 2
    • 33751155047 scopus 로고
    • Enzymes from microorganisms in extreme environments
    • Adams, M. W. W., and R. M. Kelly. 1995. Enzymes from microorganisms in extreme environments. Chem. Eng. News 18:32-42.
    • (1995) Chem. Eng. News , vol.18 , pp. 32-42
    • Adams, M.W.W.1    Kelly, R.M.2
  • 4
    • 0345817539 scopus 로고
    • Regeneration of nicotinamide cofactors for use in organic synthesis
    • Chenault, H. K., and G. M. Whitesides. 1987. Regeneration of nicotinamide cofactors for use in organic synthesis. Appl. Biochem. Biotechnol. 14:147-197.
    • (1987) Appl. Biochem. Biotechnol. , vol.14 , pp. 147-197
    • Chenault, H.K.1    Whitesides, G.M.2
  • 5
    • 0026335162 scopus 로고
    • Extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus furiosus
    • Consalvi, T., R. Chiaraluce, L. Politi, R. Vaccaro, M. De Rosa, and R. Scandurra. 1991. Extremely thermostable glutamate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Eur. J. Biochem. 202:1189-1196.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1189-1196
    • Consalvi, T.1    Chiaraluce, R.2    Politi, L.3    Vaccaro, R.4    De Rosa, M.5    Scandurra, R.6
  • 6
    • 0026733875 scopus 로고
    • Enzymes from thermophilic archaebacteria: Current and future applications in biotechnology
    • M. J. Danson, D. W. Hough, and G. G. Lumt (ed.), Portland Press Ltd., London, United Kingdom
    • Cowan, D. A. 1992. Enzymes from thermophilic archaebacteria: current and future applications in biotechnology, p. 149-169. In M. J. Danson, D. W. Hough, and G. G. Lumt (ed.), The archaebacteria: biochemistry and biotechnology, Portland Press Ltd., London, United Kingdom.
    • (1992) The Archaebacteria: Biochemistry and Biotechnology , pp. 149-169
    • Cowan, D.A.1
  • 7
    • 78651153791 scopus 로고
    • Disc electrophoresis. 2. Method and application to human serum proteins
    • Davis, B. J. 1975. Disc electrophoresis. 2. Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121:404-427.
    • (1975) Ann. N. Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 8
    • 0028833474 scopus 로고
    • Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon
    • Diruggiero, J., and F. T. Robb. 1995. Expression and in vitro assembly of recombinant glutamate dehydrogenase from the hyperthermophilic archaeon. Appl. Environ. Microbiol. 61:159-164.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 159-164
    • Diruggiero, J.1    Robb, F.T.2
  • 9
    • 0027440899 scopus 로고
    • The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: Sequence, transcription and analysis of the deduced amino acid sequence
    • Eggen, R. I. L., A. C. M. Geerling, K. Waldkotter, G. Antranikian, and W. M. de Vos. 1993. The glutamate dehydrogenase-encoding gene of the hyperthermophilic archaeon Pyrococcus furiosus: sequence, transcription and analysis of the deduced amino acid sequence. Gene 132:143-148.
    • (1993) Gene , vol.132 , pp. 143-148
    • Eggen, R.I.L.1    Geerling, A.C.M.2    Waldkotter, K.3    Antranikian, G.4    De Vos, W.M.5
  • 10
    • 0017724572 scopus 로고
    • A new spectrophotometric assay to protein in cell extracts
    • Kalb, V. F., and R. W. Bernlohr. 1977. A new spectrophotometric assay to protein in cell extracts. Anal. Biochem. 82:362-371.
    • (1977) Anal. Biochem. , vol.82 , pp. 362-371
    • Kalb, V.F.1    Bernlohr, R.W.2
  • 11
    • 0029153768 scopus 로고
    • Properties of glutamate dehydrogenase and its involvement in alanine production in a hyperthermophilic archaeon, Thermococcus profundus
    • Kobayashi, T., S. Higuchi, K. Kimura, T. Kudo, and K. Horikoshi. 1995. Properties of glutamate dehydrogenase and its involvement in alanine production in a hyperthermophilic archaeon, Thermococcus profundus. J. Biochem. 118:587-592.
    • (1995) J. Biochem. , vol.118 , pp. 587-592
    • Kobayashi, T.1    Higuchi, S.2    Kimura, K.3    Kudo, T.4    Horikoshi, K.5
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0030829444 scopus 로고    scopus 로고
    • Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus
    • Langelandsvik, A. S., I. H. Steen, N. K. Birkeland, and T. Lien. 1997. Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus. Arch. Microbiol. 168:59-67.
    • (1997) Arch. Microbiol. , vol.168 , pp. 59-67
    • Langelandsvik, A.S.1    Steen, I.H.2    Birkeland, N.K.3    Lien, T.4
  • 14
    • 0028069713 scopus 로고
    • Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis
    • Ma, K., F. T. Robb, and M. W. W. Adams. 1994. Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis. Appl. Environ. Microbiol. 60:562-568.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 562-568
    • Ma, K.1    Robb, F.T.2    Adams, M.W.W.3
  • 15
    • 0017897436 scopus 로고
    • Properties of crystalline leucine dehydrogenase from Bacillus sphaericus
    • Ohshima, T., H. Misono, and K. Soda. 1978. Properties of crystalline leucine dehydrogenase from Bacillus sphaericus. J. Biol. Chem. 253:5719-5725.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5719-5725
    • Ohshima, T.1    Misono, H.2    Soda, K.3
  • 16
    • 0022630727 scopus 로고
    • Purification and characterization of malate dehydrogenase from the phototrophic bacterium, Rhodopseudomonas capsulata
    • Ohshima, T., and H. Sakuraba. 1986. Purification and characterization of malate dehydrogenase from the phototrophic bacterium, Rhodopseudomonas capsulata. Biochim. Biophys. Acta 869:171-177.
    • (1986) Biochim. Biophys. Acta , vol.869 , pp. 171-177
    • Ohshima, T.1    Sakuraba, H.2
  • 17
    • 0025617067 scopus 로고
    • Biochemistry and biotechnology of amino acid dehydrogenases
    • Ohshima, T., and K. Soda. 1990. Biochemistry and biotechnology of amino acid dehydrogenases. Adv. Biochem. Eng. Biotechnol. 42:187-189.
    • (1990) Adv. Biochem. Eng. Biotechnol. , vol.42 , pp. 187-189
    • Ohshima, T.1    Soda, K.2
  • 18
    • 0027621232 scopus 로고
    • Purification and properties of extremely thermostable glutamate dehydrogenases from two hyperthermophilic archaebacteria, Pyrococcus woesei and Pyrococcus furiosus
    • Ohshima, T., and N. Nishida. 1993. Purification and properties of extremely thermostable glutamate dehydrogenases from two hyperthermophilic archaebacteria, Pyrococcus woesei and Pyrococcus furiosus. Biosci. Biotechnol. Biochem. 57:945-951.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 945-951
    • Ohshima, T.1    Nishida, N.2
  • 19
    • 84907035928 scopus 로고
    • Purification and characterization of extremely thermostable glutamate dehydrogenase from a hyperthermophilic archaeon, Thermococcus litoralis
    • Ohshima, V., and N. Nishida. 1994. Purification and characterization of extremely thermostable glutamate dehydrogenase from a hyperthermophilic archaeon, Thermococcus litoralis. Biocatalysis 11:117-129.
    • (1994) Biocatalysis , vol.11 , pp. 117-129
    • Ohshima, V.1    Nishida, N.2
  • 20
    • 0026589218 scopus 로고
    • Characterization of an extremely thermostable glutamate dehydrogenase: A key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus
    • Robb, F. T., J. B. Park, and M. W. W. Adams. 1992. Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus. Biochim. Biophys. Acta 1120:267-272.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 267-272
    • Robb, F.T.1    Park, J.B.2    Adams, M.W.W.3
  • 21
    • 0028104704 scopus 로고
    • 2 with sulfur or thiosulfate as electron acceptor in the anaerobic hyperthermophilic archaea Thermoproteus tenax and Pyrobaculum islandicum proceeds via the citric acid cycle
    • 2 with sulfur or thiosulfate as electron acceptor in the anaerobic hyperthermophilic archaea Thermoproteus tenax and Pyrobaculum islandicum proceeds via the citric acid cycle. Arch. Microbiol. 162:286-294.
    • (1994) Arch. Microbiol. , vol.162 , pp. 286-294
    • Seling, M.1    Schoenheit, P.2
  • 22
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C. R., O. Kandler, and M. L. Wheelis. 1990. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl. Acad. Sci. USA 87:4576-4579.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 23
    • 0000251275 scopus 로고
    • Enzyme in synthetic organic chemistry
    • J. E. Baldwin and P. D. Magnum (ed.), Elsevier Science Ltd., Oxford, United Kingdom
    • Wong, C. H., and G. M. Whitesides. 1995. Enzyme in synthetic organic chemistry, p. 131-194. In J. E. Baldwin and P. D. Magnum (ed.), Tetrahedron organic chemistry series. Elsevier Science Ltd., Oxford, United Kingdom.
    • (1995) Tetrahedron Organic Chemistry Series , pp. 131-194
    • Wong, C.H.1    Whitesides, G.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.