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Volumn 51, Issue 6, 2010, Pages 691-696

Peptide synthesis catalysed by a haloalkaliphilic serine protease from the archaeon Natrialba magadii (Nep)

Author keywords

Haloarchaea; Natrialba magadii; Organic solvent; Peptide synthesis; Protease

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CATALYSIS; DIMETHYL SULFOXIDE; ENZYME ACTIVITY; MICROORGANISMS; PEPTIDES; SODIUM CHLORIDE;

EID: 78349293425     PISSN: 02668254     EISSN: 1472765X     Source Type: Journal    
DOI: 10.1111/j.1472-765X.2010.02955.x     Document Type: Article
Times cited : (14)

References (19)
  • 1
    • 85164297955 scopus 로고    scopus 로고
    • The Halohandbook: Protocols for haloarchaeal genetics
    • In, ed. Dyall-Smith, M., last accessed 2008).
    • Allers, T. (2008) Media Recipes from the Thorsten Allers Lab. In The Halohandbook: Protocols for haloarchaeal genetics ed. Dyall-Smith, M. pp. 18-20. (last accessed 2008).
    • (2008) Media Recipes from the Thorsten Allers Lab , pp. 18-20
    • Allers, T.1
  • 2
    • 0037590011 scopus 로고    scopus 로고
    • Extremophiles as a source for novel enzymes
    • Van Den Burg, B. (2003) Extremophiles as a source for novel enzymes. Curr Opin Microbiol 6, 213-218.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 213-218
    • Van Den Burg, B.1
  • 4
    • 50649105260 scopus 로고    scopus 로고
    • Gene cloning and heterologous synthesis of a haloalkaliphilic extracellular protease of Natrialba magadii (Nep)
    • De Castro, R.E., Ruiz, D.M., Gimenez, M.I., Silveyra, M.X., Paggi, R.A. and Maupin-Furlow, J.A. (2008) Gene cloning and heterologous synthesis of a haloalkaliphilic extracellular protease of Natrialba magadii (Nep). Extremophiles 12, 677-687.
    • (2008) Extremophiles , vol.12 , pp. 677-687
    • De Castro, R.E.1    Ruiz, D.M.2    Gimenez, M.I.3    Silveyra, M.X.4    Paggi, R.A.5    Maupin-Furlow, J.A.6
  • 5
    • 0032486568 scopus 로고    scopus 로고
    • Effect of water and enzyme concentration on thermolysin-catalyzed solid-to-solid peptide synthesis
    • Erbeldinger, M., Ni, X. and Halling, P.J. (1998) Effect of water and enzyme concentration on thermolysin-catalyzed solid-to-solid peptide synthesis. Biotechnol Bioeng 59, 68-72.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 68-72
    • Erbeldinger, M.1    Ni, X.2    Halling, P.J.3
  • 6
    • 0034199501 scopus 로고    scopus 로고
    • Extracellular protease of Natrialba magadii: purification and biochemical characterization
    • Gimenez, M.I., Studdert, C.A., Sanchez, J.J. and De Castro, R.E. (2000) Extracellular protease of Natrialba magadii: purification and biochemical characterization. Extremophiles 4, 181-188.
    • (2000) Extremophiles , vol.4 , pp. 181-188
    • Gimenez, M.I.1    Studdert, C.A.2    Sanchez, J.J.3    De Castro, R.E.4
  • 7
    • 0014511920 scopus 로고
    • Effect of salts and organic solvents on the activity of Halobacterium cutirubrum catalase
    • Lanyi, J.K. and Stevenson, J. (1969) Effect of salts and organic solvents on the activity of Halobacterium cutirubrum catalase. J Bacteriol 98, 611-616.
    • (1969) J Bacteriol , vol.98 , pp. 611-616
    • Lanyi, J.K.1    Stevenson, J.2
  • 8
    • 0036006184 scopus 로고    scopus 로고
    • Synthesis of N-protected peptide alcohols catalyzed by subtilisin or alpha-chymotrypsin in organic solvents
    • Liu, P., Tian, G.L., Lo, W.H., Lee, K.S. and Ye, Y.H. (2002) Synthesis of N-protected peptide alcohols catalyzed by subtilisin or alpha-chymotrypsin in organic solvents. Prep Biochem Biotechnol 32, 29-37.
    • (2002) Prep Biochem Biotechnol , vol.32 , pp. 29-37
    • Liu, P.1    Tian, G.L.2    Lo, W.H.3    Lee, K.S.4    Ye, Y.H.5
  • 9
    • 24944510059 scopus 로고    scopus 로고
    • Recent trends in protease-catalyzed peptide synthesis
    • Lombard, C., Saulnier, J. and Wallach, J.M. (2005) Recent trends in protease-catalyzed peptide synthesis. Protein Pept Lett 12, 621-629.
    • (2005) Protein Pept Lett , vol.12 , pp. 621-629
    • Lombard, C.1    Saulnier, J.2    Wallach, J.M.3
  • 10
    • 0036669804 scopus 로고    scopus 로고
    • Extreme halophilic enzymes in organic solvents
    • Marhuenda-Egea, F.C. and Bonete, M.J. (2002) Extreme halophilic enzymes in organic solvents. Curr Opin Biotechnol 13, 385-389.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 385-389
    • Marhuenda-Egea, F.C.1    Bonete, M.J.2
  • 11
    • 43049159548 scopus 로고    scopus 로고
    • Mass spectrometric and kinetic studies on slow progression of papain-catalyzed polymerization of L-glutamic acid diethyl ester
    • Narai-Kanayama, A., Koshino, H. and Aso, K. (2008) Mass spectrometric and kinetic studies on slow progression of papain-catalyzed polymerization of L-glutamic acid diethyl ester. Biochim Biophys Acta 1780, 881-891.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 881-891
    • Narai-Kanayama, A.1    Koshino, H.2    Aso, K.3
  • 13
    • 33846409885 scopus 로고    scopus 로고
    • Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii
    • Ruiz, D.M. and De Castro, R.E. (2007) Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii. J Ind Microbiol Biotechnol 34, 111-115.
    • (2007) J Ind Microbiol Biotechnol , vol.34 , pp. 111-115
    • Ruiz, D.M.1    De Castro, R.E.2
  • 14
    • 0028414129 scopus 로고
    • Catalytic properties and potential of an extracellular protease from an extreme halophile
    • Ryu, K., Kim, J. and Dordick, J.S. (1994) Catalytic properties and potential of an extracellular protease from an extreme halophile. Enzyme Microb Technol 16, 266-275.
    • (1994) Enzyme Microb Technol , vol.16 , pp. 266-275
    • Ryu, K.1    Kim, J.2    Dordick, J.S.3
  • 15
    • 0036890248 scopus 로고    scopus 로고
    • The production of biocatalysts and biomolecules from extremophiles
    • Schiraldi, C. and De Rosa, M. (2002) The production of biocatalysts and biomolecules from extremophiles. Trends Biotechnol 20, 515-521.
    • (2002) Trends Biotechnol , vol.20 , pp. 515-521
    • Schiraldi, C.1    De Rosa, M.2
  • 16
    • 2242477886 scopus 로고    scopus 로고
    • Perspectives on biotechnological applications of archaea
    • Schiraldi, C., Giuliano, M. and De Rosa, M. (2002) Perspectives on biotechnological applications of archaea. Archaea 1, 75-86.
    • (2002) Archaea , vol.1 , pp. 75-86
    • Schiraldi, C.1    Giuliano, M.2    De Rosa, M.3
  • 17
    • 0033199021 scopus 로고    scopus 로고
    • Biocatalysis in organic media using enzymes from extremophiles
    • Sellek, G. and Chaudhuri, J. (1999) Biocatalysis in organic media using enzymes from extremophiles. Enzyme Microb Technol 25, 471-482.
    • (1999) Enzyme Microb Technol , vol.25 , pp. 471-482
    • Sellek, G.1    Chaudhuri, J.2
  • 19
    • 0000491381 scopus 로고
    • Natronobacterium gen.nov. and Natronococcus gen.nov., two genera of haloalcalophilic archaeabacteria
    • Tindall, B.J., Mills, A.A. and Grant, W.D. (1984) Natronobacterium gen.nov. and Natronococcus gen.nov., two genera of haloalcalophilic archaeabacteria. Syst App Microbiol 5, 41-57.
    • (1984) Syst App Microbiol , vol.5 , pp. 41-57
    • Tindall, B.J.1    Mills, A.A.2    Grant, W.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.