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Volumn 153, Issue 7, 2007, Pages 2116-2125

A novel type of subtilase from the psychrotolerant bacterium Pseudoalteromonas sp. SM9913: Catalytic and structural properties of deseasin MCP-01

Author keywords

[No Author keywords available]

Indexed keywords

DESEASIN; PROTEINASE; SERINE PROTEINASE; SERINE PROTEINASE MCP 01; UNCLASSIFIED DRUG;

EID: 34447511576     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.2007/006056-0     Document Type: Article
Times cited : (57)

References (38)
  • 1
    • 0029820612 scopus 로고    scopus 로고
    • Cloning, DNA sequencing and expression of the gene encoding Clostridium thermocellum cellulose Cell, the largest catalytic component of the cellulosome
    • Ahsan, M. M., Kimura, T., Karita, S., Sakka, K. & Ohmiya, K. (1996). Cloning, DNA sequencing and expression of the gene encoding Clostridium thermocellum cellulose Cell, the largest catalytic component of the cellulosome. J Bacteriol 178, 5732-5740.
    • (1996) J Bacteriol , vol.178 , pp. 5732-5740
    • Ahsan, M.M.1    Kimura, T.2    Karita, S.3    Sakka, K.4    Ohmiya, K.5
  • 2
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen, J. D., Nielsen, H., Von Heijne, G. & Brunak, S. (2004). Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340, 783-795.
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0036868198 scopus 로고    scopus 로고
    • Effects of different buffers on the thermostability and autolysis of a cold-adapted protease MCP-01
    • Chen, X.-L., Sun, C.-Y., Zhang, Y.-Z. & Gao, P.-J. (2002). Effects of different buffers on the thermostability and autolysis of a cold-adapted protease MCP-01. J Protein Chem 21, 523-527.
    • (2002) J Protein Chem , vol.21 , pp. 523-527
    • Chen, X.-L.1    Sun, C.-Y.2    Zhang, Y.-Z.3    Gao, P.-J.4
  • 5
    • 0345530905 scopus 로고    scopus 로고
    • Two different proteases produced by a deep-sea psychrotrophic strain Pseudoaltermonas sp. SM9913
    • Chen, X.-L., Zhang, Y.-Z., Gao, P.-J. & Luan, X.-W. (2003a). Two different proteases produced by a deep-sea psychrotrophic strain Pseudoaltermonas sp. SM9913. Marine Biol 143, 989-993.
    • (2003) Marine Biol , vol.143 , pp. 989-993
    • Chen, X.-L.1    Zhang, Y.-Z.2    Gao, P.-J.3    Luan, X.-W.4
  • 6
    • 0142245753 scopus 로고    scopus 로고
    • Rapid monitoring of autolysis process of proteases by capillary electrophoresis
    • Chen, X.-L., Sun, C.-Y., Zhang, Y.-Z. & Gao, P.-J. (2003b). Rapid monitoring of autolysis process of proteases by capillary electrophoresis. Biotechnol Lett 25, 1763-1767.
    • (2003) Biotechnol Lett , vol.25 , pp. 1763-1767
    • Chen, X.-L.1    Sun, C.-Y.2    Zhang, Y.-Z.3    Gao, P.-J.4
  • 7
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • Edited by M. O. Dayhoff. Washington, DC: National Biomedical Research Foundation
    • Dayhoff, M. O., Schwartz, R. M. & Orcult, B. C. (1978). A model of evolutionary change in proteins. In Atlas of Protein Sequence and Structure, pp. 345-358. Edited by M. O. Dayhoff. Washington, DC: National Biomedical Research Foundation.
    • (1978) Atlas of Protein Sequence and Structure , pp. 345-358
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcult, B.C.3
  • 8
    • 0037688133 scopus 로고    scopus 로고
    • Molecular adaptation to cold in psychrophilic enzymes
    • Feller, G. (2003). Molecular adaptation to cold in psychrophilic enzymes. Cell Mol Life Sci 60, 648-662.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 648-662
    • Feller, G.1
  • 10
    • 0028242912 scopus 로고
    • A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal mutation of pro-Kex2 protease
    • Gluschankof, P. & Fuller, R. S. (1994). A C-terminal domain conserved in precursor processing proteases is required for intramolecular N-terminal mutation of pro-Kex2 protease. EMBO J 13, 2280-2288.
    • (1994) EMBO J , vol.13 , pp. 2280-2288
    • Gluschankof, P.1    Fuller, R.S.2
  • 11
    • 0026638586 scopus 로고
    • Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching
    • Grøn, H., Meldal, M. & Breddam, K. (1992). Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching. Biochemistry 31, 6011-6018.
    • (1992) Biochemistry , vol.31 , pp. 6011-6018
    • Grøn, H.1    Meldal, M.2    Breddam, K.3
  • 12
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M. C. (1997). SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 13
    • 34447523626 scopus 로고    scopus 로고
    • Hall, T. A. (1999). BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 41, 95-98.
    • Hall, T. A. (1999). BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 41, 95-98.
  • 14
    • 0142186143 scopus 로고    scopus 로고
    • Taste improvement of refrigerated meat treated with cold-adapted protease
    • He, H., Chen, X., Li, J., Zhang, Y. & Gao, P. (2004). Taste improvement of refrigerated meat treated with cold-adapted protease. Food Chem 84, 307-311.
    • (2004) Food Chem , vol.84 , pp. 307-311
    • He, H.1    Chen, X.2    Li, J.3    Zhang, Y.4    Gao, P.5
  • 15
    • 0023196224 scopus 로고
    • Isolation of a cellodextrinase from Bacteroides succinogenes
    • Huang, L. & Forsberg, C. W. (1987). Isolation of a cellodextrinase from Bacteroides succinogenes. Appl Environ Microbiol 53, 1034-1041.
    • (1987) Appl Environ Microbiol , vol.53 , pp. 1034-1041
    • Huang, L.1    Forsberg, C.W.2
  • 16
    • 0019287872 scopus 로고
    • Thermostability and aliphatic index of globular proteins
    • Ikai, A. (1980). Thermostability and aliphatic index of globular proteins. J Biochem (Tokyo) 88, 1895-1898.
    • (1980) J Biochem (Tokyo) , vol.88 , pp. 1895-1898
    • Ikai, A.1
  • 18
    • 0032975313 scopus 로고    scopus 로고
    • Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain AclO: Gene cloning and enzyme purification and characterization
    • Kulakova, L., Galkin, A., Kurihara, T., Yoshimura, T. & Esaki, N. (1999). Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain AclO: Gene cloning and enzyme purification and characterization. Appl Environ Microbiol 65, 611-617.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 611-617
    • Kulakova, L.1    Galkin, A.2    Kurihara, T.3    Yoshimura, T.4    Esaki, N.5
  • 19
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar, S., Tamura, K. & Nei, M. (2004). MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform 5, 150-163.
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking
    • Liu, Y. G. & Whittier, R. F. (1995). Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25, 674-681.,
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.G.1    Whittier, R.F.2
  • 22
    • 34447536296 scopus 로고    scopus 로고
    • Lund, O., Nielsen, M., Lundegaard, C. & Worning, P. (2002). CPHmodels 2.0: X3M a computer program to extract 3D models. Abstract A102 at the CASP5 Conference, Fifth Community-Wide Experiment on the Critical Assessment of Techniques for Protein Structure Prediction, Pacific Grove, CA, December 2002.
    • Lund, O., Nielsen, M., Lundegaard, C. & Worning, P. (2002). CPHmodels 2.0: X3M a computer program to extract 3D models. Abstract A102 at the CASP5 Conference, Fifth Community-Wide Experiment on the Critical Assessment of Techniques for Protein Structure Prediction, Pacific Grove, CA, December 2002.
  • 23
    • 13444262384 scopus 로고    scopus 로고
    • Marchler-Bauer, A., Anderson, J. B., Cherukuri, P. F., DeWeese-Scott C., Geer, L. Y., Gwadz, M., He, S., Hurwitz, D. I., Jackson, J. D. & other authors (2005). CDD: A conserved domain database for protein classification. Nucleic Acids Res 33, D192-D196.
    • Marchler-Bauer, A., Anderson, J. B., Cherukuri, P. F., DeWeese-Scott C., Geer, L. Y., Gwadz, M., He, S., Hurwitz, D. I., Jackson, J. D. & other authors (2005). CDD: A conserved domain database for protein classification. Nucleic Acids Res 33, D192-D196.
  • 24
  • 25
    • 0036208814 scopus 로고    scopus 로고
    • Molecular analysis of the gene encoding a novel chitin-binding protease from Alteromonas sp. strain O-7 and its role in the chitinolytic system
    • Miyamoto, K, Nukui, E, Itoh, H., Sato, T., Kobayashi, T., Imada, C., Watanabe, E., Inamori, Y. & Tsujibo, H. (2002). Molecular analysis of the gene encoding a novel chitin-binding protease from Alteromonas sp. strain O-7 and its role in the chitinolytic system. J Bacteriol 184, 1865-1872.
    • (2002) J Bacteriol , vol.184 , pp. 1865-1872
    • Miyamoto, K.1    Nukui, E.2    Itoh, H.3    Sato, T.4    Kobayashi, T.5    Imada, C.6    Watanabe, E.7    Inamori, Y.8    Tsujibo, H.9
  • 26
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray, M. G. & Thompson, W. F. (1980). Rapid isolation of high molecular weight plant DNA. Nucleic Acids Res 8, 4321-4325.
    • (1980) Nucleic Acids Res , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 27
    • 0029761009 scopus 로고    scopus 로고
    • Cloning and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Xanthomonas sp. T-22
    • Oda, K., Ito, M., Uchida, K, Shibano, Y., Fukuhara, K. & Takahashi, S. (1996). Cloning and expression of an isovaleryl pepstatin-insensitive carboxyl proteinase gene from Xanthomonas sp. T-22. J Biochem (Tokyo) 120, 564-572.
    • (1996) J Biochem (Tokyo) , vol.120 , pp. 564-572
    • Oda, K.1    Ito, M.2    Uchida, K.3    Shibano, Y.4    Fukuhara, K.5    Takahashi, S.6
  • 28
    • 24044553899 scopus 로고    scopus 로고
    • Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp. strain O-7
    • Orikoshi, H., Nakayama, S., Hanato, C., Miyamoto, K & Tsujibo, H. (2005). Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp. strain O-7. J Appl Microbiol 99, 551-557.
    • (2005) J Appl Microbiol , vol.99 , pp. 551-557
    • Orikoshi, H.1    Nakayama, S.2    Hanato, C.3    Miyamoto, K.4    Tsujibo, H.5
  • 29
    • 0027457249 scopus 로고
    • Some characteristics of a proteinase from a thermophilic Bacillus sp. expressed in Escherichia coli: Comparison with the native enzyme and its processing in E. coli and in vitro
    • Peek, K, Veitch, D. P., Prescott, M., Daniel, R. M., Maciver, B. & Bergquist, P. L. (1993). Some characteristics of a proteinase from a thermophilic Bacillus sp. expressed in Escherichia coli: comparison with the native enzyme and its processing in E. coli and in vitro. Appl Environ Microbiol 59, 1168-1175.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 1168-1175
    • Peek, K.1    Veitch, D.P.2    Prescott, M.3    Daniel, R.M.4    Maciver, B.5    Bergquist, P.L.6
  • 31
    • 34249012881 scopus 로고    scopus 로고
    • Introduction: Serine peptides and their clans
    • 2nd edn, pp, Edited by A. J. Barrett, N. D. Rawlings & J. F. Woessner. London: Elsevier
    • Rawlings, N. D. & Barrett, A. J. (2004). Introduction: Serine peptides and their clans. In Handbook of Proteolytic Enzymes, 2nd edn, pp. 1425-1427. Edited by A. J. Barrett, N. D. Rawlings & J. F. Woessner. London: Elsevier.
    • (2004) Handbook of Proteolytic Enzymes , pp. 1425-1427
    • Rawlings, N.D.1    Barrett, A.J.2
  • 34
    • 0030896832 scopus 로고    scopus 로고
    • Subtilases: The superfamily of subtilisin-like proteases
    • Siezen, R. J. & Leunissen, J. A. M. (1997). Subtilases: The superfamily of subtilisin-like proteases. Protein Sci 6, 501-523.
    • (1997) Protein Sci , vol.6 , pp. 501-523
    • Siezen, R.J.1    Leunissen, J.A.M.2
  • 35
    • 0033544694 scopus 로고    scopus 로고
    • Calcium-mediated thermostability in the subtilisin super-family: The crystal structure of Bacillus Ak.1 protease at 1.8 Å resolution
    • Smith, C. A., Toogood, H. S., Baker, H. M., Daniel, R. M. & Baker, E N. (1999). Calcium-mediated thermostability in the subtilisin super-family: The crystal structure of Bacillus Ak.1 protease at 1.8 Å resolution. J Mol Biol 294, 1027-1040.
    • (1999) J Mol Biol , vol.294 , pp. 1027-1040
    • Smith, C.A.1    Toogood, H.S.2    Baker, H.M.3    Daniel, R.M.4    Baker, E.N.5
  • 36
    • 0029002967 scopus 로고
    • Polycystic kidney disease: The complete structure of the PKD1 gene and its protein
    • The International Polycystic Kidney Disease Consortium
    • The International Polycystic Kidney Disease Consortium (1995). Polycystic kidney disease: The complete structure of the PKD1 gene and its protein. Cell 81, 289-298.
    • (1995) Cell , vol.81 , pp. 289-298
  • 37
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTALX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F. & Higgins, D. G. (1997). The CLUSTALX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25, 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 38
    • 0034663707 scopus 로고    scopus 로고
    • Purification and characterization of Ak.1 protease, a thermostable subtilisin with a disulphide bond in the substrate-birlding cleft
    • Toogood, H. S., Smith, C. A., Baker, E N. & Daniel, R. M. (2000). Purification and characterization of Ak.1 protease, a thermostable subtilisin with a disulphide bond in the substrate-birlding cleft. Biochem J 350, 321-328.
    • (2000) Biochem J , vol.350 , pp. 321-328
    • Toogood, H.S.1    Smith, C.A.2    Baker, E.N.3    Daniel, R.M.4


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