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Volumn 370, Issue 2, 2003, Pages 651-659

Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima

Author keywords

Pectate lyase; Pectin; Pectinase; Thermostable; Thermotoga

Indexed keywords

CALCIUM; CATALYST ACTIVITY; ENZYMES; ESCHERICHIA COLI; FILTRATION; GENES; ORGANIC ACIDS; POTASSIUM;

EID: 0242417644     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021595     Document Type: Article
Times cited : (55)

References (45)
  • 1
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita, N. C. and Gibeaut, D. M. (1993) Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant Rev. 3, 1-30
    • (1993) Plant Rev. , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 2
    • 0027818642 scopus 로고
    • Pectin, pectinase and protopectinase: Production, properties, and applications
    • Sakai, T., Sakamoto, T., Hallaert, J. and Vandamme, E. J. (1993) Pectin, pectinase and protopectinase: production, properties, and applications. Adv. Appl. Microbiol. 39, 213-294
    • (1993) Adv. Appl. Microbiol. , vol.39 , pp. 213-294
    • Sakai, T.1    Sakamoto, T.2    Hallaert, J.3    Vandamme, E.J.4
  • 3
    • 0035191237 scopus 로고    scopus 로고
    • Applications of pectinases in the commercial sector: A review
    • Kashyap, D. R., Vohra, P. K., Chopra, S. and Tewari, R. (2001) Applications of pectinases in the commercial sector: a review. Bioresour. Technol. 77, 215-227
    • (2001) Bioresour. Technol. , vol.77 , pp. 215-227
    • Kashyap, D.R.1    Vohra, P.K.2    Chopra, S.3    Tewari, R.4
  • 4
    • 0031917790 scopus 로고    scopus 로고
    • Caldicellulosiruptor owensensis sp. nov., an anaerobic, extremely thermophilic, xylanolytic bacterium
    • Huang, C.-Y., Patel, B. K., Mah, R. A. and Baresi, L. (1998) Caldicellulosiruptor owensensis sp. nov., an anaerobic, extremely thermophilic, xylanolytic bacterium. Int. J. Syst. Bacteriol. 48, 91-97
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 91-97
    • Huang, C.-Y.1    Patel, B.K.2    Mah, R.A.3    Baresi, L.4
  • 5
    • 0033022027 scopus 로고    scopus 로고
    • Caldicellulosiruptor kristjanssonii sp. nov., a cellulolytic, extremely thermophilic, anaerobic bacterium
    • Bredholt, S., Sonne-Hansen, J., Nielsen, P., Mathrani, I. M. and Ahring, B. K. (1999) Caldicellulosiruptor kristjanssonii sp. nov., a cellulolytic, extremely thermophilic, anaerobic bacterium. Int. J. Syst. Bacteriol. 49, 991-996
    • (1999) Int. J. Syst. Bacteriol. , vol.49 , pp. 991-996
    • Bredholt, S.1    Sonne-Hansen, J.2    Nielsen, P.3    Mathrani, I.M.4    Ahring, B.K.5
  • 7
    • 0018725972 scopus 로고
    • Isolation from soil and properties of the extreme thermophile Clostridium thermohydrosulfuricum
    • Wiegel, J., Ljungdahl, L. G. and Rawson, J. R. (1979) Isolation from soil and properties of the extreme thermophile Clostridium thermohydrosulfuricum. J. Bacteriol. 139, 800-810
    • (1979) J. Bacteriol. , vol.139 , pp. 800-810
    • Wiegel, J.1    Ljungdahl, L.G.2    Rawson, J.R.3
  • 8
    • 0020533180 scopus 로고
    • Characterization of pectinolytic enzymes of Clostridium thermosulfurogenes
    • Schink, B. and Zeikus, J. G. (1983) Characterization of pectinolytic enzymes of Clostridium thermosulfurogenes. FEMS Microbiol. Lett. 17, 295-298
    • (1983) FEMS Microbiol. Lett. , vol.17 , pp. 295-298
    • Schink, B.1    Zeikus, J.G.2
  • 9
    • 0002163252 scopus 로고
    • Characteristics of Desulfurococcus amyloliticus sp. nov., a new extremely thermophilic archaebacterium isolated from thermal springs of Kamchatka and Kunashir Island
    • Bonch-Osmolovskaya, E. A., Slesarev, A. I., Miroshnichenko, M. L., Svetlichnaya, T. P. and Alekseev, V. A. (1988) Characteristics of Desulfurococcus amyloliticus sp. nov., a new extremely thermophilic archaebacterium isolated from thermal springs of Kamchatka and Kunashir Island. Mikrobiologiya 57, 94-101
    • (1988) Mikrobiologiya , vol.57 , pp. 94-101
    • Bonch-Osmolovskaya, E.A.1    Slesarev, A.I.2    Miroshnichenko, M.L.3    Svetlichnaya, T.P.4    Alekseev, V.A.5
  • 10
    • 0031267241 scopus 로고    scopus 로고
    • Purification and characterization of thermostable pectate-lyases from a newly isolated thermophilic bacterium, Thermoanaerobacter italicus sp. nov.
    • Kozianowski, G., Canganella, F., Rainey, F. A., Hippe, H. and Antranikian, G. (1997) Purification and characterization of thermostable pectate-lyases from a newly isolated thermophilic bacterium, Thermoanaerobacter italicus sp. nov. Extremophiles 1, 171-182
    • (1997) Extremophiles , vol.1 , pp. 171-182
    • Kozianowski, G.1    Canganella, F.2    Rainey, F.A.3    Hippe, H.4    Antranikian, G.5
  • 11
    • 0034328744 scopus 로고    scopus 로고
    • Purification and characterization of thermostable pectate lyase with protopectinase activity from thermophilic Bacillus sp. TS 47
    • Takao, M., Nakaniwa, T., Yoshikawa, K., Terashita, T. and Sakai, T. (2000) Purification and characterization of thermostable pectate lyase with protopectinase activity from thermophilic Bacillus sp. TS 47. Biosci. Biotechnol. Biochem. 64, 2360-2367
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 2360-2367
    • Takao, M.1    Nakaniwa, T.2    Yoshikawa, K.3    Terashita, T.4    Sakai, T.5
  • 12
    • 0036154307 scopus 로고    scopus 로고
    • Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides
    • Chhabra, S. R., Shockley, K. R., Ward, D. E. and Kelly, R. M. (2002) Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides. Appl. Environ. Microbiol. 68, 545-554
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 545-554
    • Chhabra, S.R.1    Shockley, K.R.2    Ward, D.E.3    Kelly, R.M.4
  • 13
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 °C
    • Huber, R., Langworthy, T. A., König, H., Thomm, M., Woese, C. R., Sleytr, U. B. and Stetter, K. O. (1986) Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 °C. Arch. Microbiol. 144, 324-333
    • (1986) Arch. Microbiol. , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.A.2    König, H.3    Thomm, M.4    Woese, C.R.5    Sleytr, U.B.6    Stetter, K.O.7
  • 14
    • 0001846919 scopus 로고
    • The order Thermotogales
    • Balows, A., et al., eds., Springer, Berlin, Heidelberg, New York
    • Huber, R. and Stetter, K. O. (1992) The order Thermotogales. In The Prokaryotes (Balows, A., et al., eds.), pp. 3809-3815, Springer, Berlin, Heidelberg, New York
    • (1992) The Prokaryotes , pp. 3809-3815
    • Huber, R.1    Stetter, K.O.2
  • 16
    • 0018937137 scopus 로고
    • Characterization of an acetate-decarboxylating, non-hydrogen-oxidizing methane bacterium
    • Zehnder, A. J. B., Huser, B. A., Brock, T. D. and Wuhrmann, K. (1980) Characterization of an acetate-decarboxylating, non-hydrogen-oxidizing methane bacterium. Arch. Microbiol. 124, 1-11
    • (1980) Arch. Microbiol. , vol.124 , pp. 1-11
    • Zehnder, A.J.B.1    Huser, B.A.2    Brock, T.D.3    Wuhrmann, K.4
  • 17
    • 0027465230 scopus 로고
    • Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen, S. W. M., Luesink, E. J., Stams, A. J. M. and Zehnder, A. J. B. (1993) Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur. J. Biochem. 213, 305-312
    • (1993) Eur. J. Biochem. , vol.213 , pp. 305-312
    • Kengen, S.W.M.1    Luesink, E.J.2    Stams, A.J.M.3    Zehnder, A.J.B.4
  • 18
    • 0003048982 scopus 로고
    • Preparation of genomic DNA from sulfur-dependent hyperthermophilic Archaea
    • Robb, F. T. and Place. A. R., eds., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Ramakrishnan, V. and Adams, M. W. W. (1995) Preparation of genomic DNA from sulfur-dependent hyperthermophilic Archaea. In Archaea, A Laboratory Manual: Thermophiles (Robb, F. T. and Place. A. R., eds.), pp. 95-96, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1995) Archaea, A Laboratory Manual: Thermophiles , pp. 95-96
    • Ramakrishnan, V.1    Adams, M.W.W.2
  • 23
    • 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 (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0034985962 scopus 로고    scopus 로고
    • Assaying activity and assessing thermostability of hyperthermophilic enzymes
    • Daniel, R. M. and Danson, M. J. (2001) Assaying activity and assessing thermostability of hyperthermophilic enzymes. Methods Enzymol. 334, 283-293
    • (2001) Methods Enzymol. , vol.334 , pp. 283-293
    • Daniel, R.M.1    Danson, M.J.2
  • 27
    • 0033728460 scopus 로고    scopus 로고
    • Esterification and glycosydation of oligogalacturonides: Examination of the reaction products using MALDI-TOF MS and HPAEC
    • van Alebeek, G.-J. W. M., Zabotina, O., Beldman, G., Schols, H. A. and Voragen, A. G. J. (2000) Esterification and glycosydation of oligogalacturonides: examination of the reaction products using MALDI-TOF MS and HPAEC. Carbohydr. Polym. 43, 39-46
    • (2000) Carbohydr. Polym. , vol.43 , pp. 39-46
    • Van Alebeek, G.-J.W.M.1    Zabotina, O.2    Beldman, G.3    Schols, H.A.4    Voragen, A.G.J.5
  • 28
    • 0034171340 scopus 로고    scopus 로고
    • Analysis of the genome of an alkaliphilic Bacillus strain from an industrial point of view
    • Takami, H. and Horikoshi, K. (2000) Analysis of the genome of an alkaliphilic Bacillus strain from an industrial point of view. Extremophiles 4, 99-108
    • (2000) Extremophiles , vol.4 , pp. 99-108
    • Takami, H.1    Horikoshi, K.2
  • 29
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14, 4683-4690
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 31
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J., Milpetz, F., Bork, P. and Ponting, C. P. (1998) SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. U.S.A. 95, 5857-5864
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 32
    • 0031570284 scopus 로고    scopus 로고
    • Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases
    • Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R. and Jenkins, J. (1997) Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. Structure 5, 677-689
    • (1997) Structure , vol.5 , pp. 677-689
    • Mayans, O.1    Scott, M.2    Connerton, I.3    Gravesen, T.4    Benen, J.5    Visser, J.6    Pickersgill, R.7    Jenkins, J.8
  • 35
    • 0027039394 scopus 로고
    • Improvement of the selective depolymerization of pectic substances by chemical β-elimination in aqueous solution
    • Kravtchenko, T. P., Arnould, I., Voragen, A. G. J. and Pilnik, W. (1992) Improvement of the selective depolymerization of pectic substances by chemical β-elimination in aqueous solution. Carbohydr. Polym. 19, 237-242
    • (1992) Carbohydr. Polym. , vol.19 , pp. 237-242
    • Kravtchenko, T.P.1    Arnould, I.2    Voragen, A.G.J.3    Pilnik, W.4
  • 37
    • 0032988009 scopus 로고    scopus 로고
    • The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937
    • Shevchik, V. E., Condemine, G, Robert-Baudouy, J. and Hugouvieux-Cotte-Pattat, N. (1999) The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. J. Bacteriol. 181, 3912-3919
    • (1999) J. Bacteriol. , vol.181 , pp. 3912-3919
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3    Hugouvieux-Cotte-Pattat, N.4
  • 40
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Veille, C. and Zeikus, G. J. (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microb. Mol. Biol. Rev. 65, 1-43
    • (2001) Microb. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Veille, C.1    Zeikus, G.J.2
  • 41
    • 0030944441 scopus 로고    scopus 로고
    • Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: Enzyme characteristics and potential inhibitors
    • Tardy, F., Nasser, W., Robert-Baudouy, J. and Hugouvieux-Cotte-Pattat, N. (1997) Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: enzyme characteristics and potential inhibitors. J. Bacteriol. 179, 2503-2511
    • (1997) J. Bacteriol. , vol.179 , pp. 2503-2511
    • Tardy, F.1    Nasser, W.2    Robert-Baudouy, J.3    Hugouvieux-Cotte-Pattat, N.4
  • 42
    • 0035257544 scopus 로고    scopus 로고
    • Cloning of two pectate lyase genes from the marine Antarctic bacterium Pseudoalteromonas haloplanktis strain ANT/505 and characterization of the enzymes
    • Truong, L. V., Tuyen, H., Helmke, E., Binh, L. T. and Schweder, T. (2001) Cloning of two pectate lyase genes from the marine Antarctic bacterium Pseudoalteromonas haloplanktis strain ANT/505 and characterization of the enzymes. Extremophiles 5, 35-44
    • (2001) Extremophiles , vol.5 , pp. 35-44
    • Truong, L.V.1    Tuyen, H.2    Helmke, E.3    Binh, L.T.4    Schweder, T.5
  • 43
    • 0034571727 scopus 로고    scopus 로고
    • Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: Its catalytic properties and deduced amino acid sequence
    • Kobayashi, T., Hatada, Y., Suzumatsu, A., Saeki, K., Hakamada, Y. and Ito, S. (2000) Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: its catalytic properties and deduced amino acid sequence. Extremophiles 4, 377-383
    • (2000) Extremophiles , vol.4 , pp. 377-383
    • Kobayashi, T.1    Hatada, Y.2    Suzumatsu, A.3    Saeki, K.4    Hakamada, Y.5    Ito, S.6
  • 44
  • 45
    • 0029257437 scopus 로고
    • Functional implications of structure based sequence alignment of proteins in the extracellular pectate lyase superfamily
    • Henrissat, B., Heffron, S. E., Yoder, M. D., Lietzke, S. E. and Jurnak, F. (1995) Functional implications of structure based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiol. 107, 963-976
    • (1995) Plant Physiol. , vol.107 , pp. 963-976
    • Henrissat, B.1    Heffron, S.E.2    Yoder, M.D.3    Lietzke, S.E.4    Jurnak, F.5


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