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Volumn 164, Issue 8, 2011, Pages 1323-1338

Identification and characterization of a novel thermostable gh-57 gene from metagenomic fosmid library of the juan de fuca ridge hydrothemal vent

Author keywords

Amylase; Cloning; Enzyme activity; Gene expression; Glycosidase; Metagenomics; Thermophile

Indexed keywords

AMYLASE ACTIVITY; BLACK SMOKERS; CATALYTIC RESIDUE; CONSERVED REGIONS; GLYCOSIDASES; GLYCOSIDE HYDROLASES; HOMOLOGY MODELING; HYDROTHERMAL VENT; INHIBITORY EFFECT; METAGENOMICS; OPTIMAL TEMPERATURE; PYROCOCCUS HORIKOSHII; RECOMBINANT PROTEIN; SOLUBLE STARCH; THERMOPHILE;

EID: 80052436397     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-011-9215-1     Document Type: Article
Times cited : (34)

References (32)
  • 2
    • 22144492288 scopus 로고    scopus 로고
    • AmyA, an alphaamylase with beta-cyclodextrin-forming activity, and AmyB from the thermoalkaliphilic organism Anaerobranca gottschalkii: Two alpha-amylases adapted to their different cellular localizations
    • Ballschmiter, M., Armbrecht, M., Ivanova, K., Antranikian, G., & Liebl, W. (2005). AmyA, an alphaamylase with beta-cyclodextrin-forming activity, and AmyB from the thermoalkaliphilic organism Anaerobranca gottschalkii: two alpha-amylases adapted to their different cellular localizations. Applied and Environmental Microbiology, 71, 3709-3715.
    • (2005) Applied and Environmental Microbiology , vol.71 , pp. 37093715
    • Ballschmiter, M.1    Armbrecht, M.2    Ivanova, K.3    Antranikian, G.4    Liebl, W.5
  • 3
    • 33644957243 scopus 로고    scopus 로고
    • Identification and characterization of a novel intracellular alkaline alpha-amylase from the hyperthermophilic bacterium maritima MSB8
    • Ballschmiter, M., Futterer, O., & Liebl, W. (2006). Identification and characterization of a novel intracellular alkaline alpha-amylase from the hyperthermophilic bacterium maritima MSB8. Applied and Environmental Microbiology, 72, 2206-2211.
    • (2006) Applied and Environmental Microbiology , vol.72 , pp. 2206-2211
    • Ballschmiter, M.1    Futterer, O.2    Liebl, W.3
  • 6
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases [1]
    • Henrissat, B., & Bairoch, A. (1996). Updating the sequence-based classification of glycosyl hydrolases. The Biochemical Journal, 316, 695-696. (Pubitemid 26182174)
    • (1996) Biochemical Journal , vol.316 , Issue.2 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 8
    • 0035899987 scopus 로고    scopus 로고
    • Identification of the catalytic residue of Thermococcus litoralis 4-glucanotransferase through mechanism-based labeling
    • DOI 10.1021/bi011017c
    • Imamura, H., Fushinobu, S., Jeon, B. S., Wakagi, T., & Matsuzawa, H. (2001). Identification of the catalytic residue of Thermococcus litoralis 4-alpha-glucanotransferase through mechanism-based labeling. Biochemistry, 40, 12400-12406. (Pubitemid 32959763)
    • (2001) Biochemistry , vol.40 , Issue.41 , pp. 12400-12406
    • Imamura, H.1    Fushinobu, S.2    Jeon, B.-S.3    Wakagi, T.4    Matsuzawa, H.5
  • 9
    • 0038143285 scopus 로고    scopus 로고
    • Crystal structures of 4-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor
    • DOI 10.1074/jbc.M213134200
    • Imamura, H., Fushinobu, S., Yamamoto, M., Kumasaka, T., Jeon, B. S., Wakagi, T., et al. (2003). Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor. The Journal of Biological Chemistry, 278, 19378-19386. (Pubitemid 36799333)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.21 , pp. 19378-19386
    • Imamura, H.1    Fushinobu, S.2    Yamamoto, M.3    Kumasaka, T.4    Jeon, B.-S.5    Wakagi, T.6    Matsuzawa, H.7
  • 10
    • 0031604393 scopus 로고    scopus 로고
    • Sequence of Archaeal Methanococcus jannaschii Amylase Contains Features of Families 13 and of Glycosyl Hydrolases: A Trace of Their Common Ancestor?
    • Janecek, S. (1998). Sequence of archaeal Methanococcus jannaschii alpha-amylase contains features of families 13 and 57 of glycosyl hydrolases: a trace of their common ancestor? Folia Microbiol. (Praha), 43, 123-128. (Pubitemid 128441351)
    • (1998) Folia Microbiologica , vol.43 , Issue.2 , pp. 123-128
    • Janecek, S.1
  • 11
    • 0012286188 scopus 로고    scopus 로고
    • How many conserved sequence regions are there in the amylase family?
    • Janeček Š. (2002). How many conserved sequence regions are there in the α-amylase family? Biologia Bratislava, 57, 29-41. (Pubitemid 135713689)
    • (2002) Biologia - Section Cellular and Molecular Biology , vol.57 , Issue.SUPPL. 11 , pp. 29-41
    • Janecek, S.1
  • 12
    • 33748670795 scopus 로고    scopus 로고
    • Amylolytic families of glycoside hydrolases: Focus on the family GH-57
    • Janeček Š. (2005). Amylolytic families of glycoside hydrolases: focus on the family GH-57. Biologia Bratislava, 60, 177-184. (Pubitemid 44804913)
    • (2005) Biologia - Section Cellular and Molecular Biology , vol.60 , Issue.SUPPL. 16 , pp. 177-184
    • Janecek, S.1
  • 13
    • 0030738673 scopus 로고    scopus 로고
    • 4-Glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis. Enzyme purification and characterization, and gene cloning, sequencing and expression in Escherichia coli
    • Jeon, B. S., Taguchi, H., Sakai, H., Ohshima, T., Wakagi, T., & Matsuzawa, H. (1997). 4-Alphaglucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis.enzyme purification and characterization, and gene cloning, sequencing and expression in Escherichia coli. European Journal of Biochemistry, 248, 171-178. (Pubitemid 27356985)
    • (1997) European Journal of Biochemistry , vol.248 , Issue.1 , pp. 171-178
    • Jeon, B.-S.1    Taguchi, H.2    Sakai, H.3    Ohshima, T.4    Wakagi, T.5    Matsuzawa, H.6
  • 16
    • 34347214255 scopus 로고    scopus 로고
    • Growth history of a diffusely venting sulfide structure from the Juan de Fuca Ridge: A petrological and geochemical study
    • doi:10.1029/2005GC001166
    • Kristall, B., Kelley, D. S., Hannington, M. D., & Delaney, J. R. (2006). Growth history of a diffusely venting sulfide structure from the Juan de Fuca Ridge: a petrological and geochemical study. Geochemistry, Geophysics, Geosystems, 7, Q07001. doi:10.1029/2005GC001166.
    • (2006) Geochemistry, Geophysics, Geosystems , vol.7
    • Kristall, B.1    Kelley, D.S.2    Hannington, M.D.3    Delaney, J.R.4
  • 17
    • 10744220908 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable intracellular amylase gene from the hyperthermophilic bacterium Thermotoga maritima MSB8
    • DOI 10.1016/j.resmic.2003.09.005
    • Lim, W. J., Park, S. R., An, C. L., Lee, J. Y., Hong, S. Y., Shin, E. C., et al. (2003). Cloning and characterization of a thermostable intracellular alpha-amylase gene from the hyperthermophilic bacterium Thermotoga maritima MSB8. Research in Microbiology, 154, 681-687. (Pubitemid 37487875)
    • (2003) Research in Microbiology , vol.154 , Issue.10 , pp. 681-687
    • Lim, W.J.1    Park, S.R.2    An, C.L.3    Lee, J.Y.4    Hong, S.Y.5    Shin, E.C.6    Kim, E.J.7    Kim, J.O.8    Kim, H.9    Yun, H.D.10
  • 20
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein domain annotations on the fly
    • DOI 10.1093/nar/gkh454
    • Marchler-Bauer, A., & Bryant, S. H. (2004). CD-Search: protein domain annotations on the fly. Nucleic Acids Research, 32, W327.W331. (Pubitemid 38997352)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 21
    • 33748668694 scopus 로고    scopus 로고
    • A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • DOI 10.1128/JB.00390-06
    • Murakami, T., Kanai, T., Takata, H., Kuriki, T., & Imanaka, T. (2006). A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. Journal of Bacteriology, 188, 5915-5924. (Pubitemid 44384100)
    • (2006) Journal of Bacteriology , vol.188 , Issue.16 , pp. 5915-5924
    • Murakami, T.1    Kanai, T.2    Takata, H.3    Kuriki, T.4    Imanaka, T.5
  • 23
    • 34250639490 scopus 로고    scopus 로고
    • Metagenomics, biotechnology with non-culturable microbes
    • DOI 10.1007/s00253-007-0945-5
    • Schmeisser, C., Steele, H., & Streit, W. R. (2007). Metagenomics, biotechnology with non-culturable microbes. Applied Microbiology and Biotechnology, 75, 955-962. (Pubitemid 46944554)
    • (2007) Applied Microbiology and Biotechnology , vol.75 , Issue.5 , pp. 955-962
    • Schmeisser, C.1    Steele, H.2    Streit, W.R.3
  • 24
    • 77952879225 scopus 로고    scopus 로고
    • Molecular cloning and characterization of amylase from soil metagenomic library derived from Northwestern Himalayas
    • Sharma, S., Khan, F. G., & Qazi, G. N. (2010). Molecular cloning and characterization of amylase from soil metagenomic library derived from Northwestern Himalayas. Applied Microbiology and Biotechnology, 86, 1821-1828.
    • (2010) Applied Microbiology and Biotechnology , vol.86 , pp. 1821-1828
    • Sharma, S.1    Khan, F.G.2    Qazi, G.N.3
  • 25
    • 0031300142 scopus 로고    scopus 로고
    • Recombinant approaches for accessing biodiversity
    • Short, J. M. (1997). Recombinant approaches for accessing biodiversity. Nature Biotechnology, 15, 1322-1323.
    • (1997) Nature Biotechnology , vol.15 , pp. 1322-1323
    • Short, J.M.1
  • 26
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994). CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Research, 22, 4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 27
    • 77951978627 scopus 로고    scopus 로고
    • Molecular modeling studies of L-arabinitol 4-dehydrogenase of Hypocrea jecorina: Its binding interactions with substrate and cofactor
    • Tiwari, M., & Lee, J. K. (2010). Molecular modeling studies of L-arabinitol 4-dehydrogenase of Hypocrea jecorina: its binding interactions with substrate and cofactor. Journal of Molecular Graphics & Modelling, 28, 707-713.
    • (2010) Journal of Molecular Graphics & Modelling , vol.28 , pp. 707-713
    • Tiwari, M.1    Lee, J.K.2
  • 30
    • 79951810387 scopus 로고    scopus 로고
    • Comparative metagenomics of microbial communities inhabiting deep-sea hydrothermal vent chimneys with contrasting chemistries
    • doi:10.1038/ismej.2010.1144
    • Xie, W., Wang, F., Guo, L., Chen, Z., Sievert, S. M., Meng, J., et al. (2010). Comparative metagenomics of microbial communities inhabiting deep-sea hydrothermal vent chimneys with contrasting chemistries. The ISME Journal. doi:10.1038/ismej.2010.1144.
    • (2010) The ISME Journal
    • Xie, W.1    Wang, F.2    Guo, L.3    Chen, Z.4    Sievert, S.M.5    Meng, J.6
  • 31
    • 10444244967 scopus 로고    scopus 로고
    • Characterization of a novel amylolytic enzyme encoded by a gene from a soil-derived metagenomic library
    • DOI 10.1128/AEM.70.12.7229-7235.2004
    • Yun, J., Kang, S., Park, S., Yoon, H., Kim, M. J., Heu, S., et al. (2004). Characterization of a novel amylolytic enzyme encoded by a gene from a soil-derived metagenomic library. Applied and Environmental Microbiology, 70, 7229-7235. (Pubitemid 39643787)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.12 , pp. 7229-7235
    • Yun, J.1    Kang, S.2    Park, S.3    Yoon, H.4    Kim, M.-J.5    Heu, S.6    Ryu, S.7
  • 32
    • 3242816124 scopus 로고    scopus 로고
    • Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis
    • DOI 10.1111/j.1432-1033.2004.04144.x
    • Zona, R., Chang-Pi-Hin, F., O'Donohue, M. J., & Janecek, S. (2004). Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis. European Journal of Biochemistry, 271, 2863-2872. (Pubitemid 38980273)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.14 , pp. 2863-2872
    • Zona, R.1    Chang-Pi-Hin, F.2    O'Donohue, M.J.3    Janecek, S.4


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