메뉴 건너뛰기




Volumn 60, Issue SUPPL. 16, 2005, Pages 115-121

Relationships between SLH motifs from different glycoside hydrolase families

Author keywords

Alpha amylase family; Glycoside hydrolase; SLH motif

Indexed keywords


EID: 33751339757     PISSN: 13356399     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (10)

References (38)
  • 5
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • BORASTON, A.B., BOLAM, D.N., GILBERT, H.J. & DAVIES, G.J. 2004. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 382: 769-781.
    • (2004) Biochem. J. , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 6
    • 0032839730 scopus 로고    scopus 로고
    • In Thermoanaerobacterium thermosulfurigenes EM1 S-layer homology domains do not attach to peptidoglycan
    • BRECHTEL, E. & BAHL, H. 1999. In Thermoanaerobacterium thermosulfurigenes EM1 S-layer homology domains do not attach to peptidoglycan. J. Bacteriol. 181: 5017-5023.
    • (1999) J. Bacteriol. , vol.181 , pp. 5017-5023
    • Brechtel, E.1    Bahl, H.2
  • 7
    • 0033063644 scopus 로고    scopus 로고
    • Cell wall of Thermoanaerobacterium thermosulfurigenes EM1: Isolation of its components and attachment of the xylanase XynA
    • BRECHTEL, E., MATUSCHEK, M., HELLBERG, A., EGELSEER, E.M., SCHMID, R. & BAHL, H. 1999. Cell wall of Thermoanaerobacterium thermosulfurigenes EM1: isolation of its components and attachment of the xylanase XynA. Arch. Microbiol. 171: 159-165.
    • (1999) Arch. Microbiol. , vol.171 , pp. 159-165
    • Brechtel, E.1    Matuschek, M.2    Hellberg, A.3    Egelseer, E.M.4    Schmid, R.5    Bahl, H.6
  • 8
    • 0346367471 scopus 로고    scopus 로고
    • Expression and characterization of the catalytic domain of an archaeal family 57 pullulanase type II
    • CHANG-PI-HIN, F., ERRA-PUJADA, M., DAUCHEZ, M., DEBEIRE, P., DUCHIRON, F. &. O'DONOHUE, M.J. 2002. Expression and characterization of the catalytic domain of an archaeal family 57 pullulanase type II. Biologia, Bratislava 57 (Suppl. 11): 155-162.
    • (2002) Biologia, Bratislava , vol.57 , Issue.SUPPL. 11 , pp. 155-162
    • Chang-Pi-Hin, F.1    Erra-Pujada, M.2    Dauchez, M.3    Debeire, P.4    Duchiron, F.5    O'Donohue, M.J.6
  • 9
    • 0034979496 scopus 로고    scopus 로고
    • Structure and expression of an amylopullulanase gene from Bacillus stearothermophilus TS-23
    • CHEN, J.T., CHEN, M.C., CHEN, L.L. & CHU, W.S. 2001. Structure and expression of an amylopullulanase gene from Bacillus stearothermophilus TS-23. Biotechnol. Appl. Biochem. 33: 189-199.
    • (2001) Biotechnol. Appl. Biochem. , vol.33 , pp. 189-199
    • Chen, J.T.1    Chen, M.C.2    Chen, L.L.3    Chu, W.S.4
  • 12
    • 0032464347 scopus 로고    scopus 로고
    • Structural research on surface layers: A focus on stability, surface layer homology domains, and surface layer-cell wall interactions
    • ENGELHARDT, H. & PETERS, J. 1998. Structural research on surface layers: a focus on stability, surface layer homology domains, and surface layer-cell wall interactions. J. Struct. Biol. 124: 276-302.
    • (1998) J. Struct. Biol. , vol.124 , pp. 276-302
    • Engelhardt, H.1    Peters, J.2
  • 13
    • 0032908691 scopus 로고    scopus 로고
    • The type II pullulanase of Thermococcus hydrothermalis: Molecular characterization of the gene and expression of the catalytic domain
    • ERRA-PUJADA, M., DEBEIRE, P., DUCHIRON, F. & O'DONOHUE, M.J. 1999. The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain. J. Bacteriol. 181: 3284-3287.
    • (1999) J. Bacteriol. , vol.181 , pp. 3284-3287
    • Erra-Pujada, M.1    Debeire, P.2    Duchiron, F.3    O'Donohue, M.J.4
  • 14
    • 0034876882 scopus 로고    scopus 로고
    • Purification and properties of the catalytic domain of the thermostable pullulanase type II from Thermococcus hydrothermalis
    • ERRA-PUJADA, M., CHANG-PI-HIN, F., DEBEIRE, P., DUCHIRON, F. & O'DONOHUE, M. J. 2001. Purification and properties of the catalytic domain of the thermostable pullulanase type II from Thermococcus hydrothermalis. Biotechnol. Lett. 23: 1273-1277.
    • (2001) Biotechnol. Lett. , vol.23 , pp. 1273-1277
    • Erra-Pujada, M.1    Chang-Pi-Hin, F.2    Debeire, P.3    Duchiron, F.4    O'Donohue, M.J.5
  • 15
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • FELSENSTEIN, J. 1985. Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39: 783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 16
    • 0012286188 scopus 로고    scopus 로고
    • How many conserved sequence regions are there in the α-amylase family?
    • JANECEK, S. 2002. How many conserved sequence regions are there in the α-amylase family? Biologia, Bratislava 57 (Suppl. 11): 29-41.
    • (2002) Biologia, Bratislava , vol.57 , Issue.SUPPL. 11 , pp. 29-41
    • Janecek, S.1
  • 17
    • 0344223437 scopus 로고    scopus 로고
    • The evolution of starch-binding domain
    • JANECEK, S. & SEVCIK, J. 1999. The evolution of starch-binding domain. FEBS Lett. 456: 119-125.
    • (1999) FEBS Lett. , vol.456 , pp. 119-125
    • Janecek, S.1    Sevcik, J.2
  • 18
    • 0037293103 scopus 로고    scopus 로고
    • Relation between domain evolution, specificity, and taxonomy of the α-amylase family members containing a C-terminal starch-binding domain
    • JANECEK, Š., SVENSSON, B. & MACGREGOR, E.A. 2003. Relation between domain evolution, specificity, and taxonomy of the α-amylase family members containing a C-terminal starch-binding domain. Eur. J. Biochem. 270: 635-645.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 635-645
    • Janecek, Š.1    Svensson, B.2    MacGregor, E.A.3
  • 19
    • 0028146782 scopus 로고
    • Cloning of the aapT gene and characterization of its product, α-amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601
    • LEE, S.P., MORIKAWA, M., TAKAGI, M. & IMANAKA, T. 1994. Cloning of the aapT gene and characterization of its product, α-amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601. Appl. Environ. Microbiol. 60: 3764-3773.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3764-3773
    • Lee, S.P.1    Morikawa, M.2    Takagi, M.3    Imanaka, T.4
  • 20
    • 0029000658 scopus 로고
    • OlpB, a new outer layer protein of Clostridium thermocellum, and binding of its S-layer-like domains to components of the cell envelope
    • LEMAIRE, M., OHAYON, H., GOUNON, P., FUJINO, T. & BÉGUIN, P. 1995. OlpB, a new outer layer protein of Clostridium thermocellum, and binding of its S-layer-like domains to components of the cell envelope. J. Bacteriol. 177: 2451-2459.
    • (1995) J. Bacteriol. , vol.177 , pp. 2451-2459
    • Lemaire, M.1    Ohayon, H.2    Gounon, P.3    Fujino, T.4    Béguin, P.5
  • 21
    • 0028262129 scopus 로고
    • Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis
    • LUPAS, A., ENGELHARDT, H., PETERS, J., SANTARIUS, U., VOLKER, S. & BAUMEISTER, W. 1994. Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis. J. Bacteriol. 176: 1224-1233.
    • (1994) J. Bacteriol. , vol.176 , pp. 1224-1233
    • Lupas, A.1    Engelhardt, H.2    Peters, J.3    Santarius, U.4    Volker, S.5    Baumeister, W.6
  • 22
    • 33745853308 scopus 로고    scopus 로고
    • An overview of clan GH-H and distantly-related families
    • MACGREGOR, E.A. 2005. An overview of clan GH-H and distantly-related families. Biologia, Bratislava 60 (Suppl. 16): 5-12.
    • (2005) Biologia, Bratislava , vol.60 , Issue.SUPPL. 16 , pp. 5-12
    • MacGregor, E.A.1
  • 23
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the α-amylase family of enzymes
    • MACGREGOR, E.A., JANECEK, S. & SVENSSON, B. 2001. Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim Biophys Acta 1546: 1-20.
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 1-20
    • MacGregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 24
    • 0028321448 scopus 로고
    • Pullulanase of Thermoanaerobacterium thermosulfurigenes EM1 (Clostridium thermosulfurogenes): Molecular analysis of the gene, composite structure of the enzyme, and a common model for its attachment to the cell surface
    • MATUSCHEK, M., BURCHHARDT, G., SAHM, K. & BAHL, H. 1994. Pullulanase of Thermoanaerobacterium thermosulfurigenes EM1 (Clostridium thermosulfurogenes): molecular analysis of the gene, composite structure of the enzyme, and a common model for its attachment to the cell surface. J. Bacteriol. 176: 3295-3302.
    • (1994) J. Bacteriol. , vol.176 , pp. 3295-3302
    • Matuschek, M.1    Burchhardt, G.2    Sahm, K.3    Bahl, H.4
  • 25
    • 0029853345 scopus 로고    scopus 로고
    • Characterization of genes from Thermoanaerobacterium thermosulfurigenes EM1 that encode two glycosyl hydrolases with conserved S-layer-like domains
    • MATUSCHEK, M., SAHM, K., ZIBAT, A. & BAHL, H. 1996. Characterization of genes from Thermoanaerobacterium thermosulfurigenes EM1 that encode two glycosyl hydrolases with conserved S-layer-like domains. Mol. Gen. Genet. 252: 493-496.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 493-496
    • Matuschek, M.1    Sahm, K.2    Zibat, A.3    Bahl, H.4
  • 26
    • 0032952678 scopus 로고    scopus 로고
    • Production and cell surface anchoring of functional fusions between the SLH motifs of the Bacillus anthracis S-layer proteins and the Bacillus subtilis levansucrase
    • MESNAGE, S., TOSI-COUTURE, E. & FOUET, A. 1999. Production and cell surface anchoring of functional fusions between the SLH motifs of the Bacillus anthracis S-layer proteins and the Bacillus subtilis levansucrase. Mol. Microbiol. 31: 927-936.
    • (1999) Mol. Microbiol. , vol.31 , pp. 927-936
    • Mesnage, S.1    Tosi-Couture, E.2    Fouet, A.3
  • 27
    • 0034283014 scopus 로고    scopus 로고
    • Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation
    • MESNAGE, S., FONTAINE, T., MIGNOT, T., DELEPIERRE, M., MOCK, M. & FOUET, A. 2000. Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation. EMBO J. 19: 4473-4484.
    • (2000) EMBO J. , vol.19 , pp. 4473-4484
    • Mesnage, S.1    Fontaine, T.2    Mignot, T.3    Delepierre, M.4    Mock, M.5    Fouet, A.6
  • 28
    • 33751341506 scopus 로고    scopus 로고
    • Three-dimensional structure of glucodextranase, a glycoside hydrolase family 15 enzyme
    • MIZUNO, M., TONOZUKA, T., ICHIKAWA, K., KAMITORI, S., NISHIKAWA, A. & SAKANO, Y. 2005. Three-dimensional structure of glucodextranase, a glycoside hydrolase family 15 enzyme. Biologia, Bratislava 60 (Suppl. 16): 171-177.
    • (2005) Biologia, Bratislava , vol.60 , Issue.SUPPL. 16 , pp. 171-177
    • Mizuno, M.1    Tonozuka, T.2    Ichikawa, K.3    Kamitori, S.4    Nishikawa, A.5    Sakano, Y.6
  • 30
    • 0030203863 scopus 로고    scopus 로고
    • TREEVIEW: An application to display phylogenetic trees on personal computers
    • PAGE, R.D. 1996. TREEVIEW: an application to display phylogenetic trees on personal computers. Comput. Applic. Biosci. 12: 357-358.
    • (1996) Comput. Applic. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 31
    • 0024467302 scopus 로고
    • S-layer protein gene of Acetogenium kivui: Cloning and expression in Escherichia coli and determination of the nucleotide sequence
    • PETERS, J., PETERS, M., LOTTSPEICH, F. & BAUMEISTER, W. 1989. S-layer protein gene of Acetogenium kivui: cloning and expression in Escherichia coli and determination of the nucleotide sequence. J. Bacteriol. 171: 6307-6315.
    • (1989) J. Bacteriol. , vol.171 , pp. 6307-6315
    • Peters, J.1    Peters, M.2    Lottspeich, F.3    Baumeister, W.4
  • 33
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • SAITOU, N. & NEI, M. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4: 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 34
    • 4344695274 scopus 로고    scopus 로고
    • Extracellular glycosyl hydrolases from clostridia
    • SCHWARZ, W.H., ZVERLOV, V.V. & BAHL, H. 2004. Extracellular glycosyl hydrolases from clostridia. Adv. Appl. Microbiol. 56: 215-261.
    • (2004) Adv. Appl. Microbiol. , vol.56 , pp. 215-261
    • Schwarz, W.H.1    Zverlov, V.V.2    Bahl, H.3
  • 37
    • 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. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 3242816124 scopus 로고    scopus 로고
    • Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis
    • 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. Eur. J. Biochem. 271: 2863-2872.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2863-2872
    • Zona, R.1    Chang-Pi-Hin, F.2    O'Donohue, M.J.3    Janecek, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.