메뉴 건너뛰기




Volumn 67, Issue 11, 2003, Pages 2359-2364

A thermostable non-xylanolytic α-glucuronidase of Thermotoga maritima MSB8

Author keywords

Non xylanolytic glucuronidase; p nitrophenyl D glucuronopyranoside hydrolyzing glucuronidase; Thermostable glucuronidase; Thermotoga maritima

Indexed keywords

ESCHERICHIA COLI; THERMOTOGA; THERMOTOGA MARITIMA;

EID: 3042846865     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.67.2359     Document Type: Article
Times cited : (24)

References (25)
  • 1
    • 0032857545 scopus 로고    scopus 로고
    • Cloning of an α-glucosidase gene from Thermococcus hydrothermalis by functional complementation of a Saccharomyces cerevisiae mal11 mutant strain
    • Galichet, A., and Belarbi, A., Cloning of an α-glucosidase gene from Thermococcus hydrothermalis by functional complementation of a Saccharomyces cerevisiae mal11 mutant strain. FEBS Lett., 458, 188-192 (1999).
    • (1999) FEBS Lett. , vol.458 , pp. 188-192
    • Galichet, A.1    Belarbi, A.2
  • 3
    • 0031934403 scopus 로고    scopus 로고
    • Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima
    • Bibel, M., Brettl, C., Gosslar, U., Kriegshäuser, G., and Liebl, W., Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima. FEMS Microbiol. Lett., 158, 9-15 (1998).
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 9-15
    • Bibel, M.1    Brettl, C.2    Gosslar, U.3    Kriegshäuser, G.4    Liebl, W.5
  • 4
    • 0031014417 scopus 로고    scopus 로고
    • Isolation and analysis of a gene encoding α-glucuronidase, an enzyme with a novel primary structure involved in the breakdown of xylan
    • Ruile, P., Winterhalter, C., and Liebl, W., Isolation and analysis of a gene encoding α-glucuronidase, an enzyme with a novel primary structure involved in the breakdown of xylan. Mol. Microbiol., 23, 267-279 (1997).
    • (1997) Mol. Microbiol. , vol.23 , pp. 267-279
    • Ruile, P.1    Winterhalter, C.2    Liebl, W.3
  • 5
    • 0037165613 scopus 로고    scopus 로고
    • Evidence that the putative α-glucosidase of Thermotoga maritima MSB8 is a pNP α-D-glucuronopyranoside hydrolyzing α-glucuronidase
    • Suresh, C., Rus'd, A. A., Kitaoka, M., and Hayashi, K., Evidence that the putative α-glucosidase of Thermotoga maritima MSB8 is a pNP α-D-glucuronopyranoside hydrolyzing α-glucuronidase. FEBS Lett., 517, 159-162 (2002).
    • (2002) FEBS Lett. , vol.517 , pp. 159-162
    • Suresh, C.1    Rus'd, A.A.2    Kitaoka, M.3    Hayashi, K.4
  • 6
    • 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., Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C. Arch. Microbiol., 144, 324-333 (1986).
    • (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
  • 8
    • 0034984373 scopus 로고    scopus 로고
    • Thermostability of proteins from Thermotoga maritima
    • eds. Adams, M. W. W., and Kelly, R. M., Academic Press, San Diego
    • Jaenicke, R., and Böhm, G., Thermostability of proteins from Thermotoga maritima. In "Methods in Enzymology" vol. 334, eds. Adams, M. W. W., and Kelly, R. M., Academic Press, San Diego, pp. 438-469 (2001).
    • (2001) Methods in Enzymology , vol.334 , pp. 438-469
    • Jaenicke, R.1    Böhm, G.2
  • 9
    • 0028924376 scopus 로고
    • Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials
    • Bronnenmeier, K., Kern, A., Liebl, W., and Staudenbauer, W. L., Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials. Appl. Environ. Microbiol., 61, 1399-1407 (1995).
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1399-1407
    • Bronnenmeier, K.1    Kern, A.2    Liebl, W.3    Staudenbauer, W.L.4
  • 10
    • 0026431593 scopus 로고
    • The extremely thermophilic eubacterium, Thermotoga maritima, contains a novel iron-hydrogenase whose cellular activity is dependent upon tungsten
    • Juszczak, A., Aono, S., and Adams, M. W. W., The extremely thermophilic eubacterium, Thermotoga maritima, contains a novel iron-hydrogenase whose cellular activity is dependent upon tungsten. J. Biol. Chem., 266, 13834-13841 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 13834-13841
    • Juszczak, A.1    Aono, S.2    Adams, M.W.W.3
  • 11
    • 0018121934 scopus 로고
    • Refinement of the coomassie blue method of protein quantitation. a simple and linear spectrophotometric assay for ≤0.5 to 50 μg of protein
    • Spector, T., Refinement of the coomassie blue method of protein quantitation. A simple and linear spectrophotometric assay for ≤0.5 to 50 μg of protein. Anal. Biochem., 86, 142-146 (1978).
    • (1978) Anal. Biochem. , vol.86 , pp. 142-146
    • Spector, T.1
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0001253934 scopus 로고
    • The synthesis of aryl glycosiduronic acids
    • Marsh, C. A., and Levvy, G. A., The synthesis of aryl glycosiduronic acids. Biochem. J., 68, 617-621 (1958).
    • (1958) Biochem. J. , vol.68 , pp. 617-621
    • Marsh, C.A.1    Levvy, G.A.2
  • 14
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • eds. Gilbert, H. J., Davies, G., Henrissat, B., and Svensson, B., The Royal Society of Chemistry, Cambridge
    • Coutinho, P. M., and Henrissat, B., Carbohydrate-active enzymes: an integrated database approach. In "Recent Advances in Carbohydrate Bioengineering", eds. Gilbert, H. J., Davies, G., Henrissat, B., and Svensson, B., The Royal Society of Chemistry, Cambridge, pp. 3-12 (1999).
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 15
    • 0020736511 scopus 로고
    • Bioconversion of hemicellulose: Aspects of hemicellulase production by Trichoderma reesei QM 9414 and enzymic saccharification of hemicellulose
    • Dekker, R. F. G., Bioconversion of hemicellulose: aspects of hemicellulase production by Trichoderma reesei QM 9414 and enzymic saccharification of hemicellulose. Biotechnol. Bioeng., 30, 1127-1146 (1983).
    • (1983) Biotechnol. Bioeng. , vol.30 , pp. 1127-1146
    • Dekker, R.F.G.1
  • 16
    • 0000262755 scopus 로고
    • Accessory enzymes involved in the hydrolysis of xylans
    • eds. Leatham, G. F., and Himmel, M. E., American Chemical Society, Washington, DC
    • Poutanen, K., Tenkanen, M., Korte, H., and Puls, J., Accessory enzymes involved in the hydrolysis of xylans. In "Enzymes in Biomass Conversion", eds. Leatham, G. F., and Himmel, M. E., American Chemical Society, Washington, DC, pp. 426-436 (1991).
    • (1991) Enzymes in Biomass Conversion , pp. 426-436
    • Poutanen, K.1    Tenkanen, M.2    Korte, H.3    Puls, J.4
  • 17
    • 0030642144 scopus 로고    scopus 로고
    • Xylanolytic enzymes from fungi and bacteria
    • Sunna, A., and Antranikian, G., Xylanolytic enzymes from fungi and bacteria. Crit. Rev. Biotechnol., 17, 39-67 (1997).
    • (1997) Crit. Rev. Biotechnol. , vol.17 , pp. 39-67
    • Sunna, A.1    Antranikian, G.2
  • 18
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides
    • de Vries, R. P., and Visser, J., Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. Rev., 65, 497-522 (2001).
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 497-522
    • De Vries, R.P.1    Visser, J.2
  • 19
    • 0034629241 scopus 로고    scopus 로고
    • An α-glucuronidase of Schizophyllum commune acting on polymeric xylan
    • Tenkanen, M., and Siika-aho, M., An α-glucuronidase of Schizophyllum commune acting on polymeric xylan. J. Biotechnol., 78, 149-161 (2000).
    • (2000) J. Biotechnol. , vol.78 , pp. 149-161
    • Tenkanen, M.1    Siika-aho, M.2
  • 20
    • 0008859703 scopus 로고
    • The relationship between glucuronidase and galacturonidase activity in the limpet and in mammalian tissues
    • Marsh, C. A., and Levvy, G. A., The relationship between glucuronidase and galacturonidase activity in the limpet and in mammalian tissues. Biochem. J., 68, 610-617 (1958).
    • (1958) Biochem. J. , vol.68 , pp. 610-617
    • Marsh, C.A.1    Levvy, G.A.2
  • 21
    • 0000137653 scopus 로고
    • α-4-O-Methyl-D-glucuronidase component of xylanolytic complexes
    • eds. Wood, W. A., and Kellogg, S. T., Academic Press, San Diego
    • Fontana, J. D., Gebara, M., Blumel, M., Schneider, H., MacKenzie, C. R., and Johnson, K. G., α-4-O-Methyl-D-glucuronidase component of xylanolytic complexes. In "Methods in Enzymology" vol. 160, eds. Wood, W. A., and Kellogg, S. T., Academic Press, San Diego, pp. 560-571 (1988).
    • (1988) Methods in Enzymology , vol.160 , pp. 560-571
    • Fontana, J.D.1    Gebara, M.2    Blumel, M.3    Schneider, H.4    MacKenzie, C.R.5    Johnson, K.G.6
  • 23
    • 0034669364 scopus 로고    scopus 로고
    • A chromogenic substrate for a β-xylosidase-coupled assay of α-glucuronidase
    • Biely, P., Hirsch, J., la Grange, D. C., van Zyl, W. H., and Prior, B. A., A chromogenic substrate for a β-xylosidase-coupled assay of α-glucuronidase. Anal. Biochem., 286, 289-294 (2000).
    • (2000) Anal. Biochem. , vol.286 , pp. 289-294
    • Biely, P.1    Hirsch, J.2    La Grange, D.C.3    Van Zyl, W.H.4    Prior, B.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.