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Volumn 3, Issue 1, 2010, Pages 84-92

Hyperthermostable acetyl xylan esterase

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL XYLAN ESTERASE; AXEA ENZYME; ESTERASE; UNCLASSIFIED DRUG;

EID: 77953567290     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/j.1751-7915.2009.00150.x     Document Type: Article
Times cited : (23)

References (23)
  • 1
    • 0023029475 scopus 로고
    • Cooperativity of esterases and xylanases in the enzymatic degradation of acetyl xylan
    • Biely, P., MacKenzie, C.R., Puls, J., and Schneider, H. (1986) Cooperativity of esterases and xylanases in the enzymatic degradation of acetyl xylan. Bio/Technology 4: 731-733.
    • (1986) Bio/Technology , vol.4 , pp. 731-733
    • Biely, P.1    MacKenzie, C.R.2    Puls, J.3    Schneider, H.4
  • 2
    • 0028973385 scopus 로고    scopus 로고
    • Castanares, A., McCrae, S.I., and Wood, T.M. (1995) D-Xylan- degrading enzyme system from the fungus Phanerochaete chrysosporium: isolation and partial characterisation of an α-(4-O-methyl)- D-glucuronidase. J Biotechnol 43: 183-194.
    • Castanares, A., McCrae, S.I., and Wood, T.M. (1995) D-Xylan- degrading enzyme system from the fungus Phanerochaete chrysosporium: isolation and partial characterisation of an α-(4-O-methyl)- D-glucuronidase. J Biotechnol 43: 183-194.
  • 3
    • 0037470149 scopus 로고    scopus 로고
    • Carbohydrateinduced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima
    • Chhabra, S.R., Shockley, K.R., Conners, S.B., Scott, K.L., Wolfinger, R.D., and Kelly, R.M. (2003) Carbohydrateinduced differential gene expression patterns in the hyperthermophilic bacterium Thermotoga maritima. J Biol Chem 278: 7540-7552.
    • (2003) J Biol Chem , vol.278 , pp. 7540-7552
    • Chhabra, S.R.1    Shockley, K.R.2    Conners, S.B.3    Scott, K.L.4    Wolfinger, R.D.5    Kelly, R.M.6
  • 4
    • 77953596223 scopus 로고    scopus 로고
    • Coutinho, P.M., and Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach. In Recent Advances in Carbohydrate Bioengineering. Gilbert, H.J., Davies, G., Henrissat, B., and Svensson, B. (eds). Cambridge, UK: The Royal Society of Chemistry, pp. 3-12 [WWW document]. URL http://www.cazy.org/.
    • Coutinho, P.M., and Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach. In Recent Advances in Carbohydrate Bioengineering. Gilbert, H.J., Davies, G., Henrissat, B., and Svensson, B. (eds). Cambridge, UK: The Royal Society of Chemistry, pp. 3-12 [WWW document]. URL http://www.cazy.org/.
  • 5
    • 0031912439 scopus 로고    scopus 로고
    • Purification and characterization of an acetyl xylan esterase from Bacillus pumilus
    • Degrassi, G., Okeke, B.C., Bruschi, C.V., and Venturi, V. (1998) Purification and characterization of an acetyl xylan esterase from Bacillus pumilus. Appl Environ Microbiol 64: 789-792.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 789-792
    • Degrassi, G.1    Okeke, B.C.2    Bruschi, C.V.3    Venturi, V.4
  • 6
    • 0033910674 scopus 로고    scopus 로고
    • The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity
    • Degrassi, G., Kojic, M., Ljubijankic, G., and Venturi, V. (2000) The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity. Microbiology 146: 1585-1591.
    • (2000) Microbiology , vol.146 , pp. 1585-1591
    • Degrassi, G.1    Kojic, M.2    Ljubijankic, G.3    Venturi, V.4
  • 7
    • 0027253969 scopus 로고
    • Cloning and characterization of β-galactoside and β-glucoside hydrolysing enzymes of Thermotoga maritima
    • Gabelsberger, J., Liebl, W., and Schleifer, K.H. (1993) Cloning and characterization of β-galactoside and β-glucoside hydrolysing enzymes of Thermotoga maritima. FEMS Microbiol Lett 109: 131-138.
    • (1993) FEMS Microbiol Lett , vol.109 , pp. 131-138
    • Gabelsberger, J.1    Liebl, W.2    Schleifer, K.H.3
  • 8
    • 71749086512 scopus 로고    scopus 로고
    • Thermotogales
    • 3rd edn, Dworkin, M, Falkow, S, Rosenberg, E, Schleifer, K.-H, and Stackebrandt, E, eds, New York, USA: Springer-Verlag, pp
    • Huber, R., and Hannig, M. (2006) Thermotogales. In The Prokaryotes. An Evolving Electronic Resource for the Microbiological Community, 3rd edn, Vol. VII. Dworkin, M., Falkow, S., Rosenberg, E., Schleifer, K.-H., and Stackebrandt, E. (eds). New York, USA: Springer-Verlag, pp. 899-922.
    • (2006) The Prokaryotes. An Evolving Electronic Resource for the Microbiological Community , vol.7 , pp. 899-922
    • Huber, R.1    Hannig, M.2
  • 10
    • 0000090628 scopus 로고
    • Measurement of acetylxylan esterase in Streptomyces
    • Johnson, K.G., Fontana, D., and MacKenzie, C.R. (1988) Measurement of acetylxylan esterase in Streptomyces Meth Enzymol 160: 551-560.
    • (1988) Meth Enzymol , vol.160 , pp. 551-560
    • Johnson, K.G.1    Fontana, D.2    MacKenzie, C.R.3
  • 11
    • 33749854901 scopus 로고    scopus 로고
    • Comparative characterization of deletion derivatives of the modular xylanase XynA of Thermotoga maritima
    • Kleine, J., and Liebl, W. (2006) Comparative characterization of deletion derivatives of the modular xylanase XynA of Thermotoga maritima. Extremophiles 10: 378-381.
    • (2006) Extremophiles , vol.10 , pp. 378-381
    • Kleine, J.1    Liebl, W.2
  • 12
    • 0027497465 scopus 로고
    • Degradation of different [(glucurono)arabino]xylans by combination of purified xylan-degrading enzymes
    • Kormelink, F.J.M., and Voragen, A.G.J. (1993) Degradation of different [(glucurono)arabino]xylans by combination of purified xylan-degrading enzymes. Appl Microbiol Biotechnol 38: 688-695.
    • (1993) Appl Microbiol Biotechnol , vol.38 , pp. 688-695
    • Kormelink, F.J.M.1    Voragen, A.G.J.2
  • 13
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • Kulkarni, N., Shendye, A., and Rao, M. (1999) Molecular and biotechnological aspects of xylanases. FEMS Microbiol Rev 23: 411-456.
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye, A.2    Rao, M.3
  • 14
    • 0026660023 scopus 로고
    • Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli
    • Liebl, W., Feil, R., Gabelsberger, J., Kellermann, J., and Schleifer, K.H. (1992) Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli. Eur J Biochem 207: 81-88.
    • (1992) Eur J Biochem , vol.207 , pp. 81-88
    • Liebl, W.1    Feil, R.2    Gabelsberger, J.3    Kellermann, J.4    Schleifer, K.H.5
  • 15
    • 38949210770 scopus 로고    scopus 로고
    • Xylanase attachment to the cell wall of the hyperthermophilic bacterium Thermotoga maritima
    • Liebl, W., Winterhalter, C., Baumeister, W., Armbrecht, M., and Valdez, M. (2008) Xylanase attachment to the cell wall of the hyperthermophilic bacterium Thermotoga maritima. J Bacteriol 190: 1350-1358.
    • (2008) J Bacteriol , vol.190 , pp. 1350-1358
    • Liebl, W.1    Winterhalter, C.2    Baumeister, W.3    Armbrecht, M.4    Valdez, M.5
  • 16
    • 0030886131 scopus 로고    scopus 로고
    • Isolation, analysis, and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: A beta-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity
    • Lorenz, W.W., and Wiegel, J. (1997) Isolation, analysis, and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: a beta-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity. Appl Environ Microbiol 179: 5436-5441.
    • (1997) Appl Environ Microbiol , vol.179 , pp. 5436-5441
    • Lorenz, W.W.1    Wiegel, J.2
  • 17
    • 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. (1997) 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) Mol Microbiol , vol.23 , pp. 267-279
    • Ruile, P.1    Winterhalter, C.2    Liebl, W.3
  • 18
    • 0032980767 scopus 로고    scopus 로고
    • The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6
    • Shulami, S., Gat, O., Sonenshein, A.L., and Shoham, Y. (1999) The glucuronic acid utilization gene cluster from Bacillus stearothermophilus T-6. J Bacteriol 181: 3695-3704.
    • (1999) J Bacteriol , vol.181 , pp. 3695-3704
    • Shulami, S.1    Gat, O.2    Sonenshein, A.L.3    Shoham, Y.4
  • 19
    • 33846932041 scopus 로고    scopus 로고
    • A twocomponent system regulates the expression of an ABC transporter for xylo-oligosaccharides in Geobacillus stearothermophilus
    • Shulami, S., Zaide, G., Zolotnitsky, G., Langut, Y., Feld, G., Sonenshein, A.L., and Shoham, Y. (2007) A twocomponent system regulates the expression of an ABC transporter for xylo-oligosaccharides in Geobacillus stearothermophilus. Appl Environ Microbiol 73: 874-884.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 874-884
    • Shulami, S.1    Zaide, G.2    Zolotnitsky, G.3    Langut, Y.4    Feld, G.5    Sonenshein, A.L.6    Shoham, Y.7
  • 20
    • 0035092271 scopus 로고    scopus 로고
    • Thermophilic adaptation of proteins
    • Sterner, R., and Liebl, W. (2001) Thermophilic adaptation of proteins. Crit Rev Biochem Mol Biol 36: 39-106.
    • (2001) Crit Rev Biochem Mol Biol , vol.36 , pp. 39-106
    • Sterner, R.1    Liebl, W.2
  • 21
    • 0038047121 scopus 로고    scopus 로고
    • Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9 A resolution
    • Vincent, F., Charnock, S.J., Verschueren, K.H.G., Turkenburg, J.P., Scott, D.J., Offen, W.A., et al. (2003) Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9 A resolution. J Mol Biol 330: 593-606.
    • (2003) J Mol Biol , vol.330 , pp. 593-606
    • Vincent, F.1    Charnock, S.J.2    Verschueren, K.H.G.3    Turkenburg, J.P.4    Scott, D.J.5    Offen, W.A.6
  • 22
    • 0029008857 scopus 로고
    • Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima strain MSB8
    • Winterhalter, C., and Liebl, W. (1995) Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima strain MSB8. Appl Environ Microbiol 61: 1810-1815.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1810-1815
    • Winterhalter, C.1    Liebl, W.2
  • 23
    • 0028901697 scopus 로고
    • Identification of a novel cellulose-binding domain within the multi-domain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima
    • Winterhalter, C., Heinrich, P., Candussio, A., Wich, G., and Liebl, W. (1995) Identification of a novel cellulose-binding domain within the multi-domain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima. Mol Microbiol 15: 431-444.
    • (1995) Mol Microbiol , vol.15 , pp. 431-444
    • Winterhalter, C.1    Heinrich, P.2    Candussio, A.3    Wich, G.4    Liebl, W.5


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