메뉴 건너뛰기




Volumn 32, Issue 2, 2014, Pages 316-332

β-Xylosidases and α-L-arabinofuranosidases: Accessory enzymes for arabinoxylan degradation

Author keywords

Biomass; Glycoside hydrolases; Hemicellulases; Hemicellulose; Polysaccharide degradation; Xylanolytic enzymes

Indexed keywords

BIOFUELS; BIOMASS; CELLULOSE; PLANTS (BOTANY); SUBSTRATES;

EID: 84895478762     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2013.11.005     Document Type: Review
Times cited : (121)

References (201)
  • 1
    • 4744359728 scopus 로고    scopus 로고
    • Crystal structure of family GH-8 chitosanase with subclass II specificity from Bacillus sp. K17
    • Adachi W., Sakihama Y., Shimizu S., Sunami T., Fukazawa T., Suzuki M., et al. Crystal structure of family GH-8 chitosanase with subclass II specificity from Bacillus sp. K17. J Mol Biol 2004, 343:785-795.
    • (2004) J Mol Biol , vol.343 , pp. 785-795
    • Adachi, W.1    Sakihama, Y.2    Shimizu, S.3    Sunami, T.4    Fukazawa, T.5    Suzuki, M.6
  • 2
    • 4344653896 scopus 로고    scopus 로고
    • Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes
    • Adelsberger H., Hertel C., Glawischnig E., Zverlov V.V., Schwarz W.H. Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes. Microbiology 2004, 150:2257-2266.
    • (2004) Microbiology , vol.150 , pp. 2257-2266
    • Adelsberger, H.1    Hertel, C.2    Glawischnig, E.3    Zverlov, V.V.4    Schwarz, W.H.5
  • 3
    • 68749112865 scopus 로고    scopus 로고
    • Crystal structure of an inverting GH 43 1, 5-α-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate
    • Alhassid A., Ben-David A., Tabachnikov O., Libster D., Naveh E., Zolotnitsky G., et al. Crystal structure of an inverting GH 43 1, 5-α-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate. Biochem J 2009, 422:73-82.
    • (2009) Biochem J , vol.422 , pp. 73-82
    • Alhassid, A.1    Ben-David, A.2    Tabachnikov, O.3    Libster, D.4    Naveh, E.5    Zolotnitsky, G.6
  • 4
    • 0029876033 scopus 로고    scopus 로고
    • Stereochemical course and reaction products of the action of β-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI
    • Armand S., Vieille C., Gey C., Heyraud A., Zeikus J.G., Henrissat B. Stereochemical course and reaction products of the action of β-xylosidase from Thermoanaerobacterium saccharolyticum strain B6A-RI. Eur J Biochem 1996, 236:706-713.
    • (1996) Eur J Biochem , vol.236 , pp. 706-713
    • Armand, S.1    Vieille, C.2    Gey, C.3    Heyraud, A.4    Zeikus, J.G.5    Henrissat, B.6
  • 5
    • 33746614259 scopus 로고    scopus 로고
    • Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls
    • Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R. Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls. Proc Natl Acad Sci U S A 2006, 103:11417-11422.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11417-11422
    • Bauer, S.1    Vasu, P.2    Persson, S.3    Mort, A.J.4    Somerville, C.R.5
  • 6
    • 77956580439 scopus 로고    scopus 로고
    • Diversity of glycosyl hydrolases from cellulose-depleting communities enriched from casts of two earthworm species
    • Beloqui A., Nechitaylo T.Y., Lopez-Cortes N., Ghazi A., Guazzaroni M.E., Polaina J., et al. Diversity of glycosyl hydrolases from cellulose-depleting communities enriched from casts of two earthworm species. Appl Environ Microbiol 2010, 76:5934-5946.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5934-5946
    • Beloqui, A.1    Nechitaylo, T.Y.2    Lopez-Cortes, N.3    Ghazi, A.4    Guazzaroni, M.E.5    Polaina, J.6
  • 7
    • 0035884410 scopus 로고    scopus 로고
    • The Pseudomonas cellulosa glycoside hydrolase family 51 arabinofuranosidase exhibits wide substrate specificity
    • Beylot M.H., McKie V.A., Voragen A.G., Doeswijk-Voragen C.H., Gilbert H.J. The Pseudomonas cellulosa glycoside hydrolase family 51 arabinofuranosidase exhibits wide substrate specificity. Biochem J 2001, 358:607-617.
    • (2001) Biochem J , vol.358 , pp. 607-617
    • Beylot, M.H.1    McKie, V.A.2    Voragen, A.G.3    Doeswijk-Voragen, C.H.4    Gilbert, H.J.5
  • 8
    • 2542453684 scopus 로고    scopus 로고
    • X4 modules represent a new family of carbohydrate-binding modules that display novel properties
    • Bolam D.N., Xie H., Pell G., Hogg D., Galbraith G., Henrissat B., et al. X4 modules represent a new family of carbohydrate-binding modules that display novel properties. J Biol Chem 2004, 279:22953-22963.
    • (2004) J Biol Chem , vol.279 , pp. 22953-22963
    • Bolam, D.N.1    Xie, H.2    Pell, G.3    Hogg, D.4    Galbraith, G.5    Henrissat, B.6
  • 10
    • 34250849697 scopus 로고    scopus 로고
    • Recombinant expression and characterization of XynD from Bacillus subtilis subsp. subtilis ATCC 6051: a GH 43 arabinoxylan arabinofuranohydrolase
    • Bourgois T.M., Van Craeyveld V., Van Campenhout S., Courtin C.M., Delcour J.A., Robben J., et al. Recombinant expression and characterization of XynD from Bacillus subtilis subsp. subtilis ATCC 6051: a GH 43 arabinoxylan arabinofuranohydrolase. Appl Microbiol Biotechnol 2007, 75:1309-1317.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 1309-1317
    • Bourgois, T.M.1    Van Craeyveld, V.2    Van Campenhout, S.3    Courtin, C.M.4    Delcour, J.A.5    Robben, J.6
  • 11
    • 0035917899 scopus 로고    scopus 로고
    • Glutamic acid 160 is the acid-base catalyst of b-xylosidase from Bacillus stearothermophilus T-6: a family 39 glycoside hydrolase
    • Bravman T., Mechaly A., Shulami S., Belakhov V., Baasov T., Shoham G., et al. Glutamic acid 160 is the acid-base catalyst of b-xylosidase from Bacillus stearothermophilus T-6: a family 39 glycoside hydrolase. FEBS Lett 2001, 495:115-119.
    • (2001) FEBS Lett , vol.495 , pp. 115-119
    • Bravman, T.1    Mechaly, A.2    Shulami, S.3    Belakhov, V.4    Baasov, T.5    Shoham, G.6
  • 12
    • 0041816478 scopus 로고    scopus 로고
    • Detailed kinetic analysis of a family 52 glycoside hydrolase: a β-xylosidase from Geobacillus stearothermophilus
    • Bravman T., Zolotnitsky G., Belakhov V., Shoham G., Henrissat B., Baasov T., et al. Detailed kinetic analysis of a family 52 glycoside hydrolase: a β-xylosidase from Geobacillus stearothermophilus. Biochemistry 2003, 42:10528-10536.
    • (2003) Biochemistry , vol.42 , pp. 10528-10536
    • Bravman, T.1    Zolotnitsky, G.2    Belakhov, V.3    Shoham, G.4    Henrissat, B.5    Baasov, T.6
  • 13
    • 0035917892 scopus 로고    scopus 로고
    • Stereochemistry of family 52 glycosyl hydrolases: a β-xylosidase from Bacillus stearothermophilus T-6 is a retaining enzyme
    • Bravman T., Zolotnitsky G., Shulami S., Belakhov V., Solomon D., Baasov T., et al. Stereochemistry of family 52 glycosyl hydrolases: a β-xylosidase from Bacillus stearothermophilus T-6 is a retaining enzyme. FEBS Lett 2001, 495:39-43.
    • (2001) FEBS Lett , vol.495 , pp. 39-43
    • Bravman, T.1    Zolotnitsky, G.2    Shulami, S.3    Belakhov, V.4    Solomon, D.5    Baasov, T.6
  • 15
    • 0037041053 scopus 로고    scopus 로고
    • A β-glucosidase/xylosidase from the phytopathogenic oomycete, Phytophthora infestans
    • Brunner F., Wirtz W., Rose J.K.C., Darvill A.G., Govers F., Scheel D., et al. A β-glucosidase/xylosidase from the phytopathogenic oomycete, Phytophthora infestans. Phytochemistry 2002, 59:689-696.
    • (2002) Phytochemistry , vol.59 , pp. 689-696
    • Brunner, F.1    Wirtz, W.2    Rose, J.K.C.3    Darvill, A.G.4    Govers, F.5    Scheel, D.6
  • 16
    • 43949124808 scopus 로고    scopus 로고
    • Structure of the two-subsite β-d-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane
    • Brunzelle J.S., Jordan D.B., McCaslin D.R., Olczak A., Wawrzak Z. Structure of the two-subsite β-d-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane. Arch Biochem Biophys 2008, 474:157-166.
    • (2008) Arch Biochem Biophys , vol.474 , pp. 157-166
    • Brunzelle, J.S.1    Jordan, D.B.2    McCaslin, D.R.3    Olczak, A.4    Wawrzak, Z.5
  • 17
    • 33646165074 scopus 로고    scopus 로고
    • The structure of an inverting GH43 β-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role of the three catalytic residues
    • Brüx C., Ben-David A., Shallom-Shezifi D., Leon M., Niefind K., Shoham G., et al. The structure of an inverting GH43 β-xylosidase from Geobacillus stearothermophilus with its substrate reveals the role of the three catalytic residues. J Mol Biol 2006, 359:97-109.
    • (2006) J Mol Biol , vol.359 , pp. 97-109
    • Brüx, C.1    Ben-David, A.2    Shallom-Shezifi, D.3    Leon, M.4    Niefind, K.5    Shoham, G.6
  • 18
    • 77953626492 scopus 로고    scopus 로고
    • Cellulosilyticum ruminicola, a newly described rumen bacterium that possesses redundant fibrolytic-protein-encoding genes and degrades lignocellulose with multiple carbohydrate-borne fibrolytic enzymes
    • Cai S., Li J., Hu F.Z., Zhang K., Luo Y., Janto B., et al. Cellulosilyticum ruminicola, a newly described rumen bacterium that possesses redundant fibrolytic-protein-encoding genes and degrades lignocellulose with multiple carbohydrate-borne fibrolytic enzymes. Appl Environ Microbiol 2010, 76:3818-3824.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 3818-3824
    • Cai, S.1    Li, J.2    Hu, F.Z.3    Zhang, K.4    Luo, Y.5    Janto, B.6
  • 19
    • 34547505787 scopus 로고    scopus 로고
    • Purification and characterization of a highly thermostable α-l-arabinofuranosidase from Geobacillus caldoxylolyticus TK4
    • Canakci S., Belduz A.O., Saha B., Yasar A., Ayaz F.A., Yayli N. Purification and characterization of a highly thermostable α-l-arabinofuranosidase from Geobacillus caldoxylolyticus TK4. Appl Microbiol Biotechnol 2007, 75:813-820.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 813-820
    • Canakci, S.1    Belduz, A.O.2    Saha, B.3    Yasar, A.4    Ayaz, F.A.5    Yayli, N.6
  • 20
    • 54349103940 scopus 로고    scopus 로고
    • Cloning, purification, and characterization of a thermostable α-l-arabinofuranosidase from Anoxybacillus kestanbolensis AC26Sari
    • Canakci S., Kacagan M., Inan K., Belduz A., Saha B. Cloning, purification, and characterization of a thermostable α-l-arabinofuranosidase from Anoxybacillus kestanbolensis AC26Sari. Appl Microbiol Biotechnol 2008, 81:61-68.
    • (2008) Appl Microbiol Biotechnol , vol.81 , pp. 61-68
    • Canakci, S.1    Kacagan, M.2    Inan, K.3    Belduz, A.4    Saha, B.5
  • 22
    • 53649102805 scopus 로고    scopus 로고
    • Efficient hydrolysis of hemicellulose by a Fusarium graminearum xylanase blend produced at high levels in Escherichia coli
    • Carapito R., Carapito C., Jeltsch J.M., Phalip V. Efficient hydrolysis of hemicellulose by a Fusarium graminearum xylanase blend produced at high levels in Escherichia coli. Bioresour Technol 2009, 100:845-850.
    • (2009) Bioresour Technol , vol.100 , pp. 845-850
    • Carapito, R.1    Carapito, C.2    Jeltsch, J.M.3    Phalip, V.4
  • 23
    • 33748290144 scopus 로고    scopus 로고
    • Cloning and characterization of a cold-active xylanase enzyme from an environmental DNA library
    • Charles C.L., Rena E.K.-A., Kurt W., George H.R., Dominic W.S.W. Cloning and characterization of a cold-active xylanase enzyme from an environmental DNA library. Extremophiles 2006, 10:295-300.
    • (2006) Extremophiles , vol.10 , pp. 295-300
    • Charles, C.L.1    Rena, E.K.-A.2    Kurt, W.3    George, H.R.4    Dominic, W.S.W.5
  • 24
    • 0036685303 scopus 로고    scopus 로고
    • Identification of the two essential groups in the family 3 β-glucosidase from Flavobacterium meningosepticum by labelling and tandem mass spectrometric analysis
    • Chir J., Withers S., Wan C.F., Li Y.K. Identification of the two essential groups in the family 3 β-glucosidase from Flavobacterium meningosepticum by labelling and tandem mass spectrometric analysis. Biochem J 2002, 365:857-863.
    • (2002) Biochem J , vol.365 , pp. 857-863
    • Chir, J.1    Withers, S.2    Wan, C.F.3    Li, Y.K.4
  • 25
    • 77954222256 scopus 로고    scopus 로고
    • A new archaeal β-glycosidase from Sulfolobus solfataricus: seeding a novel retaining β-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2
    • Cobucci-Ponzano B., Aurilia V., Riccio G., Henrissat B., Coutinho P.M., Strazzulli A., et al. A new archaeal β-glycosidase from Sulfolobus solfataricus: seeding a novel retaining β-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2. J Biol Chem 2010, 285:20691-20703.
    • (2010) J Biol Chem , vol.285 , pp. 20691-20703
    • Cobucci-Ponzano, B.1    Aurilia, V.2    Riccio, G.3    Henrissat, B.4    Coutinho, P.M.5    Strazzulli, A.6
  • 27
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins T., Gerday C., Feller G. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol Rev 2005, 29:3-23.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 28
    • 54949145317 scopus 로고    scopus 로고
    • The family 52 β-xylosidase from Geobacillus stearothermophilus is a dimer: structural and biophysical characterization of a glycoside hydrolase
    • Contreras L.M., Gomez J., Prieto J., Clemente-Jiménez J.M., Las Heras-Vazquez F.J., Rodriguez-Vico F., et al. The family 52 β-xylosidase from Geobacillus stearothermophilus is a dimer: structural and biophysical characterization of a glycoside hydrolase. Biochim Biophys Acta 2008, 1784:1924-1934.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1924-1934
    • Contreras, L.M.1    Gomez, J.2    Prieto, J.3    Clemente-Jiménez, J.M.4    Las Heras-Vazquez, F.J.5    Rodriguez-Vico, F.6
  • 29
    • 16644395774 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of a thermostable family 52 β-d-xylosidase from Geobacillus stearothermophilus T-6
    • Czjzek M., Bravman T., Henrissat B., Shoham Y. Crystallization and preliminary crystallographic analysis of a thermostable family 52 β-d-xylosidase from Geobacillus stearothermophilus T-6. Acta Crystallogr D Biol Crystallogr 2004, 60:1461-1463.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1461-1463
    • Czjzek, M.1    Bravman, T.2    Henrissat, B.3    Shoham, Y.4
  • 30
    • 7444227450 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of family 39 β-d-xylosidase from Geobacillus stearothermophilus T-6
    • Czjzek M., Bravman T., Henrissat B., Shoham Y. Crystallization and preliminary X-ray analysis of family 39 β-d-xylosidase from Geobacillus stearothermophilus T-6. Acta Crystallogr D Biol Crystallogr 2004, 60:583-585.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 583-585
    • Czjzek, M.1    Bravman, T.2    Henrissat, B.3    Shoham, Y.4
  • 31
    • 26844535502 scopus 로고    scopus 로고
    • Enzyme-substrate complex structures of a GH39 β-xylosidase from Geobacillus stearothermophilus
    • Czjzek M., David A.B., Bravman T., Shoham G., Henrissat B., Shoham Y. Enzyme-substrate complex structures of a GH39 β-xylosidase from Geobacillus stearothermophilus. J Mol Biol 2005, 353:838-846.
    • (2005) J Mol Biol , vol.353 , pp. 838-846
    • Czjzek, M.1    David, A.B.2    Bravman, T.3    Shoham, G.4    Henrissat, B.5    Shoham, Y.6
  • 32
    • 0001963859 scopus 로고
    • The primary cell walls of flowering plants
    • Academic Press, Inc., New York, N.E. Tolbert (Ed.)
    • Darvill A., McNeil M., Albersheim P., Delmer D.P. The primary cell walls of flowering plants. The biochemistry of plants 1980, vol. 1:91-162. Academic Press, Inc., New York. N.E. Tolbert (Ed.).
    • (1980) The biochemistry of plants , vol.1 , pp. 91-162
    • Darvill, A.1    McNeil, M.2    Albersheim, P.3    Delmer, D.P.4
  • 33
    • 0033991365 scopus 로고    scopus 로고
    • An α-L-arabinofuranosidase from Penicillium purpurogenum: production, purification and properties
    • De Ioannes P., Peirano A., Steiner J., Eyzaguirre J. An α-L-arabinofuranosidase from Penicillium purpurogenum: production, purification and properties. J Biotechnol 2000, 76:253-258.
    • (2000) J Biotechnol , vol.76 , pp. 253-258
    • De Ioannes, P.1    Peirano, A.2    Steiner, J.3    Eyzaguirre, J.4
  • 34
    • 33645943709 scopus 로고    scopus 로고
    • Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the β-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product
    • De Vos D., Collins T., Nerinckx W., Savvides S.N., Claeyssens M., Gerday C., et al. Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the β-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product. Biochemistry (Mosc) 2006, 45:4797-4807.
    • (2006) Biochemistry (Mosc) , vol.45 , pp. 4797-4807
    • De Vos, D.1    Collins, T.2    Nerinckx, W.3    Savvides, S.N.4    Claeyssens, M.5    Gerday, C.6
  • 35
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides
    • de Vries R.P., Visser J. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol Mol Biol Rev 2001, 65:497-522.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 497-522
    • de Vries, R.P.1    Visser, J.2
  • 36
    • 37249089008 scopus 로고    scopus 로고
    • Characterization of a family 54 α-l-arabinofuranosidase from Aureobasidium pullulans
    • de Wet B., Matthew M., Storbeck K.H., van Zyl W., Prior B. Characterization of a family 54 α-l-arabinofuranosidase from Aureobasidium pullulans. Appl Microbiol Biotechnol 2008, 77:975-983.
    • (2008) Appl Microbiol Biotechnol , vol.77 , pp. 975-983
    • de Wet, B.1    Matthew, M.2    Storbeck, K.H.3    van Zyl, W.4    Prior, B.5
  • 37
    • 0034110774 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a highly thermostable α-l-arabinofuranosidase from Thermobacillus xylanilyticus
    • Debeche T., Cummings N., Connerton I., Debeire P., O'Donohue M.J. Genetic and biochemical characterization of a highly thermostable α-l-arabinofuranosidase from Thermobacillus xylanilyticus. Appl Environ Microbiol 2000, 66:1734-1736.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 1734-1736
    • Debeche, T.1    Cummings, N.2    Connerton, I.3    Debeire, P.4    O'Donohue, M.J.5
  • 38
    • 66749150169 scopus 로고    scopus 로고
    • Enzymatic deconstruction of xylan for biofuel production
    • Dodd D., Cann I.K. Enzymatic deconstruction of xylan for biofuel production. GCB Bioenergy 2009, 1:2-17.
    • (2009) GCB Bioenergy , vol.1 , pp. 2-17
    • Dodd, D.1    Cann, I.K.2
  • 39
    • 65549112969 scopus 로고    scopus 로고
    • Biochemical analysis of a β-d-xylosidase and a bifunctional xylanase-ferulic acid esterase from a xylanolytic gene cluster in Prevotella ruminicola 23
    • Dodd D., Kocherginskaya S.A., Spies M.A., Beery K.E., Abbas C.A., Mackie R.I., et al. Biochemical analysis of a β-d-xylosidase and a bifunctional xylanase-ferulic acid esterase from a xylanolytic gene cluster in Prevotella ruminicola 23. J Bacteriol 2009, 191:3328-3338.
    • (2009) J Bacteriol , vol.191 , pp. 3328-3338
    • Dodd, D.1    Kocherginskaya, S.A.2    Spies, M.A.3    Beery, K.E.4    Abbas, C.A.5    Mackie, R.I.6
  • 40
    • 0032519716 scopus 로고    scopus 로고
    • Substrate-binding domains of glycanases from Streptomyces lividans: characterization of a new family of xylan-binding domains
    • Dupont C., Roberge M., Shareck F., Morosoli R., Kluepfel D. Substrate-binding domains of glycanases from Streptomyces lividans: characterization of a new family of xylan-binding domains. Biochem J 1998, 330:41-45.
    • (1998) Biochem J , vol.330 , pp. 41-45
    • Dupont, C.1    Roberge, M.2    Shareck, F.3    Morosoli, R.4    Kluepfel, D.5
  • 41
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O., Brunak S., von Heijne G., Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2007, 2:953-971.
    • (2007) Nat Protoc , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 43
    • 0033567339 scopus 로고    scopus 로고
    • Homologous xylanases from Clostridium thermocellum: evidence for bi-functional activity, synergism between xylanase catalytic modules and the presence of xylan-binding domains in enzyme complexes
    • Fernandes A.C., Fontes C.M., Gilbert H.J., Hazlewood G.P., Fernandes T.H., Ferreira L.M. Homologous xylanases from Clostridium thermocellum: evidence for bi-functional activity, synergism between xylanase catalytic modules and the presence of xylan-binding domains in enzyme complexes. Biochem J 1999, 342:105-110.
    • (1999) Biochem J , vol.342 , pp. 105-110
    • Fernandes, A.C.1    Fontes, C.M.2    Gilbert, H.J.3    Hazlewood, G.P.4    Fernandes, T.H.5    Ferreira, L.M.6
  • 44
    • 0027444855 scopus 로고
    • Molecular cloning, expression and structure of the endo-1, 5-α-l-arabinase gene of Aspergillus niger
    • Flipphi M.J.A., Panneman H., Veen P., Visser J., Graaff L.H. Molecular cloning, expression and structure of the endo-1, 5-α-l-arabinase gene of Aspergillus niger. Appl Microbiol Biotechnol 1993, 40:318-326.
    • (1993) Appl Microbiol Biotechnol , vol.40 , pp. 318-326
    • Flipphi, M.J.A.1    Panneman, H.2    Veen, P.3    Visser, J.4    Graaff, L.H.5
  • 45
    • 0027157925 scopus 로고
    • Cloning of the Aspergillus niger gene encoding α-l-arabinofuranosidase A
    • Flipphi M.J.A., Visser J., Veen P., Graaff L.H. Cloning of the Aspergillus niger gene encoding α-l-arabinofuranosidase A. Appl Microbiol Biotechnol 1993, 39:335-340.
    • (1993) Appl Microbiol Biotechnol , vol.39 , pp. 335-340
    • Flipphi, M.J.A.1    Visser, J.2    Veen, P.3    Graaff, L.H.4
  • 46
    • 47149113965 scopus 로고    scopus 로고
    • A family 51 α-l-arabinofuranosidase from Penicillium purpurogenum: purification, properties and amino acid sequence
    • Fritz M., Ravanal M.C., Braet C., Eyzaguirre J. A family 51 α-l-arabinofuranosidase from Penicillium purpurogenum: purification, properties and amino acid sequence. Mycol Res 2008, 112:933-942.
    • (2008) Mycol Res , vol.112 , pp. 933-942
    • Fritz, M.1    Ravanal, M.C.2    Braet, C.3    Eyzaguirre, J.4
  • 47
    • 20444504291 scopus 로고    scopus 로고
    • Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125
    • Fushinobu S., Hidaka M., Honda Y., Wakagi T., Shoun H., Kitaoka M. Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125. J Biol Chem 2005, 280:17180-17186.
    • (2005) J Biol Chem , vol.280 , pp. 17180-17186
    • Fushinobu, S.1    Hidaka, M.2    Honda, Y.3    Wakagi, T.4    Shoun, H.5    Kitaoka, M.6
  • 48
    • 0029146225 scopus 로고
    • 14: sequence relationships, synergistic interactions, and oxygen sensitivity of a novel enzyme with exoxylanase and β-(1,4)-xylosidase activities
    • 14: sequence relationships, synergistic interactions, and oxygen sensitivity of a novel enzyme with exoxylanase and β-(1,4)-xylosidase activities. Appl Environ Microbiol 1995, 61:2958-2964.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2958-2964
    • Gasparic, A.1    Martin, J.2    Daniel, A.S.3    Flint, H.J.4
  • 49
    • 0026734152 scopus 로고
    • Stereoselective hydrolysis catalyzed by related β-1,4-glucanases and β-1,4-xylanases
    • Gebler J., Gilkes N.R., Claeyssens M., Wilson D.B., Beguin P., Wakarchuk W.W., et al. Stereoselective hydrolysis catalyzed by related β-1,4-glucanases and β-1,4-xylanases. J Biol Chem 1992, 267:12559-12561.
    • (1992) J Biol Chem , vol.267 , pp. 12559-12561
    • Gebler, J.1    Gilkes, N.R.2    Claeyssens, M.3    Wilson, D.B.4    Beguin, P.5    Wakarchuk, W.W.6
  • 50
    • 0034122956 scopus 로고    scopus 로고
    • Multidomain and multifunctional glycosyl hydrolases from the extreme thermophile Caldicellulosiruptor isolate Tok7B.1
    • Gibbs M.D., Reeves R.A., Farrington G.K., Anderson P., Williams D.P., Bergquist P.L. Multidomain and multifunctional glycosyl hydrolases from the extreme thermophile Caldicellulosiruptor isolate Tok7B.1. Curr Microbiol 2000, 40:333-340.
    • (2000) Curr Microbiol , vol.40 , pp. 333-340
    • Gibbs, M.D.1    Reeves, R.A.2    Farrington, G.K.3    Anderson, P.4    Williams, D.P.5    Bergquist, P.L.6
  • 51
    • 78149436124 scopus 로고    scopus 로고
    • Combined transcriptome and proteome analysis of Bifidobacterium animalis subsp. lactis BB-12 grown on xylo-oligosaccharides and a model of their utilization
    • Gilad O., Jacobsen S., Stuer-Lauridsen B., Pedersen M.B., Garrigues C., Svensson B. Combined transcriptome and proteome analysis of Bifidobacterium animalis subsp. lactis BB-12 grown on xylo-oligosaccharides and a model of their utilization. Appl Environ Microbiol 2010, 76:7285-7291.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 7285-7291
    • Gilad, O.1    Jacobsen, S.2    Stuer-Lauridsen, B.3    Pedersen, M.B.4    Garrigues, C.5    Svensson, B.6
  • 52
    • 0028984077 scopus 로고
    • Purification and characterization of α-l-arabinofuranosidase from Bacillus stearothermophilus T-6
    • Gilead S., Shoham Y. Purification and characterization of α-l-arabinofuranosidase from Bacillus stearothermophilus T-6. Appl Environ Microbiol 1995, 61:170-174.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 170-174
    • Gilead, S.1    Shoham, Y.2
  • 53
    • 0025748793 scopus 로고
    • Two β-glycanase genes are clustered in Bacillus polymyxa: molecular cloning, expression, and sequence analysis of genes encoding a xylanase and an endo-β-(1,3)-(1,4)-glucanase
    • Gosalbes M.J., Pérez-González J.A., González R., Navarro A. Two β-glycanase genes are clustered in Bacillus polymyxa: molecular cloning, expression, and sequence analysis of genes encoding a xylanase and an endo-β-(1,3)-(1,4)-glucanase. J Bacteriol 1991, 173:7705-7710.
    • (1991) J Bacteriol , vol.173 , pp. 7705-7710
    • Gosalbes, M.J.1    Pérez-González, J.A.2    González, R.3    Navarro, A.4
  • 54
    • 58549102500 scopus 로고    scopus 로고
    • Cell wall fermentation kinetics are impacted more by lignin content and ferulate cross-linking than by lignin composition
    • Grabber J.H., Mertens D.R., Kim H., Funk C., Lu F., Ralph J. Cell wall fermentation kinetics are impacted more by lignin content and ferulate cross-linking than by lignin composition. J Sci Food Agric 2009, 89:112-129.
    • (2009) J Sci Food Agric , vol.89 , pp. 112-129
    • Grabber, J.H.1    Mertens, D.R.2    Kim, H.3    Funk, C.4    Lu, F.5    Ralph, J.6
  • 55
    • 77955654728 scopus 로고    scopus 로고
    • Characterization of the family GH54 α-l-arabinofuranosidases in Penicillium funiculosum including a novel protein bearing a cellulose-binding domain
    • Guais O., Tourrasse O., Dourdoigne M., Parrou J., Francois J. Characterization of the family GH54 α-l-arabinofuranosidases in Penicillium funiculosum including a novel protein bearing a cellulose-binding domain. Appl Microbiol Biotechnol 2010, 87:1007-1021.
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 1007-1021
    • Guais, O.1    Tourrasse, O.2    Dourdoigne, M.3    Parrou, J.4    Francois, J.5
  • 56
    • 0034333059 scopus 로고    scopus 로고
    • Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases
    • Harvey A.J., Hrmova M., De Gori R., Varghese J.N., Fincher G.B. Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases. Proteins 2000, 41:257-269.
    • (2000) Proteins , vol.41 , pp. 257-269
    • Harvey, A.J.1    Hrmova, M.2    De Gori, R.3    Varghese, J.N.4    Fincher, G.B.5
  • 58
    • 0035226754 scopus 로고    scopus 로고
    • Xln23 from Streptomyces chattanoogensis UAH23 encodes a putative enzyme with separate xylanase and arabinofuranosidase catalytic domains
    • Hernandez A., Copa-Patino J.L., Soliveri J. xln23 from Streptomyces chattanoogensis UAH23 encodes a putative enzyme with separate xylanase and arabinofuranosidase catalytic domains. DNA Seq 2001, 12:167-177.
    • (2001) DNA Seq , vol.12 , pp. 167-177
    • Hernandez, A.1    Copa-Patino, J.L.2    Soliveri, J.3
  • 59
    • 84890527379 scopus 로고    scopus 로고
    • Characterization of a hexameric exo-acting GH51 a-l-arabinofuranosidase from the mesophilic Bacillus subtilis
    • Hoffmam Z., Oliveira L., Cota J., Alvarez T., Diogo J., Oliveira Neto M., et al. Characterization of a hexameric exo-acting GH51 a-l-arabinofuranosidase from the mesophilic Bacillus subtilis. Mol Biotechnol 2013, 1-8.
    • (2013) Mol Biotechnol , pp. 1-8
    • Hoffmam, Z.1    Oliveira, L.2    Cota, J.3    Alvarez, T.4    Diogo, J.5    Oliveira Neto, M.6
  • 60
    • 11244279648 scopus 로고    scopus 로고
    • A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase
    • Honda Y., Kitaoka M. A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase. J Biol Chem 2004, 279:55097-55103.
    • (2004) J Biol Chem , vol.279 , pp. 55097-55103
    • Honda, Y.1    Kitaoka, M.2
  • 61
    • 17644434949 scopus 로고    scopus 로고
    • Crystal structure and snapshots along the reaction pathway of a family 51 α-l-arabinofuranosidase
    • Hövel K., Shallom D., Niefind K., Belakhov V., Shoham G., Baasov T., et al. Crystal structure and snapshots along the reaction pathway of a family 51 α-l-arabinofuranosidase. EMBO J 2003, 22:4922-4932.
    • (2003) EMBO J , vol.22 , pp. 4922-4932
    • Hövel, K.1    Shallom, D.2    Niefind, K.3    Belakhov, V.4    Shoham, G.5    Baasov, T.6
  • 62
    • 0037844916 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of a family 51 glycoside hydrolase, the α-l-arabinofuranosidase from Geobacillus stearothermophilus T-6
    • Hövel K., Shallom D., Niefind K., Baasov T., Shoham G., Shoham Y., et al. Crystallization and preliminary X-ray analysis of a family 51 glycoside hydrolase, the α-l-arabinofuranosidase from Geobacillus stearothermophilus T-6. Acta Crystallogr D Biol Crystallogr 2003, 59:913-915.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 913-915
    • Hövel, K.1    Shallom, D.2    Niefind, K.3    Baasov, T.4    Shoham, G.5    Shoham, Y.6
  • 63
    • 0031433085 scopus 로고    scopus 로고
    • Barley b-d-glucan exohydrolases. substrate specificity and kinetic properties
    • Hrmova M., Fincher G.B. Barley b-d-glucan exohydrolases. substrate specificity and kinetic properties. Carbohydr Res 1997, 305:209-221.
    • (1997) Carbohydr Res , vol.305 , pp. 209-221
    • Hrmova, M.1    Fincher, G.B.2
  • 64
    • 84870046695 scopus 로고    scopus 로고
    • The substrate/product-binding modes of a novel GH120 beta-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485
    • Huang C.-H., Sun Y., Ko T., Chen C., Zheng Y., Chan H., et al. The substrate/product-binding modes of a novel GH120 beta-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485. Biochem J 2012, 448:401-407.
    • (2012) Biochem J , vol.448 , pp. 401-407
    • Huang, C.-H.1    Sun, Y.2    Ko, T.3    Chen, C.4    Zheng, Y.5    Chan, H.6
  • 65
    • 33751427383 scopus 로고    scopus 로고
    • Characterization of an exo-β-1, 3-d-galactanase from Streptomyces avermitilis NBRC14893 acting on arabinogalactan-proteins
    • Ichinose H., Kotake T., Tsumuraya Y., Kaneko S. Characterization of an exo-β-1, 3-d-galactanase from Streptomyces avermitilis NBRC14893 acting on arabinogalactan-proteins. Biosci Biotechnol Biochem 2006, 70:2745-2750.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 2745-2750
    • Ichinose, H.1    Kotake, T.2    Tsumuraya, Y.3    Kaneko, S.4
  • 66
    • 50249172181 scopus 로고    scopus 로고
    • Characterization of a modular enzyme of exo-1,5-α-l-arabinofuranosidase and arabinan binding module from Streptomyces avermitilis NBRC14893
    • Ichinose H., Yoshida M., Fujimoto Z., Kaneko S. Characterization of a modular enzyme of exo-1,5-α-l-arabinofuranosidase and arabinan binding module from Streptomyces avermitilis NBRC14893. Appl Microbiol Biotechnol 2008, 80:399-408.
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 399-408
    • Ichinose, H.1    Yoshida, M.2    Fujimoto, Z.3    Kaneko, S.4
  • 68
    • 21844480904 scopus 로고    scopus 로고
    • An exo-b-1,3-galactanase having a novel β-1,3-galactan-binding module from Phanerochaete chrysosporium
    • Ichinose H., Yoshida M., Kotake T., Kuno A., Igarashi K., Tsumuraya Y., et al. An exo-b-1,3-galactanase having a novel β-1,3-galactan-binding module from Phanerochaete chrysosporium. J Biol Chem 2005, 280:25820-25829.
    • (2005) J Biol Chem , vol.280 , pp. 25820-25829
    • Ichinose, H.1    Yoshida, M.2    Kotake, T.3    Kuno, A.4    Igarashi, K.5    Tsumuraya, Y.6
  • 69
    • 84863242735 scopus 로고    scopus 로고
    • Crystal structures of glycoside hydrolase family 51 α-l-arabinofuranosidase from Thermotoga maritima
    • Im D.H., Kimura K.I., Hayasaka F., Tanaka T., Noguchi M., Kobayashi A., et al. Crystal structures of glycoside hydrolase family 51 α-l-arabinofuranosidase from Thermotoga maritima. Biosci Biotechnol Biochem 2012, 76:423-428.
    • (2012) Biosci Biotechnol Biochem , vol.76 , pp. 423-428
    • Im, D.H.1    Kimura, K.I.2    Hayasaka, F.3    Tanaka, T.4    Noguchi, M.5    Kobayashi, A.6
  • 70
    • 53449083444 scopus 로고    scopus 로고
    • Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis
    • Inacio J.M., Correia I.L., de Sa-Nogueira I. Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis. Microbiology 2008, 154:2719-2729.
    • (2008) Microbiology , vol.154 , pp. 2719-2729
    • Inacio, J.M.1    Correia, I.L.2    de Sa-Nogueira, I.3
  • 71
    • 44949133209 scopus 로고    scopus 로고
    • Characterization of abn2 (yxiA), encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharide degradation
    • Inácio J.M., de Sá-Nogueira I. Characterization of abn2 (yxiA), encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharide degradation. J Bacteriol 2008, 190:4272-4280.
    • (2008) J Bacteriol , vol.190 , pp. 4272-4280
    • Inácio, J.M.1    de Sá-Nogueira, I.2
  • 72
    • 0030793569 scopus 로고    scopus 로고
    • Structure and functions of feruloylated polysaccharides
    • Ishii T. Structure and functions of feruloylated polysaccharides. Plant Sci 1997, 127:111-127.
    • (1997) Plant Sci , vol.127 , pp. 111-127
    • Ishii, T.1
  • 73
    • 0345491341 scopus 로고    scopus 로고
    • Xylosidases associated with the cell surface of Penicillium herquei IFO 4674
    • Ito T., Yokoyama E., Sato H., Ujita M., Funaguma T., Furukawa K., et al. Xylosidases associated with the cell surface of Penicillium herquei IFO 4674. J Biosci Bioeng 2003, 96:354-359.
    • (2003) J Biosci Bioeng , vol.96 , pp. 354-359
    • Ito, T.1    Yokoyama, E.2    Sato, H.3    Ujita, M.4    Funaguma, T.5    Furukawa, K.6
  • 74
    • 34547512927 scopus 로고    scopus 로고
    • Structure-function relationships of a catalytically efficient β-d-xylosidase
    • Jordan D., Li X.L., Dunlap C., Whitehead T., Cotta M. Structure-function relationships of a catalytically efficient β-d-xylosidase. Appl Biochem Biotechnol 2007, 141:51-76.
    • (2007) Appl Biochem Biotechnol , vol.141 , pp. 51-76
    • Jordan, D.1    Li, X.L.2    Dunlap, C.3    Whitehead, T.4    Cotta, M.5
  • 75
    • 84877736470 scopus 로고    scopus 로고
    • Highly active β-xylosidases of glycoside hydrolase family 43 operating on natural and artificial substrates
    • Jordan D.B., Wagschal K., Grigorescu A.A., Braker J.D. Highly active β-xylosidases of glycoside hydrolase family 43 operating on natural and artificial substrates. Appl Microbiol Biotechnol 2013, 97:4415-4428.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 4415-4428
    • Jordan, D.B.1    Wagschal, K.2    Grigorescu, A.A.3    Braker, J.D.4
  • 77
    • 0031662792 scopus 로고    scopus 로고
    • Purification and substrate specificities of two α-l-arabinofuranosidases from Aspergillus awamori IFO 4033
    • Kaneko S., Arimoto M., Ohba M., Kobayashi H., Ishii T., Kusakabe I. Purification and substrate specificities of two α-l-arabinofuranosidases from Aspergillus awamori IFO 4033. Appl Environ Microbiol 1998, 64:4021-4027.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4021-4027
    • Kaneko, S.1    Arimoto, M.2    Ohba, M.3    Kobayashi, H.4    Ishii, T.5    Kusakabe, I.6
  • 78
    • 0025605798 scopus 로고
    • Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes
    • Kellett L.E., Poole D.M., Ferreira L.M., Durrant A.J., Hazlewood G.P., Gilbert H.J. Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes. Biochem J 1990, 272:369-376.
    • (1990) Biochem J , vol.272 , pp. 369-376
    • Kellett, L.E.1    Poole, D.M.2    Ferreira, L.M.3    Durrant, A.J.4    Hazlewood, G.P.5    Gilbert, H.J.6
  • 80
    • 0031832740 scopus 로고    scopus 로고
    • ArfI and arfII, two genes encoding α-l-arabinofuranosidases in Cytophaga xylanolytica
    • Kim K.S., Lilburn T.G., Renner M.J., Breznak J.A. arfI and arfII, two genes encoding α-l-arabinofuranosidases in Cytophaga xylanolytica. Appl Environ Microbiol 1998, 64:1919-1923.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1919-1923
    • Kim, K.S.1    Lilburn, T.G.2    Renner, M.J.3    Breznak, J.A.4
  • 81
    • 0034004579 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of an α-l-arabinofuranosidase from Aspergillus sojae
    • Kimura I., Yoshioka N., Kimura Y., Tajima S. Cloning, sequencing and expression of an α-l-arabinofuranosidase from Aspergillus sojae. J Biosci Bioeng 2000, 89:262-266.
    • (2000) J Biosci Bioeng , vol.89 , pp. 262-266
    • Kimura, I.1    Yoshioka, N.2    Kimura, Y.3    Tajima, S.4
  • 82
    • 0027907989 scopus 로고
    • Mode of action of (1,4)-β-d-arabinoxylan arabinofuranohydrolase (AXH) and α-l-arabinofuranosidases on alkali-extractable wheat-flour arabinoxylan
    • Kormelink F.J.M., Gruppen H., Voragen A.G.J. Mode of action of (1,4)-β-d-arabinoxylan arabinofuranohydrolase (AXH) and α-l-arabinofuranosidases on alkali-extractable wheat-flour arabinoxylan. Carbohydr Res 1993, 249:345-353.
    • (1993) Carbohydr Res , vol.249 , pp. 345-353
    • Kormelink, F.J.M.1    Gruppen, H.2    Voragen, A.G.J.3
  • 83
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland D.E. Stereochemistry and the mechanism of enzymatic reactions. Biol Rev 1953, 28:416-436.
    • (1953) Biol Rev , vol.28 , pp. 416-436
    • Koshland, D.E.1
  • 84
    • 0036952134 scopus 로고    scopus 로고
    • Characterization of two noncellulosomal subunits, ArfA and BgaA, from Clostridium cellulovorans that cooperate with the cellulosome in plant cell wall degradation
    • Kosugi A., Murashima K., Doi R.H. Characterization of two noncellulosomal subunits, ArfA and BgaA, from Clostridium cellulovorans that cooperate with the cellulosome in plant cell wall degradation. J Bacteriol 2002, 184:6859-6865.
    • (2002) J Bacteriol , vol.184 , pp. 6859-6865
    • Kosugi, A.1    Murashima, K.2    Doi, R.H.3
  • 85
    • 70350451411 scopus 로고    scopus 로고
    • Molecular cloning and expression in Pichia pastoris of a Irpex lacteus exo-β-(1-3)-galactanase gene
    • Kotake T., Kitazawa K., Takata R., Okabe K., Ichinose H., Kaneko S., et al. Molecular cloning and expression in Pichia pastoris of a Irpex lacteus exo-β-(1-3)-galactanase gene. Biosci Biotechnol Biochem 2009, 73:2303-2309.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 2303-2309
    • Kotake, T.1    Kitazawa, K.2    Takata, R.3    Okabe, K.4    Ichinose, H.5    Kaneko, S.6
  • 86
    • 33747892378 scopus 로고    scopus 로고
    • An α-l-arabinofuranosidase/β-d-xylosidase from immature seeds of radish (Raphanus sativus L.)
    • Kotake T., Tsuchiya K., Aohara T., Konishi T., Kaneko S., Igarashi K., et al. An α-l-arabinofuranosidase/β-d-xylosidase from immature seeds of radish (Raphanus sativus L.). J Exp Bot 2006, 57:2353-2362.
    • (2006) J Exp Bot , vol.57 , pp. 2353-2362
    • Kotake, T.1    Tsuchiya, K.2    Aohara, T.3    Konishi, T.4    Kaneko, S.5    Igarashi, K.6
  • 88
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • Kulkarni N., Shendye A., Rao M. Molecular and biotechnological aspects of xylanases. FEMS Microbiol Rev 1999, 23:411-456.
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye, A.2    Rao, M.3
  • 89
    • 0033844476 scopus 로고    scopus 로고
    • Coexpression of the Bacillus pumilus β-xylosidase (xynB) gene with the Trichoderma reesei β-xylanase 2 (xyn2) gene in the yeast Saccharomyces cerevisiae
    • La Grange D.C., Claeyssens M., Pretorius I.S., Van Zyl W.H. Coexpression of the Bacillus pumilus β-xylosidase (xynB) gene with the Trichoderma reesei β-xylanase 2 (xyn2) gene in the yeast Saccharomyces cerevisiae. Appl Microbiol Biotechnol 2000, 54:195-200.
    • (2000) Appl Microbiol Biotechnol , vol.54 , pp. 195-200
    • La Grange, D.C.1    Claeyssens, M.2    Pretorius, I.S.3    Van Zyl, W.H.4
  • 91
    • 34548209675 scopus 로고    scopus 로고
    • Recombinant expression and characterization of a reducing-end xylose-releasing exo-oligoxylanase from Bifidobacterium adolescentis
    • Lagaert S., Van Campenhout S., Pollet A., Bourgois T.M., Delcour J.A., Courtin C.M., et al. Recombinant expression and characterization of a reducing-end xylose-releasing exo-oligoxylanase from Bifidobacterium adolescentis. Appl Environ Microbiol 2007, 73:5374-5377.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 5374-5377
    • Lagaert, S.1    Van Campenhout, S.2    Pollet, A.3    Bourgois, T.M.4    Delcour, J.A.5    Courtin, C.M.6
  • 92
    • 78649442942 scopus 로고    scopus 로고
    • Substrate specificity of three recombinant α-l-arabinofuranosidases from Bifidobacterium adolescentis and their divergent action on arabinoxylan and arabinoxylan oligosaccharides
    • Lagaert S., Pollet A., Delcour J.A., Lavigne R., Courtin C.M., Volckaert G. Substrate specificity of three recombinant α-l-arabinofuranosidases from Bifidobacterium adolescentis and their divergent action on arabinoxylan and arabinoxylan oligosaccharides. Biochem Biophys Res Commun 2010, 402:644-650.
    • (2010) Biochem Biophys Res Commun , vol.402 , pp. 644-650
    • Lagaert, S.1    Pollet, A.2    Delcour, J.A.3    Lavigne, R.4    Courtin, C.M.5    Volckaert, G.6
  • 93
    • 82455208964 scopus 로고    scopus 로고
    • Characterization of two β-xylosidases from Bifidobacterium adolescentis and their contribution to the hydrolysis of prebiotic xylooligosaccharides
    • Lagaert S., Pollet A., Delcour J.A., Lavigne R., Courtin C.M., Volckaert G. Characterization of two β-xylosidases from Bifidobacterium adolescentis and their contribution to the hydrolysis of prebiotic xylooligosaccharides. Appl Microbiol Biotechnol 2011, 92:1179-1185.
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 1179-1185
    • Lagaert, S.1    Pollet, A.2    Delcour, J.A.3    Lavigne, R.4    Courtin, C.M.5    Volckaert, G.6
  • 96
    • 0035874475 scopus 로고    scopus 로고
    • Barley arabinoxylan arabinofuranohydrolases: purification, characterization and determination of primary structures from cDNA clones
    • Lee R.C., Burton R.A., Hrmova M., Fincher G.B. Barley arabinoxylan arabinofuranohydrolases: purification, characterization and determination of primary structures from cDNA clones. Biochem J 2001, 356:181-189.
    • (2001) Biochem J , vol.356 , pp. 181-189
    • Lee, R.C.1    Burton, R.A.2    Hrmova, M.3    Fincher, G.B.4
  • 97
    • 0038413775 scopus 로고    scopus 로고
    • Bifunctional family 3 glycoside hydrolases from barley with α-l-arabinofuranosidase and β-d-xylosidase activity
    • Lee R.C., Hrmova M., Burton R.A., Lahnstein J., Fincher G.B. Bifunctional family 3 glycoside hydrolases from barley with α-l-arabinofuranosidase and β-d-xylosidase activity. J Biol Chem 2003, 278:5377-5387.
    • (2003) J Biol Chem , vol.278 , pp. 5377-5387
    • Lee, R.C.1    Hrmova, M.2    Burton, R.A.3    Lahnstein, J.4    Fincher, G.B.5
  • 98
    • 0027234633 scopus 로고
    • Genetic organization, sequence and biochemical characterization of recombinant β-xylosidase from Thermoanaerobacterium saccharolyticum strain B6Α-RI
    • Lee Y.E., Zeikus J.G. Genetic organization, sequence and biochemical characterization of recombinant β-xylosidase from Thermoanaerobacterium saccharolyticum strain B6Α-RI. J Gen Microbiol 1993, 139:1235-1243.
    • (1993) J Gen Microbiol , vol.139 , pp. 1235-1243
    • Lee, Y.E.1    Zeikus, J.G.2
  • 99
    • 77956896301 scopus 로고    scopus 로고
    • Hydrolytic properties of a thermostable α-l-arabinofuranosidase from Caldicellulosiruptor saccharolyticus
    • Lim Y.R., Yoon R.Y., Seo E.S., Kim Y.S., Park C.S., Oh D.K. Hydrolytic properties of a thermostable α-l-arabinofuranosidase from Caldicellulosiruptor saccharolyticus. J Appl Microbiol 2010, 109:1188-1197.
    • (2010) J Appl Microbiol , vol.109 , pp. 1188-1197
    • Lim, Y.R.1    Yoon, R.Y.2    Seo, E.S.3    Kim, Y.S.4    Park, C.S.5    Oh, D.K.6
  • 100
    • 78149234937 scopus 로고    scopus 로고
    • Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism
    • Litzinger S., Fischer S., Polzer P., Diederichs K., Welte W., Mayer C. Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism. J Biol Chem 2010, 285:35675-35684.
    • (2010) J Biol Chem , vol.285 , pp. 35675-35684
    • Litzinger, S.1    Fischer, S.2    Polzer, P.3    Diederichs, K.4    Welte, W.5    Mayer, C.6
  • 102
    • 0034682041 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of the bifunctional xylosidase-arabinosidase from the anaerobic thermophile Thermoanaerobacter ethanolicus
    • Mai V., Wiegel J., Lorenz W.W. Cloning, sequencing, and characterization of the bifunctional xylosidase-arabinosidase from the anaerobic thermophile Thermoanaerobacter ethanolicus. Gene 2000, 247:137-143.
    • (2000) Gene , vol.247 , pp. 137-143
    • Mai, V.1    Wiegel, J.2    Lorenz, W.W.3
  • 103
    • 0028170281 scopus 로고
    • Purification and characterization of an α-l-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA)
    • Manin C., Shareek F., Morosoli R., Kluepfel D. Purification and characterization of an α-l-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA). Biochem J 1994, 302:443-449.
    • (1994) Biochem J , vol.302 , pp. 443-449
    • Manin, C.1    Shareek, F.2    Morosoli, R.3    Kluepfel, D.4
  • 104
    • 0141482166 scopus 로고    scopus 로고
    • Purification and functional characterization of a novel α-l-arabinofuranosidase from Bifidobacterium longum B667
    • Margolles A., de los Reyes-Gavilán C.G. Purification and functional characterization of a novel α-l-arabinofuranosidase from Bifidobacterium longum B667. Appl Environ Microbiol 2003, 69:5096-5103.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 5096-5103
    • Margolles, A.1    de los Reyes-Gavilán, C.G.2
  • 105
    • 0034652374 scopus 로고    scopus 로고
    • Purification, characterization and gene cloning of two α-l-arabinofuranosidases from Streptomyces chartreusis GS901
    • Matsuo N., Kaneko S., Kuno A., Kobayashi H., Kusakabe I. Purification, characterization and gene cloning of two α-l-arabinofuranosidases from Streptomyces chartreusis GS901. Biochem J 2000, 346:9-15.
    • (2000) Biochem J , vol.346 , pp. 9-15
    • Matsuo, N.1    Kaneko, S.2    Kuno, A.3    Kobayashi, H.4    Kusakabe, I.5
  • 106
    • 84860122751 scopus 로고    scopus 로고
    • Introducing endo-xylanase activity into an exo-acting arabinofuranosidase that targets side chains
    • McKee L.S., Peña M.J., Rogowski A., Jackson A., Lewis R.J., York W.S., et al. Introducing endo-xylanase activity into an exo-acting arabinofuranosidase that targets side chains. Proc Natl Acad Sci U S A 2012, 109:6537-6542.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 6537-6542
    • McKee, L.S.1    Peña, M.J.2    Rogowski, A.3    Jackson, A.4    Lewis, R.J.5    York, W.S.6
  • 107
    • 0030944842 scopus 로고    scopus 로고
    • Arabinanase A from Pseudomonas fluorescens subsp. cellulosa exhibits both an endo- and an exo- mode of action
    • McKie V.A., Black G.W., Millward-Sadler S.J., Hazlewood G.P., Laurie J.I., Gilbert H.J. Arabinanase A from Pseudomonas fluorescens subsp. cellulosa exhibits both an endo- and an exo- mode of action. Biochem J 1997, 323:547-555.
    • (1997) Biochem J , vol.323 , pp. 547-555
    • McKie, V.A.1    Black, G.W.2    Millward-Sadler, S.J.3    Hazlewood, G.P.4    Laurie, J.I.5    Gilbert, H.J.6
  • 108
    • 3042627669 scopus 로고    scopus 로고
    • Purification and characterization of enzymes exhibiting β-d-xylosidase activities in stem tissues of Arabidopsis
    • Minic Z., Rihouey C., Do C.T., Lerouge P., Jouanin L. Purification and characterization of enzymes exhibiting β-d-xylosidase activities in stem tissues of Arabidopsis. Plant Physiol 2004, 135:867-878.
    • (2004) Plant Physiol , vol.135 , pp. 867-878
    • Minic, Z.1    Rihouey, C.2    Do, C.T.3    Lerouge, P.4    Jouanin, L.5
  • 110
    • 33750575137 scopus 로고    scopus 로고
    • The family 42 carbohydrate-binding module of family 54 α-l-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose
    • Miyanaga A., Koseki T., Miwa Y., Mese Y., Nakamura S., Kuno A., et al. The family 42 carbohydrate-binding module of family 54 α-l-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose. Biochem J 2006, 399:503-511.
    • (2006) Biochem J , vol.399 , pp. 503-511
    • Miyanaga, A.1    Koseki, T.2    Miwa, Y.3    Mese, Y.4    Nakamura, S.5    Kuno, A.6
  • 111
    • 7244254401 scopus 로고    scopus 로고
    • Crystal structure of a family 54 α-l-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose
    • Miyanaga A., Koseki T., Matsuzawa H., Wakagi T., Shoun H., Fushinobu S. Crystal structure of a family 54 α-l-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose. J Biol Chem 2004, 279:44907-44914.
    • (2004) J Biol Chem , vol.279 , pp. 44907-44914
    • Miyanaga, A.1    Koseki, T.2    Matsuzawa, H.3    Wakagi, T.4    Shoun, H.5    Fushinobu, S.6
  • 112
    • 26444500989 scopus 로고    scopus 로고
    • Hyperthermophilic a-l-arabinofuranosidase from Thermotoga maritima MSB8: molecular cloning, gene expression, and characterization of the recombinant protein
    • Miyazaki K. Hyperthermophilic a-l-arabinofuranosidase from Thermotoga maritima MSB8: molecular cloning, gene expression, and characterization of the recombinant protein. Extremophiles 2005, 9:399-406.
    • (2005) Extremophiles , vol.9 , pp. 399-406
    • Miyazaki, K.1
  • 113
    • 0028882679 scopus 로고
    • Purification and characterization of an arabinofuranosidase from Bacillus polymyxa expressed in Bacillus subtilis
    • Morales P., Sendra J.M., Pérez-González J.A. Purification and characterization of an arabinofuranosidase from Bacillus polymyxa expressed in Bacillus subtilis. Appl Microbiol Biotechnol 1995, 44:112-117.
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 112-117
    • Morales, P.1    Sendra, J.M.2    Pérez-González, J.A.3
  • 114
    • 33846128482 scopus 로고    scopus 로고
    • Gene cloning and expression in Escherichia coli of a bi-functional β-d-xylosidase/α-l-arabinosidase from Sulfolobus solfataricus involved in xylan degradation
    • Morana A., Paris O., Maurelli L., Rossi M., Cannio R. Gene cloning and expression in Escherichia coli of a bi-functional β-d-xylosidase/α-l-arabinosidase from Sulfolobus solfataricus involved in xylan degradation. Extremophiles 2007, 11:123-132.
    • (2007) Extremophiles , vol.11 , pp. 123-132
    • Morana, A.1    Paris, O.2    Maurelli, L.3    Rossi, M.4    Cannio, R.5
  • 115
    • 77954429078 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of BxlA, an intracellular β-d-xylosidase from Streptomyces thermoviolaceus OPC-520
    • Morioka H., Miki Y., Saito K., Tomoo K., Ishida T., Hasegawa T., et al. Crystallization and preliminary X-ray crystallographic analysis of BxlA, an intracellular β-d-xylosidase from Streptomyces thermoviolaceus OPC-520. Acta Crystallogr Sect F Struct Biol Cryst Commun 2010, 66:791-793.
    • (2010) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.66 , pp. 791-793
    • Morioka, H.1    Miki, Y.2    Saito, K.3    Tomoo, K.4    Ishida, T.5    Hasegawa, T.6
  • 116
    • 0033136098 scopus 로고    scopus 로고
    • Family 10 and 11 xylanase genes from Caldicellulosiruptor sp. strain Rt69B.1
    • Morris D.D., Gibbs M.D., Ford M., Thomas J., Bergquist P.L. Family 10 and 11 xylanase genes from Caldicellulosiruptor sp. strain Rt69B.1. Extremophiles 1999, 3:103-111.
    • (1999) Extremophiles , vol.3 , pp. 103-111
    • Morris, D.D.1    Gibbs, M.D.2    Ford, M.3    Thomas, J.4    Bergquist, P.L.5
  • 117
    • 63249108767 scopus 로고    scopus 로고
    • Evaluation of the transglycosylation activities of a GH 39 β-d-xylosidase for the synthesis of xylose-based glycosides
    • Muzard M., Aubry N., Plantier-Royon R., O'Donohue M., Rémond C. Evaluation of the transglycosylation activities of a GH 39 β-d-xylosidase for the synthesis of xylose-based glycosides. J Mol Catal B: Enzym 2009, 58:1-5.
    • (2009) J Mol Catal B: Enzym , vol.58 , pp. 1-5
    • Muzard, M.1    Aubry, N.2    Plantier-Royon, R.3    O'Donohue, M.4    Rémond, C.5
  • 118
    • 0025608736 scopus 로고
    • Purification and properties of thermostable xylanase and β-xylosidase produced by a newly isolated Bacillus stearothermophilus strain
    • Nanmori T., Watanabe T., Shinke R., Kohno A., Kawamura Y. Purification and properties of thermostable xylanase and β-xylosidase produced by a newly isolated Bacillus stearothermophilus strain. J Bacteriol 1990, 172:6669-6672.
    • (1990) J Bacteriol , vol.172 , pp. 6669-6672
    • Nanmori, T.1    Watanabe, T.2    Shinke, R.3    Kohno, A.4    Kawamura, Y.5
  • 119
    • 0032828923 scopus 로고    scopus 로고
    • An α-l-arabinofuranosidase from Trichoderma reesei containing a noncatalytic xylan-binding domain
    • Nogawa M., Yatsui K., Tomioka A., Okada H., Morikawa Y. An α-l-arabinofuranosidase from Trichoderma reesei containing a noncatalytic xylan-binding domain. Appl Environ Microbiol 1999, 65:3964-3968.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3964-3968
    • Nogawa, M.1    Yatsui, K.2    Tomioka, A.3    Okada, H.4    Morikawa, Y.5
  • 121
    • 84881107323 scopus 로고    scopus 로고
    • Characterization of a glycoside hydrolase family-51 α-l-arabinofuranosidase gene from Aureobasidium pullulans ATCC 20524 and its encoded product
    • Ohta K., Fujii S., Higashida C. Characterization of a glycoside hydrolase family-51 α-l-arabinofuranosidase gene from Aureobasidium pullulans ATCC 20524 and its encoded product. J Biosci Bioeng 2013, 116:287-292.
    • (2013) J Biosci Bioeng , vol.116 , pp. 287-292
    • Ohta, K.1    Fujii, S.2    Higashida, C.3
  • 122
    • 1542374649 scopus 로고    scopus 로고
    • Paenibacillus sp. TS12 glucosylceramidase: kinetic studies of a novel sub-family of family 3 glycosidases and identification of the catalytic residues
    • Paal K., Ito M., Withers S.G. Paenibacillus sp. TS12 glucosylceramidase: kinetic studies of a novel sub-family of family 3 glycosidases and identification of the catalytic residues. Biochem J 2004, 378:141.
    • (2004) Biochem J , vol.378 , pp. 141
    • Paal, K.1    Ito, M.2    Withers, S.G.3
  • 123
    • 47249161669 scopus 로고    scopus 로고
    • The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit
    • Paës G., Skov L.K., O'Donohue M.J., Rémond C., Kastrup J.S., Gajhede M., et al. The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit. Biochemistry 2008, 47:7441-7451.
    • (2008) Biochemistry , vol.47 , pp. 7441-7451
    • Paës, G.1    Skov, L.K.2    O'Donohue, M.J.3    Rémond, C.4    Kastrup, J.S.5    Gajhede, M.6
  • 124
    • 0021765009 scopus 로고
    • Isolation of two b-xylosidase genes of Bacillus pumilus and comparison of their gene products
    • Panbangred W., Kawaguchi O., Tomita T., Shinmyo A., Okada H. Isolation of two b-xylosidase genes of Bacillus pumilus and comparison of their gene products. Eur J Biochem 1984, 138:267-273.
    • (1984) Eur J Biochem , vol.138 , pp. 267-273
    • Panbangred, W.1    Kawaguchi, O.2    Tomita, T.3    Shinmyo, A.4    Okada, H.5
  • 125
    • 43549097333 scopus 로고    scopus 로고
    • Cell-wall carbohydrates and their modification as a resource for biofuels
    • Pauly M., Keegstra K. Cell-wall carbohydrates and their modification as a resource for biofuels. Plant J 2008, 54:559-568.
    • (2008) Plant J , vol.54 , pp. 559-568
    • Pauly, M.1    Keegstra, K.2
  • 126
    • 38349109419 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular α-l-arabinosidase from a novel isolate Bacillus pumilus ARA and its over-expression in Escherichia coli
    • Pei J., Shao W. Purification and characterization of an extracellular α-l-arabinosidase from a novel isolate Bacillus pumilus ARA and its over-expression in Escherichia coli. Appl Microbiol Biotechnol 2008, 78:115-121.
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 115-121
    • Pei, J.1    Shao, W.2
  • 127
    • 0002326885 scopus 로고
    • Isolation and composition of the soluble pentosans of wheat flours
    • Perlin A.S. Isolation and composition of the soluble pentosans of wheat flours. Cereal Chem 1951, 28:370-381.
    • (1951) Cereal Chem , vol.28 , pp. 370-381
    • Perlin, A.S.1
  • 128
    • 0002326885 scopus 로고
    • Structure of the soluble pentosans of wheat flours
    • Perlin A.S. Structure of the soluble pentosans of wheat flours. Cereal Chem 1951, 28:382-393.
    • (1951) Cereal Chem , vol.28 , pp. 382-393
    • Perlin, A.S.1
  • 129
    • 0030602181 scopus 로고    scopus 로고
    • Stereochemical course of hydrolysis catalyzed by arabinofuranosyl hydrolases
    • Pitson S.M., Voragen A.G.J., Beldman G. Stereochemical course of hydrolysis catalyzed by arabinofuranosyl hydrolases. FEBS Lett 1996, 398:7-11.
    • (1996) FEBS Lett , vol.398 , pp. 7-11
    • Pitson, S.M.1    Voragen, A.G.J.2    Beldman, G.3
  • 130
    • 77955554477 scopus 로고    scopus 로고
    • Structural determinants of the substrate specificities of xylanases from different glycoside hydrolase families
    • Pollet A., Delcour J.A., Courtin C.M. Structural determinants of the substrate specificities of xylanases from different glycoside hydrolase families. Crit Rev Biotechnol 2010, 30:176-191.
    • (2010) Crit Rev Biotechnol , vol.30 , pp. 176-191
    • Pollet, A.1    Delcour, J.A.2    Courtin, C.M.3
  • 131
    • 77955561000 scopus 로고    scopus 로고
    • Functional analysis of glycoside hydrolase family 8 xylanases shows narrow but distinct substrate specificities and biotechnological potential
    • Pollet A., Schoepe J., Dornez E., Strelkov S.V., Delcour J.A., Courtin C.M. Functional analysis of glycoside hydrolase family 8 xylanases shows narrow but distinct substrate specificities and biotechnological potential. Appl Microbiol Biotechnol 2010, 87:2125-2135.
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 2125-2135
    • Pollet, A.1    Schoepe, J.2    Dornez, E.3    Strelkov, S.V.4    Delcour, J.A.5    Courtin, C.M.6
  • 132
    • 1042291218 scopus 로고    scopus 로고
    • Three acidic residues are at the active site of a β-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68
    • Pons T., Naumoff D.G., Martinez-Fleites C., Hernandez L. Three acidic residues are at the active site of a β-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68. Proteins 2004, 54:424-432.
    • (2004) Proteins , vol.54 , pp. 424-432
    • Pons, T.1    Naumoff, D.G.2    Martinez-Fleites, C.3    Hernandez, L.4
  • 133
    • 77649336582 scopus 로고    scopus 로고
    • Structural and functional analyses of β-glucosidase 3B from Thermotoga neapolitana: a thermostable three-domain representative of glycoside hydrolase 3
    • Pozzo T., Pasten J.L., Karlsson E.N., Logan D.T. Structural and functional analyses of β-glucosidase 3B from Thermotoga neapolitana: a thermostable three-domain representative of glycoside hydrolase 3. J Mol Biol 2010, 397:724-739.
    • (2010) J Mol Biol , vol.397 , pp. 724-739
    • Pozzo, T.1    Pasten, J.L.2    Karlsson, E.N.3    Logan, D.T.4
  • 134
    • 14544271931 scopus 로고    scopus 로고
    • Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A
    • Proctor M.R., Taylor E.J., Nurizzo D., Turkenburg J.P., Lloyd R.M., Vardakou M., et al. Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A. Proc Natl Acad Sci U S A 2005, 102:2697-2702.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2697-2702
    • Proctor, M.R.1    Taylor, E.J.2    Nurizzo, D.3    Turkenburg, J.P.4    Lloyd, R.M.5    Vardakou, M.6
  • 135
    • 33947661471 scopus 로고    scopus 로고
    • Isolation and characterization of a thermostable β-xylosidase in the thermophilic bacterium Geobacillus pallidus
    • Quintero D., Velasco Z., Hurtado-Gomez E., Neira J.L., Contreras L.M. Isolation and characterization of a thermostable β-xylosidase in the thermophilic bacterium Geobacillus pallidus. Biochim Biophys Acta 2007, 1774:510-518.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 510-518
    • Quintero, D.1    Velasco, Z.2    Hurtado-Gomez, E.3    Neira, J.L.4    Contreras, L.M.5
  • 136
    • 33746913962 scopus 로고    scopus 로고
    • Mode of action and properties of the β-xylosidases from Talaromyces emersonii and Trichoderma reesei
    • Rasmussen L.E., Sørensen H.R., Vind J., Viksø-Nielsen A. Mode of action and properties of the β-xylosidases from Talaromyces emersonii and Trichoderma reesei. Biotechnol Bioeng 2006, 94:869-876.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 869-876
    • Rasmussen, L.E.1    Sørensen, H.R.2    Vind, J.3    Viksø-Nielsen, A.4
  • 137
    • 84865604955 scopus 로고    scopus 로고
    • Enzyme kinetics and identification of the rate-limiting step of enzymatic arabinoxylan degradation
    • Rasmussen L.E., Xu C., Sørensen J.F., Nielsen M.K., Meyer A.S. Enzyme kinetics and identification of the rate-limiting step of enzymatic arabinoxylan degradation. Biochem Eng J 2012, 69:8-16.
    • (2012) Biochem Eng J , vol.69 , pp. 8-16
    • Rasmussen, L.E.1    Xu, C.2    Sørensen, J.F.3    Nielsen, M.K.4    Meyer, A.S.5
  • 138
    • 39649122848 scopus 로고    scopus 로고
    • Action of a GH 51 α-l-arabinofuranosidase on wheat-derived arabinoxylans and arabino-xylooligosaccharides
    • Rémond C., Boukari I., Chambat G., O'Donohue M. Action of a GH 51 α-l-arabinofuranosidase on wheat-derived arabinoxylans and arabino-xylooligosaccharides. Carbohydr Polym 2008, 72:424-430.
    • (2008) Carbohydr Polym , vol.72 , pp. 424-430
    • Rémond, C.1    Boukari, I.2    Chambat, G.3    O'Donohue, M.4
  • 139
    • 0031985280 scopus 로고    scopus 로고
    • Purification and properties of ArfI, an α-l-arabinofuranosidase from Cytophaga xylanolytica
    • Renner M.J., Breznak J.A. Purification and properties of ArfI, an α-l-arabinofuranosidase from Cytophaga xylanolytica. Appl Environ Microbiol 1998, 64:43-52.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 43-52
    • Renner, M.J.1    Breznak, J.A.2
  • 140
    • 28244477099 scopus 로고    scopus 로고
    • Structural insights into the β-Xylosidase from Trichoderma reesei obtained by synchrotron small-angle X-ray scattering and circular dichroism spectroscopy
    • Rojas A.L., Fischer H., Eneiskaya E.V., Kulminskaya A.A., Shabalin K.A., Neustroev K.N., et al. Structural insights into the β-Xylosidase from Trichoderma reesei obtained by synchrotron small-angle X-ray scattering and circular dichroism spectroscopy. Biochemistry 2005, 44:15578-15584.
    • (2005) Biochemistry , vol.44 , pp. 15578-15584
    • Rojas, A.L.1    Fischer, H.2    Eneiskaya, E.V.3    Kulminskaya, A.A.4    Shabalin, K.A.5    Neustroev, K.N.6
  • 142
    • 0037623814 scopus 로고    scopus 로고
    • Hemicellulose bioconversion
    • Saha B. Hemicellulose bioconversion. J Ind Microbiol Biotechnol 2003, 30:279-291.
    • (2003) J Ind Microbiol Biotechnol , vol.30 , pp. 279-291
    • Saha, B.1
  • 143
    • 84856406038 scopus 로고    scopus 로고
    • Molecular identification of a cold-adapted endo-arabinanase of Penicillium chrysogenum
    • Sakamoto T., Ihara H., Shibano A., Nagahiro H., Kawasaki H. Molecular identification of a cold-adapted endo-arabinanase of Penicillium chrysogenum. J Appl Glycosci 2005, 52:369-372.
    • (2005) J Appl Glycosci , vol.52 , pp. 369-372
    • Sakamoto, T.1    Ihara, H.2    Shibano, A.3    Nagahiro, H.4    Kawasaki, H.5
  • 144
    • 84874113993 scopus 로고    scopus 로고
    • Substrate specificity and gene expression of two Penicillium chrysogenum α-l-arabinofuranosidases (AFQ1 and AFS1) belonging to glycoside hydrolase families 51 and 54
    • Sakamoto T., Inui M., Yasui K., Hosokawa S., Ihara H. Substrate specificity and gene expression of two Penicillium chrysogenum α-l-arabinofuranosidases (AFQ1 and AFS1) belonging to glycoside hydrolase families 51 and 54. Appl Microbiol Biotechnol 2013, 97:1121-1130.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 1121-1130
    • Sakamoto, T.1    Inui, M.2    Yasui, K.3    Hosokawa, S.4    Ihara, H.5
  • 145
    • 0037414560 scopus 로고    scopus 로고
    • Purification and properties of two type-B α-l-arabinofuranosidases produced by Penicillium chrysogenum
    • Sakamoto T., Kawasaki H. Purification and properties of two type-B α-l-arabinofuranosidases produced by Penicillium chrysogenum. Biochim Biophys Acta 2003, 1621:204-210.
    • (2003) Biochim Biophys Acta , vol.1621 , pp. 204-210
    • Sakamoto, T.1    Kawasaki, H.2
  • 146
    • 79954938986 scopus 로고    scopus 로고
    • Identification of a GH62 α-l-arabinofuranosidase specific for arabinoxylan produced by Penicillium chrysogenum
    • Sakamoto T., Ogura A., Inui M., Tokuda S., Hosokawa S., Ihara H., et al. Identification of a GH62 α-l-arabinofuranosidase specific for arabinoxylan produced by Penicillium chrysogenum. Appl Microbiol Biotechnol 2011, 90:137-146.
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 137-146
    • Sakamoto, T.1    Ogura, A.2    Inui, M.3    Tokuda, S.4    Hosokawa, S.5    Ihara, H.6
  • 147
    • 0030924909 scopus 로고    scopus 로고
    • Molecular cloning and nucleotide sequence of an endo-1,5-α-l-arabinase gene from Bacillus subtilis
    • Sakamoto T., Yamada M., Kawasaki H., Sakai T. Molecular cloning and nucleotide sequence of an endo-1,5-α-l-arabinase gene from Bacillus subtilis. Eur J Biochem 1997, 245:708-714.
    • (1997) Eur J Biochem , vol.245 , pp. 708-714
    • Sakamoto, T.1    Yamada, M.2    Kawasaki, H.3    Sakai, T.4
  • 150
    • 0024618051 scopus 로고
    • Identification of the Butyrivibrio fibrisolvens xylosidase gene (xylB) coding region and its expression in Escherichia coli
    • Sewell G.W., Utt E.A., Hespell R.B., Mackenzie K.F., Ingram L.O. Identification of the Butyrivibrio fibrisolvens xylosidase gene (xylB) coding region and its expression in Escherichia coli. Appl Environ Microbiol 1989, 55:306-311.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 306-311
    • Sewell, G.W.1    Utt, E.A.2    Hespell, R.B.3    Mackenzie, K.F.4    Ingram, L.O.5
  • 151
    • 19944427947 scopus 로고    scopus 로고
    • Biochemical characterization and identification of the catalytic residues of a family 43 β-d-xylosidase from Geobacillus stearothermophilus T-6
    • Shallom D., Leon M., Bravman T., Ben-David A., Zaide G., Belakhov V., et al. Biochemical characterization and identification of the catalytic residues of a family 43 β-d-xylosidase from Geobacillus stearothermophilus T-6. Biochemistry (Mosc) 2005, 44:387-397.
    • (2005) Biochemistry (Mosc) , vol.44 , pp. 387-397
    • Shallom, D.1    Leon, M.2    Bravman, T.3    Ben-David, A.4    Zaide, G.5    Belakhov, V.6
  • 152
    • 0037070548 scopus 로고    scopus 로고
    • The identification of the acid-base catalyst of a-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase
    • Shallom D., Belakhov V., Solomon D., Gilead-Gropper S., Baasov T., Shoham G., et al. The identification of the acid-base catalyst of a-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase. FEBS Lett 2002, 514:163-167.
    • (2002) FEBS Lett , vol.514 , pp. 163-167
    • Shallom, D.1    Belakhov, V.2    Solomon, D.3    Gilead-Gropper, S.4    Baasov, T.5    Shoham, G.6
  • 153
    • 0346319022 scopus 로고    scopus 로고
    • Detailed kinetic analysis and identification of the nucleophile in α-l-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase
    • Shallom D., Belakhov V., Solomon D., Shoham G., Baasov T., Shoham Y. Detailed kinetic analysis and identification of the nucleophile in α-l-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase. J Biol Chem 2002, 277:43667-43673.
    • (2002) J Biol Chem , vol.277 , pp. 43667-43673
    • Shallom, D.1    Belakhov, V.2    Solomon, D.3    Shoham, G.4    Baasov, T.5    Shoham, Y.6
  • 154
    • 79551476044 scopus 로고    scopus 로고
    • Characterization of a novel β-xylosidase, XylC, from Thermoanaerobacterium saccharolyticum JW/SL-YS485
    • Shao W., Xue Y., Wu A., Kataeva I., Pei J., Wu H., et al. Characterization of a novel β-xylosidase, XylC, from Thermoanaerobacterium saccharolyticum JW/SL-YS485. Appl Environ Microbiol 2011, 77:719-726.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 719-726
    • Shao, W.1    Xue, Y.2    Wu, A.3    Kataeva, I.4    Pei, J.5    Wu, H.6
  • 155
    • 77954887963 scopus 로고    scopus 로고
    • Gene cloning, expression, and characterization of a family 51 α-l-arabinofuranosidase from Streptomyces sp. S9
    • Shi P., Li N., Yang P., Wang Y., Luo H., Bai Y., et al. Gene cloning, expression, and characterization of a family 51 α-l-arabinofuranosidase from Streptomyces sp. S9. Appl Biochem Biotechnol 2010, 162:707-718.
    • (2010) Appl Biochem Biotechnol , vol.162 , pp. 707-718
    • Shi, P.1    Li, N.2    Yang, P.3    Wang, Y.4    Luo, H.5    Bai, Y.6
  • 156
    • 11944256494 scopus 로고
    • Catalytic mechanism of enzymic glycosyl transfer
    • Sinnott M.L. Catalytic mechanism of enzymic glycosyl transfer. Chem Rev 1990, 90:1171-1202.
    • (1990) Chem Rev , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 157
    • 17944361929 scopus 로고    scopus 로고
    • Functional cloning of an endo-arabinanase from Aspergillus aculeatus and its heterologous expression in A. oryzae and tobacco
    • Skjøt M., Kauppinen S., Kofod L., Fuglsang C., Pauly M., Dalbøge H., et al. Functional cloning of an endo-arabinanase from Aspergillus aculeatus and its heterologous expression in A. oryzae and tobacco. Mol Genet Genomics 2001, 265:913-921.
    • (2001) Mol Genet Genomics , vol.265 , pp. 913-921
    • Skjøt, M.1    Kauppinen, S.2    Kofod, L.3    Fuglsang, C.4    Pauly, M.5    Dalbøge, H.6
  • 158
    • 33947654156 scopus 로고    scopus 로고
    • Expression in Escherichia coli and characterization of β-xylosidases GH39 and GH-43 from Bacillus halodurans C-125
    • Smaali I., Rémond C., O'Donohue M. Expression in Escherichia coli and characterization of β-xylosidases GH39 and GH-43 from Bacillus halodurans C-125. Appl Microbiol Biotechnol 2006, 73:582-590.
    • (2006) Appl Microbiol Biotechnol , vol.73 , pp. 582-590
    • Smaali, I.1    Rémond, C.2    O'Donohue, M.3
  • 159
    • 33751542736 scopus 로고    scopus 로고
    • A novel GH43 α-l-arabinofuranosidase from Humicola insolens: mode of action and synergy with GH51 α-l-arabinofuranosidases on wheat arabinoxylan
    • Sørensen H.R., Jørgensen C.T., Hansen C.H., Jørgensen C.I., Pedersen S., Meyer A.S. A novel GH43 α-l-arabinofuranosidase from Humicola insolens: mode of action and synergy with GH51 α-l-arabinofuranosidases on wheat arabinoxylan. Appl Microbiol Biotechnol 2006, 73:850-861.
    • (2006) Appl Microbiol Biotechnol , vol.73 , pp. 850-861
    • Sørensen, H.R.1    Jørgensen, C.T.2    Hansen, C.H.3    Jørgensen, C.I.4    Pedersen, S.5    Meyer, A.S.6
  • 160
    • 33847168573 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of wheat arabinoxylan by a recombinant "minimal" enzyme cocktail containing β-xylosidase and novel endo-1,4-β-xylanase and α-l-arabinofuranosidase activities
    • Sørensen H.R., Pedersen S., Jørgensen C.T., Meyer A.S. Enzymatic hydrolysis of wheat arabinoxylan by a recombinant "minimal" enzyme cocktail containing β-xylosidase and novel endo-1,4-β-xylanase and α-l-arabinofuranosidase activities. Biotechnol Prog 2007, 23:100-107.
    • (2007) Biotechnol Prog , vol.23 , pp. 100-107
    • Sørensen, H.R.1    Pedersen, S.2    Jørgensen, C.T.3    Meyer, A.S.4
  • 161
    • 84860389042 scopus 로고    scopus 로고
    • Structure of a novel thermostable GH51 α-l-arabinofuranosidase from Thermotoga petrophila RKU-1
    • Souza T.A., Santos C.R., Souza A.R., Oldiges D.P., Ruller R., Prade R.A., et al. Structure of a novel thermostable GH51 α-l-arabinofuranosidase from Thermotoga petrophila RKU-1. Protein Sci 2011, 20:1632-1637.
    • (2011) Protein Sci , vol.20 , pp. 1632-1637
    • Souza, T.A.1    Santos, C.R.2    Souza, A.R.3    Oldiges, D.P.4    Ruller, R.5    Prade, R.A.6
  • 162
    • 77956268504 scopus 로고    scopus 로고
    • Substrate cleavage pattern, biophysical characterization and low-resolution structure of a novel hyperthermostable arabinanase from Thermotoga petrophila
    • Squina F.M., Santos C.R., Ribeiro D.A., Cota J., de Oliveira R.R., Ruller R., et al. Substrate cleavage pattern, biophysical characterization and low-resolution structure of a novel hyperthermostable arabinanase from Thermotoga petrophila. Biochem Biophys Res Commun 2010, 399:505-511.
    • (2010) Biochem Biophys Res Commun , vol.399 , pp. 505-511
    • Squina, F.M.1    Santos, C.R.2    Ribeiro, D.A.3    Cota, J.4    de Oliveira, R.R.5    Ruller, R.6
  • 163
    • 34547125795 scopus 로고    scopus 로고
    • Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated β-lactam resistance
    • Stubbs K.A., Balcewich M., Mark B.L., Vocadlo D.J. Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated β-lactam resistance. J Biol Chem 2007, 282:21382-21391.
    • (2007) J Biol Chem , vol.282 , pp. 21382-21391
    • Stubbs, K.A.1    Balcewich, M.2    Mark, B.L.3    Vocadlo, D.J.4
  • 164
    • 0036210191 scopus 로고    scopus 로고
    • Biotechnology of microbial xylanases: enzymology, molecular biology and application
    • Subramaniyan S., Prema P. Biotechnology of microbial xylanases: enzymology, molecular biology and application. Crit Rev Biotechnol 2002, 22:33-64.
    • (2002) Crit Rev Biotechnol , vol.22 , pp. 33-64
    • Subramaniyan, S.1    Prema, P.2
  • 165
    • 0030642144 scopus 로고    scopus 로고
    • Xylanolytic enzymes from fungi and bacteria
    • Sunna A., Antranikian G. Xylanolytic enzymes from fungi and bacteria. Crit Rev Biotechnol 1997, 17:39-67.
    • (1997) Crit Rev Biotechnol , vol.17 , pp. 39-67
    • Sunna, A.1    Antranikian, G.2
  • 166
    • 0035290271 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a family 52 β-xylosidase gene (xysB) of a multiple-xylanase-producing bacterium, Aeromonas caviae ME-1
    • Suzuki T., Kitawaga E., Sakakibara F., Ibata K., USUI K., Kawai K. Cloning, expression, and characterization of a family 52 β-xylosidase gene (xysB) of a multiple-xylanase-producing bacterium, Aeromonas caviae ME-1. Biosci Biotechnol Biochem 2001, 65:487-494.
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 487-494
    • Suzuki, T.1    Kitawaga, E.2    Sakakibara, F.3    Ibata, K.4    USUI, K.5    Kawai, K.6
  • 167
    • 0036479367 scopus 로고    scopus 로고
    • Molecular cloning of the gene encoding thermostable endo-1,5-α-l-arabinase of Bacillus thermodenitrificans TS-3 and its expression in Bacillus subtilis
    • Takao M., Yamaguchi A., Yoshikawa K., Terashita T., Sakai T. Molecular cloning of the gene encoding thermostable endo-1,5-α-l-arabinase of Bacillus thermodenitrificans TS-3 and its expression in Bacillus subtilis. Biosci Biotechnol Biochem 2002, 66:430-433.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 430-433
    • Takao, M.1    Yamaguchi, A.2    Yoshikawa, K.3    Terashita, T.4    Sakai, T.5
  • 168
    • 78049251842 scopus 로고    scopus 로고
    • Degradation of carbohydrate moieties of arabinogalactan-proteins by glycoside hydrolases from Neurospora crassa
    • Takata R., Tokita K., Mori S., Shimoda R., Harada N., Ichinose H., et al. Degradation of carbohydrate moieties of arabinogalactan-proteins by glycoside hydrolases from Neurospora crassa. Carbohydr Res 2010, 345:2516-2522.
    • (2010) Carbohydr Res , vol.345 , pp. 2516-2522
    • Takata, R.1    Tokita, K.2    Mori, S.3    Shimoda, R.4    Harada, N.5    Ichinose, H.6
  • 169
    • 27244440358 scopus 로고    scopus 로고
    • Isolation, characterization, and cloning of α-l-arabinofuranosidase expressed during fruit ripening of Japanese pear
    • Tateishi A., Mori H., Watari J., Nagashima K., Yamaki S., Inoue H. Isolation, characterization, and cloning of α-l-arabinofuranosidase expressed during fruit ripening of Japanese pear. Plant Physiol 2005, 138:1653-1664.
    • (2005) Plant Physiol , vol.138 , pp. 1653-1664
    • Tateishi, A.1    Mori, H.2    Watari, J.3    Nagashima, K.4    Yamaki, S.5    Inoue, H.6
  • 170
    • 33645559423 scopus 로고    scopus 로고
    • Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum
    • Taylor E.J., Smith N.L., Turkenburg J.P., D'souza S., Gilbert H.J., Davies G.J. Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum. Biochem J 2006, 395:31-37.
    • (2006) Biochem J , vol.395 , pp. 31-37
    • Taylor, E.J.1    Smith, N.L.2    Turkenburg, J.P.3    D'souza, S.4    Gilbert, H.J.5    Davies, G.J.6
  • 171
    • 67650828376 scopus 로고    scopus 로고
    • Beneficial biofuels-the food, energy, and environment trilemma
    • Tilman D., Socolow R., Foley J.A., Hill J., Larson E., Lynd L., et al. Beneficial biofuels-the food, energy, and environment trilemma. Science 2009, 325:270-271.
    • (2009) Science , vol.325 , pp. 270-271
    • Tilman, D.1    Socolow, R.2    Foley, J.A.3    Hill, J.4    Larson, E.5    Lynd, L.6
  • 172
    • 0036479363 scopus 로고    scopus 로고
    • Cloning and expression of an α-l-arabinofuranosidase gene (stxIV) from Streptomyces thermoviolaceus OPC-520, and characterization of the enzyme
    • Tsujibo H., Takada C., Wakamatsu Y., Kosaka M., Tsuji A., Miyamoto K., et al. Cloning and expression of an α-l-arabinofuranosidase gene (stxIV) from Streptomyces thermoviolaceus OPC-520, and characterization of the enzyme. Biosci Biotechnol Biochem 2002, 66:434-438.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 434-438
    • Tsujibo, H.1    Takada, C.2    Wakamatsu, Y.3    Kosaka, M.4    Tsuji, A.5    Miyamoto, K.6
  • 173
    • 37849012558 scopus 로고    scopus 로고
    • Cloning of a novel gene encoding β-1,3-xylosidase from a marine bacterium, Vibrio sp. strain XY-214, and characterization of the gene product
    • Umemoto Y., Onishi R., Araki T. Cloning of a novel gene encoding β-1,3-xylosidase from a marine bacterium, Vibrio sp. strain XY-214, and characterization of the gene product. Appl Environ Microbiol 2008, 74:305-308.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 305-308
    • Umemoto, Y.1    Onishi, R.2    Araki, T.3
  • 176
    • 0037470085 scopus 로고    scopus 로고
    • The structure of a cold-adapted family 8 xylanase at 1.3 angstrom resolution-structural adaptations to cold and investigation of the active site
    • Van Petegem F., Collins T., Meuwis M.A., Gerday C., Feller G., Van Beeumen J. The structure of a cold-adapted family 8 xylanase at 1.3 angstrom resolution-structural adaptations to cold and investigation of the active site. J Biol Chem 2003, 278:7531-7539.
    • (2003) J Biol Chem , vol.278 , pp. 7531-7539
    • Van Petegem, F.1    Collins, T.2    Meuwis, M.A.3    Gerday, C.4    Feller, G.5    Van Beeumen, J.6
  • 177
    • 59849117690 scopus 로고    scopus 로고
    • Structural analysis of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase in complex with xylotetraose reveals a different binding mechanism compared with other members of the same family
    • Vandermarliere E., Bourgois T.M., Winn M.D., Van Campenhout S., Volckaert G., Delcour J.A., et al. Structural analysis of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase in complex with xylotetraose reveals a different binding mechanism compared with other members of the same family. Biochem J 2009, 418:39-47.
    • (2009) Biochem J , vol.418 , pp. 39-47
    • Vandermarliere, E.1    Bourgois, T.M.2    Winn, M.D.3    Van Campenhout, S.4    Volckaert, G.5    Delcour, J.A.6
  • 178
    • 0033081517 scopus 로고    scopus 로고
    • Three-dimensional structure of a barley β-d-glucan exohydrolase, a family 3 glycosyl hydrolase
    • Varghese J.N., Hrmova M., Fincher G.B. Three-dimensional structure of a barley β-d-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 1999, 7:179-190.
    • (1999) Structure , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3
  • 179
    • 0025987758 scopus 로고
    • Induction, purification and characterisation of arabinases produced by Aspergillus niger
    • Veen P., Flipphi M.J.A., Voragen A.G.J., Visser J. Induction, purification and characterisation of arabinases produced by Aspergillus niger. Arch Microbiol 1991, 157:23-28.
    • (1991) Arch Microbiol , vol.157 , pp. 23-28
    • Veen, P.1    Flipphi, M.J.A.2    Voragen, A.G.J.3    Visser, J.4
  • 180
    • 0030898058 scopus 로고    scopus 로고
    • New -l-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme
    • Vincent P., Shareck F., Dupont C., Morosoli R., Kluepfel D. New -l-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme. Biochem J 1997, 322:845-852.
    • (1997) Biochem J , vol.322 , pp. 845-852
    • Vincent, P.1    Shareck, F.2    Dupont, C.3    Morosoli, R.4    Kluepfel, D.5
  • 181
    • 0032532593 scopus 로고    scopus 로고
    • Identification of Glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum β-xylosidase using electrospray MS
    • Vocadlo D.J., MacKenzie L.F., He S., Zeikus G.J., Withers S.G. Identification of Glu-277 as the catalytic nucleophile of Thermoanaerobacterium saccharolyticum β-xylosidase using electrospray MS. Biochem J 1998, 335:449-455.
    • (1998) Biochem J , vol.335 , pp. 449-455
    • Vocadlo, D.J.1    MacKenzie, L.F.2    He, S.3    Zeikus, G.J.4    Withers, S.G.5
  • 182
    • 0037031264 scopus 로고    scopus 로고
    • A case for reverse protonation: identification of Glu160 as an acid/base catalyst in Thermoanaerobacterium saccharolyticum β-xylosidase and detailed kinetic analysis of a site-directed mutant
    • Vocadlo D.J., Wicki J., Rupitz K., Withers S.G. A case for reverse protonation: identification of Glu160 as an acid/base catalyst in Thermoanaerobacterium saccharolyticum β-xylosidase and detailed kinetic analysis of a site-directed mutant. Biochemistry 2002, 41:9736-9746.
    • (2002) Biochemistry , vol.41 , pp. 9736-9746
    • Vocadlo, D.J.1    Wicki, J.2    Rupitz, K.3    Withers, S.G.4
  • 183
    • 0028899664 scopus 로고
    • Cloning and characterization of the Bgxa gene from Erwinia chrysanthemi D1 which encodes A β-glucosidase/xylosidase enzyme
    • Vroemen S., Heldens J., Boyd C., Henrissat B., Keen N.T. Cloning and characterization of the Bgxa gene from Erwinia chrysanthemi D1 which encodes A β-glucosidase/xylosidase enzyme. Mol Gen Genet 1995, 246:465-477.
    • (1995) Mol Gen Genet , vol.246 , pp. 465-477
    • Vroemen, S.1    Heldens, J.2    Boyd, C.3    Henrissat, B.4    Keen, N.T.5
  • 185
    • 58149172062 scopus 로고    scopus 로고
    • Biochemical characterization of a novel dual-function arabinofuranosidase/xylosidase isolated from a compost starter mixture
    • Wagschal K., Heng C., Lee C.C., Wong D.W.S. Biochemical characterization of a novel dual-function arabinofuranosidase/xylosidase isolated from a compost starter mixture. Appl Microbiol Biotechnol 2009, 81:855-863.
    • (2009) Appl Microbiol Biotechnol , vol.81 , pp. 855-863
    • Wagschal, K.1    Heng, C.2    Lee, C.C.3    Wong, D.W.S.4
  • 186
    • 49349105229 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a glycoside hydrolase family 39 xylosidase from Bacillus halodurans C-125
    • Wagschal K., Franqui-Espiet D., Lee C., Robertson G., Wong D. Cloning, expression and characterization of a glycoside hydrolase family 39 xylosidase from Bacillus halodurans C-125. Appl Biochem Biotechnol 2008, 146:69-78.
    • (2008) Appl Biochem Biotechnol , vol.146 , pp. 69-78
    • Wagschal, K.1    Franqui-Espiet, D.2    Lee, C.3    Robertson, G.4    Wong, D.5
  • 188
    • 66349118920 scopus 로고    scopus 로고
    • Purification and characterization of a glycoside hydrolase family 43 β-xylosidase from Geobacillus thermoleovorans IT-08
    • Wagschal K., Heng C., Lee C., Robertson G., Orts W., Wong D. Purification and characterization of a glycoside hydrolase family 43 β-xylosidase from Geobacillus thermoleovorans IT-08. Appl Biochem Biotechnol 2009, 155:1-10.
    • (2009) Appl Biochem Biotechnol , vol.155 , pp. 1-10
    • Wagschal, K.1    Heng, C.2    Lee, C.3    Robertson, G.4    Orts, W.5    Wong, D.6
  • 189
    • 84856233808 scopus 로고    scopus 로고
    • Catalytic properties of β-d-xylosidase XylBH43 from Bacillus halodurans C-125 and mutant XylBH43-W147G
    • Wagschal K., Jordan D.B., Braker J.D. Catalytic properties of β-d-xylosidase XylBH43 from Bacillus halodurans C-125 and mutant XylBH43-W147G. Process Biochem 2012, 47:366-372.
    • (2012) Process Biochem , vol.47 , pp. 366-372
    • Wagschal, K.1    Jordan, D.B.2    Braker, J.D.3
  • 190
    • 34548580678 scopus 로고    scopus 로고
    • Expression, purification and characterization of a bifunctional α-l-arabinofuranosidase/β-d-xylosidase from Trichoderma koningii G-39
    • Wan C.F., Chen C.T., Huang L.N., Li Y.K. Expression, purification and characterization of a bifunctional α-l-arabinofuranosidase/β-d-xylosidase from Trichoderma koningii G-39. J Chin Chem Soc 2007, 54:109-116.
    • (2007) J Chin Chem Soc , vol.54 , pp. 109-116
    • Wan, C.F.1    Chen, C.T.2    Huang, L.N.3    Li, Y.K.4
  • 191
    • 33846532317 scopus 로고    scopus 로고
    • Mutagenesis and mechanistic study of a glycoside hydrolase family 54 α-l-arabinofuranosidase from Trichoderma koningii
    • Wan C.F., Chen W.H., Chen C.T., Chang M.D.-T., Lo L.C., Li Y.K. Mutagenesis and mechanistic study of a glycoside hydrolase family 54 α-l-arabinofuranosidase from Trichoderma koningii. Biochem J 2007, 401:551-558.
    • (2007) Biochem J , vol.401 , pp. 551-558
    • Wan, C.F.1    Chen, W.H.2    Chen, C.T.3    Chang, M.D.-T.4    Lo, L.C.5    Li, Y.K.6
  • 192
    • 0028191018 scopus 로고
    • Changing enzymic reaction mechanisms by mutagenesis: conversion of a retaining glucosidase to an inverting enzyme
    • Wang Q., Graham R.W., Trimbur D., Warren R.A.J., Withers S.G. Changing enzymic reaction mechanisms by mutagenesis: conversion of a retaining glucosidase to an inverting enzyme. J Am Chem Soc 1994, 116:11594-11595.
    • (1994) J Am Chem Soc , vol.116 , pp. 11594-11595
    • Wang, Q.1    Graham, R.W.2    Trimbur, D.3    Warren, R.A.J.4    Withers, S.G.5
  • 193
    • 0034863521 scopus 로고    scopus 로고
    • Identification of a broad-specificity xylosidase/arabinosidase important for xylooligosaccharide fermentation by the ruminal anaerobe Selenomonas ruminantium GA192
    • Whitehead T.R., Cotta M.A. Identification of a broad-specificity xylosidase/arabinosidase important for xylooligosaccharide fermentation by the ruminal anaerobe Selenomonas ruminantium GA192. Curr Microbiol 2001, 43:293-298.
    • (2001) Curr Microbiol , vol.43 , pp. 293-298
    • Whitehead, T.R.1    Cotta, M.A.2
  • 194
    • 0025273798 scopus 로고
    • The genes for three xylan-degrading activities from Bacteroides ovatus are clustered in a 3.8-kilobase region
    • Whitehead T.R., Hespell R.B. The genes for three xylan-degrading activities from Bacteroides ovatus are clustered in a 3.8-kilobase region. J Bacteriol 1990, 172:2408-2412.
    • (1990) J Bacteriol , vol.172 , pp. 2408-2412
    • Whitehead, T.R.1    Hespell, R.B.2
  • 195
    • 46149117011 scopus 로고    scopus 로고
    • Cloning and characterization of a novel exo-α-1,5-arabinanase gene and the enzyme
    • Wong D., Chan V., Batt S. Cloning and characterization of a novel exo-α-1,5-arabinanase gene and the enzyme. Appl Microbiol Biotechnol 2008, 79:941-949.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 941-949
    • Wong, D.1    Chan, V.2    Batt, S.3
  • 196
    • 73449091880 scopus 로고    scopus 로고
    • Functional cloning and expression of a novel endo-α-1,5-l-arabinanase from a metagenomic library
    • Wong D.W.S., Chan V.J., McCormack A.A. Functional cloning and expression of a novel endo-α-1,5-l-arabinanase from a metagenomic library. Protein Pept Lett 2009, 16:1435-1441.
    • (2009) Protein Pept Lett , vol.16 , pp. 1435-1441
    • Wong, D.W.S.1    Chan, V.J.2    McCormack, A.A.3
  • 197
    • 0024087074 scopus 로고
    • Multiplicity of β-1,4-xylanase in microorganisms: functions and applications
    • Wong K.K., Tan L.U., Saddler J.N. Multiplicity of β-1,4-xylanase in microorganisms: functions and applications. Microbiol Mol Biol Rev 1988, 52:305-317.
    • (1988) Microbiol Mol Biol Rev , vol.52 , pp. 305-317
    • Wong, K.K.1    Tan, L.U.2    Saddler, J.N.3
  • 198
    • 34848836082 scopus 로고    scopus 로고
    • Molecular cloning of a bifunctional β-xylosidase/α-l-arabinosidase from alfalfa roots: heterologous expression in Medicago truncatula and substrate specificity of the purified enzyme
    • Xiong J.S., Balland-Vanney M., Xie Z.P., Schultze M., Kondorosi A., Kondorosi E., et al. Molecular cloning of a bifunctional β-xylosidase/α-l-arabinosidase from alfalfa roots: heterologous expression in Medicago truncatula and substrate specificity of the purified enzyme. J Exp Bot 2007, 58:2799-2810.
    • (2007) J Exp Bot , vol.58 , pp. 2799-2810
    • Xiong, J.S.1    Balland-Vanney, M.2    Xie, Z.P.3    Schultze, M.4    Kondorosi, A.5    Kondorosi, E.6
  • 199
    • 0026337930 scopus 로고
    • Sequence and properties of b-xylosidase from Bacillus pumilus IPO. Contradiction of the previous nucleotide sequence
    • Xu W.Z., Shima Y., Negoro S., Urabe I. Sequence and properties of b-xylosidase from Bacillus pumilus IPO. Contradiction of the previous nucleotide sequence. Eur J Biochem 1991, 202:1197-1203.
    • (1991) Eur J Biochem , vol.202 , pp. 1197-1203
    • Xu, W.Z.1    Shima, Y.2    Negoro, S.3    Urabe, I.4
  • 200
    • 10744221210 scopus 로고    scopus 로고
    • Crystal structure of β-d-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase
    • Yang J.K., Yoon H.J., Ahn H.J., Il Lee B., Pedelacq J.D., Liong E.C., et al. Crystal structure of β-d-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase. J Mol Biol 2004, 335:155-165.
    • (2004) J Mol Biol , vol.335 , pp. 155-165
    • Yang, J.K.1    Yoon, H.J.2    Ahn, H.J.3    Il Lee, B.4    Pedelacq, J.D.5    Liong, E.C.6
  • 201
    • 77956642710 scopus 로고    scopus 로고
    • Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus
    • Yoshida E., Hidaka M., Fushinobu S., Koyanagi T., Minami H., Tamaki H., et al. Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus. Biochem J 2010, 431:39-49.
    • (2010) Biochem J , vol.431 , pp. 39-49
    • Yoshida, E.1    Hidaka, M.2    Fushinobu, S.3    Koyanagi, T.4    Minami, H.5    Tamaki, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.