메뉴 건너뛰기




Volumn 10, Issue 1, 2017, Pages

When substrate inhibits and inhibitor activates: Implications of β-glucosidases

Author keywords

Glucose activation; Glucose inhibition; Glucose tolerance; Nonproductive binding; Transglycosylation; glucosidase

Indexed keywords

BINS; BIOTECHNOLOGY; CATALYSIS; ENZYMES; GLUCOSE; GLYCOSYLATION; HYDROLYSIS; SUBSTRATES;

EID: 85010980518     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/s13068-016-0690-z     Document Type: Article
Times cited : (47)

References (76)
  • 1
    • 84870952001 scopus 로고    scopus 로고
    • Role and significance of beta-glucosidases in the hydrolysis of cellulose for bioethanol production
    • 1:CAS:528:DC%2BC38XhsFWhsb%2FJ
    • Singhania RR, Patel AK, Sukumaran RK, Larroche C, Pandey A. Role and significance of beta-glucosidases in the hydrolysis of cellulose for bioethanol production. Bioresour Technol. 2013;127:500-7.
    • (2013) Bioresour Technol , vol.127 , pp. 500-507
    • Singhania, R.R.1    Patel, A.K.2    Sukumaran, R.K.3    Larroche, C.4    Pandey, A.5
  • 2
    • 67649436135 scopus 로고    scopus 로고
    • Yield-determining factors in high-solids enzymatic hydrolysis of lignocellulose
    • Kristensen JB, Felby C, Jørgensen H. Yield-determining factors in high-solids enzymatic hydrolysis of lignocellulose. Biotechnol Biofuels. 2009;2:11.
    • (2009) Biotechnol Biofuels , vol.2 , pp. 11
    • Kristensen, J.B.1    Felby, C.2    Jørgensen, H.3
  • 3
    • 85027931281 scopus 로고    scopus 로고
    • The role of product inhibition as a yield-determining factor in enzymatic high-solid hydrolysis of pretreated corn stover
    • 1:CAS:528:DC%2BC2cXhtFOqur%2FM
    • Olsen SN, Borch K, Cruys-Bagger N, Westh P. The role of product inhibition as a yield-determining factor in enzymatic high-solid hydrolysis of pretreated corn stover. Appl Biochem Biotechnol. 2014;174:146-55.
    • (2014) Appl Biochem Biotechnol , vol.174 , pp. 146-155
    • Olsen, S.N.1    Borch, K.2    Cruys-Bagger, N.3    Westh, P.4
  • 4
    • 84881116511 scopus 로고    scopus 로고
    • Product inhibition of cellulases studied with 14C-labeled cellulose substrates
    • 1:CAS:528:DC%2BC3sXhtlWgtLrO
    • Teugjas H, Väljamäe P. Product inhibition of cellulases studied with 14C-labeled cellulose substrates. Biotechnol Biofuels. 2013;6:104.
    • (2013) Biotechnol Biofuels , vol.6 , pp. 104
    • Teugjas, H.1    Väljamäe, P.2
  • 6
    • 84880913078 scopus 로고    scopus 로고
    • Selecting β-glucosidases to support cellulases in cellulose saccharification
    • 1:CAS:528:DC%2BC3sXhtlWgtLrN
    • Teugjas H, Väljamäe P. Selecting β-glucosidases to support cellulases in cellulose saccharification. Biotechnol Biofuels. 2013;6:105.
    • (2013) Biotechnol Biofuels , vol.6 , pp. 105
    • Teugjas, H.1    Väljamäe, P.2
  • 8
    • 17744362070 scopus 로고    scopus 로고
    • Transglucosidic reactions of the Aspergillus Niger family 3 β-glucosidase: Qualitative and quantitative analyses and evidence that the transglucosidic rate is independent of pH
    • 1:CAS:528:DC%2BD2MXis1Gks78%3D
    • Seidle HF, Huber RE. Transglucosidic reactions of the Aspergillus niger family 3 β-glucosidase: qualitative and quantitative analyses and evidence that the transglucosidic rate is independent of pH. Arch Biochem Biophys. 2005;436:254-64.
    • (2005) Arch Biochem Biophys , vol.436 , pp. 254-264
    • Seidle, H.F.1    Huber, R.E.2
  • 11
    • 0026443120 scopus 로고
    • Cloning, characterization, nucleotide sequence of a gene encoding Microbispora BglB, a thermostable β-glucosidase expressed in Escherichia coli
    • 1:CAS:528:DyaK3sXksVagtbg%3D
    • Wright RM, Yablonsky MD, Shalita ZP, Goyal AK, Eveleigh DE. Cloning, characterization, nucleotide sequence of a gene encoding Microbispora BglB, a thermostable β-glucosidase expressed in Escherichia coli. Appl Environ Microbiol. 1992;58:3455-65.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3455-3465
    • Wright, R.M.1    Yablonsky, M.D.2    Shalita, Z.P.3    Goyal, A.K.4    Eveleigh, D.E.5
  • 12
    • 0029100735 scopus 로고
    • Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238)
    • Perez-Pons JA, Rebordosa X, Querol E. Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238). Biochim Biophys Acta. 1995;1251:145-53.
    • (1995) Biochim Biophys Acta , vol.1251 , pp. 145-153
    • Perez-Pons, J.A.1    Rebordosa, X.2    Querol, E.3
  • 13
    • 7644238142 scopus 로고    scopus 로고
    • β-glucosidase activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose
    • 1:CAS:528:DC%2BD2cXptFOksLk%3D
    • Zanoelo FF, Polizeli MLTM, Terenzi HF, Jorge JA. β-glucosidase activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose. FEMS Microbiol Lett. 2004;240:137-43.
    • (2004) FEMS Microbiol Lett , vol.240 , pp. 137-143
    • Zanoelo, F.F.1    Polizeli, M.L.T.M.2    Terenzi, H.F.3    Jorge, J.A.4
  • 14
    • 42049095517 scopus 로고    scopus 로고
    • Identification of glucose tolerant acid active β-glucosidases from thermophilic and thermotolerant fungi
    • 1:CAS:528:DC%2BD1cXksVaktb4%3D
    • Sonia KG, Chadha BS, Badhan AK, Saini HS, Bhat MK. Identification of glucose tolerant acid active β-glucosidases from thermophilic and thermotolerant fungi. World J Microbiol Biotechnol. 2008;24:599-604.
    • (2008) World J Microbiol Biotechnol , vol.24 , pp. 599-604
    • Sonia, K.G.1    Chadha, B.S.2    Badhan, A.K.3    Saini, H.S.4    Bhat, M.K.5
  • 15
    • 77949292657 scopus 로고    scopus 로고
    • Furriel RPM. Purification and biochemical characterization of a glucose-stimulated β-d-glucosidase produced by Humicola grisea var. Thermoidea grown on sugarcane bagasse
    • 1:CAS:528:DC%2BC3cXjtFWls7w%3D
    • Nascimento CV, Souza FHM, Masui DC, Leone FA, Peralta RM, Jorge JA. Furriel RPM. Purification and biochemical characterization of a glucose-stimulated β-d-glucosidase produced by Humicola grisea var. thermoidea grown on sugarcane bagasse. J Microbiol. 2010;48:53-62.
    • (2010) J Microbiol. , vol.48 , pp. 53-62
    • Nascimento, C.V.1    Souza, F.H.M.2    Masui, D.C.3    Leone, F.A.4    Peralta, R.M.5    Jorge, J.A.6
  • 16
    • 77957737285 scopus 로고    scopus 로고
    • Cloning and characterization of a β-glucosidase from marine microbial metagenome with excellent glucose tolerance
    • Zemin F, Fang W, Liu J, Hong Y, Peng H, Zhang X, Sun B, Xiao Y. Cloning and characterization of a β-glucosidase from marine microbial metagenome with excellent glucose tolerance. J Microbiol Biotechnol. 2010;20:1351-8.
    • (2010) J Microbiol Biotechnol , vol.20 , pp. 1351-1358
    • Zemin, F.1    Fang, W.2    Liu, J.3    Hong, Y.4    Peng, H.5    Zhang, X.6    Sun, B.7    Xiao, Y.8
  • 17
    • 79952575277 scopus 로고    scopus 로고
    • Heterologous expression and characterization of a glucose-stimulated β-glucosidase from the termite Neotermes koshunensis in Aspergillus oryzae
    • 1:CAS:528:DC%2BC3MXitlakt74%3D
    • Uchima CA, Tokuda G, Watanabe H, Kitamoto K, Arioka M. Heterologous expression and characterization of a glucose-stimulated β-glucosidase from the termite Neotermes koshunensis in Aspergillus oryzae. Appl Microbiol Biotechnol. 2011;89:1761-71.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 1761-1771
    • Uchima, C.A.1    Tokuda, G.2    Watanabe, H.3    Kitamoto, K.4    Arioka, M.5
  • 18
    • 84860852677 scopus 로고    scopus 로고
    • Thermoanaerobacterium thermosaccharolyticum β-glucosidase: A glucose-tolerant enzyme with high specific activity for cellobiose
    • 1:CAS:528:DC%2BC38XhtVyku7bL
    • Pei J, Pang Q, Zhao L, Fan S, Shi H. Thermoanaerobacterium thermosaccharolyticum β-glucosidase: a glucose-tolerant enzyme with high specific activity for cellobiose. Biotechnol Biofuels. 2012;5:31.
    • (2012) Biotechnol Biofuels , vol.5 , pp. 31
    • Pei, J.1    Pang, Q.2    Zhao, L.3    Fan, S.4    Shi, H.5
  • 19
    • 84880056854 scopus 로고    scopus 로고
    • Characterization of a novel β-glucosidase from a compost microbial metagenome with strong transglycosylation activity
    • 1:CAS:528:DC%2BC3sXpvVGmsrs%3D
    • Uchiyama T, Miyazaki K, Yaoi K. Characterization of a novel β-glucosidase from a compost microbial metagenome with strong transglycosylation activity. J Biol Chem. 2013;288:18325-34.
    • (2013) J Biol Chem , vol.288 , pp. 18325-18334
    • Uchiyama, T.1    Miyazaki, K.2    Yaoi, K.3
  • 20
    • 84881104601 scopus 로고    scopus 로고
    • Gene cloning and characterization of a novel salt-tolerant and glucose-enhanced β-glucosidase from marine Streptomycete
    • 1:CAS:528:DC%2BC3sXjslehtrw%3D
    • Mai Z, Yang J, Tian X, Li J, Zhang S. Gene cloning and characterization of a novel salt-tolerant and glucose-enhanced β-glucosidase from marine Streptomycete. Appl Biochem Biotechnol. 2013;169:1512-22.
    • (2013) Appl Biochem Biotechnol , vol.169 , pp. 1512-1522
    • Mai, Z.1    Yang, J.2    Tian, X.3    Li, J.4    Zhang, S.5
  • 21
    • 84879062717 scopus 로고    scopus 로고
    • Glucose and xylose stimulation of a β-glucosidase from the thermophilic fungus Humicola insolens: A kinetic and biophysical study
    • 1:CAS:528:DC%2BC3sXhtVGrsb3J
    • Souza FHM, Inocentes RF, Ward RJ, Jorge JA, Furriel RPM. Glucose and xylose stimulation of a β-glucosidase from the thermophilic fungus Humicola insolens: a kinetic and biophysical study. J Mol Catal B: Enz. 2013;94:119-28.
    • (2013) J Mol Catal B: Enz. , vol.94 , pp. 119-128
    • Souza, F.H.M.1    Inocentes, R.F.2    Ward, R.J.3    Jorge, J.A.4    Furriel, R.P.M.5
  • 23
    • 84931260664 scopus 로고    scopus 로고
    • Glucose-tolerant β-glucosidase retrieved from Kusaya gravy metagenome
    • Uchiyama T, Yaoi K, Miyazaki K. Glucose-tolerant β-glucosidase retrieved from Kusaya gravy metagenome. Front Microbiol. 2015;6:548.
    • (2015) Front Microbiol. , vol.6 , pp. 548
    • Uchiyama, T.1    Yaoi, K.2    Miyazaki, K.3
  • 24
    • 84956944870 scopus 로고    scopus 로고
    • Engineering a novel glucose-tolerant β-glucosidase as supplementation to enhance the hydrolysis of sugarcane bagasse at high glucose concentration
    • Cao L-C, Wang Z-J, Ren G-H, Kong W, Li L, Xie W, Liu Y-H. Engineering a novel glucose-tolerant β-glucosidase as supplementation to enhance the hydrolysis of sugarcane bagasse at high glucose concentration. Biotechnol Biofuels. 2015;8:202.
    • (2015) Biotechnol Biofuels , vol.8 , pp. 202
    • Cao, L.-C.1    Wang, Z.-J.2    Ren, G.-H.3    Kong, W.4    Li, L.5    Xie, W.6    Liu, Y.-H.7
  • 25
    • 84945456621 scopus 로고    scopus 로고
    • Overexpression and characterization of a glucose-tolerant β-glucosidase from T. Aotearoense with high specific activity for cellobiose
    • 1:CAS:528:DC%2BC2MXotVOisL8%3D
    • Yang F, Yang X, Li Z, Du C, Wang J, Li S. Overexpression and characterization of a glucose-tolerant β-glucosidase from T. aotearoense with high specific activity for cellobiose. Appl Microbiol Biotechnol. 2015;99:8903-15.
    • (2015) Appl Microbiol Biotechnol , vol.99 , pp. 8903-8915
    • Yang, F.1    Yang, X.2    Li, Z.3    Du, C.4    Wang, J.5    Li, S.6
  • 26
    • 84948441858 scopus 로고    scopus 로고
    • A mechanism of glucose tolerance and stimulation of GH1 β-glucosidase
    • 1:CAS:528:DC%2BC2MXhvFGjurvN
    • Yang Y, Zhang X, Yin Q, Fang W, Wang X, Zhang X, Xiao Y. A mechanism of glucose tolerance and stimulation of GH1 β-glucosidase. Sci Rep. 2015;5:17296.
    • (2015) Sci Rep. , vol.5 , pp. 17296
    • Yang, Y.1    Zhang, X.2    Yin, Q.3    Fang, W.4    Wang, X.5    Zhang, X.6    Xiao, Y.7
  • 27
    • 84925496790 scopus 로고    scopus 로고
    • Molecular cloning and expression of thermostable glucose-tolerant β-glucosidase of Penicillium funiculosum NCL1 in Pichia pastoris and its characterization
    • 1:CAS:528:DC%2BC2MXhs1artb0%3D
    • Ramani G, Meera B, Vanitha C, Rajendhran J, Gunasekaran P. Molecular cloning and expression of thermostable glucose-tolerant β-glucosidase of Penicillium funiculosum NCL1 in Pichia pastoris and its characterization. J Ind Microbiol Biotechnol. 2015;42:553-65.
    • (2015) J Ind Microbiol Biotechnol , vol.42 , pp. 553-565
    • Ramani, G.1    Meera, B.2    Vanitha, C.3    Rajendhran, J.4    Gunasekaran, P.5
  • 29
    • 84941651774 scopus 로고    scopus 로고
    • A Neurospora crassa β-glucosidase with potential for lignocellulose hydrolysis shows strong glucose tolerance and stimulation by glucose and xylose
    • 1:CAS:528:DC%2BC2MXhsFShs7%2FJ
    • Meleiro LP, Salgado JCS, Maldonado RF, Alponti JS, Zimbardi ALRL, Jorge JA, Ward RJ, Furriel RPM. A Neurospora crassa β-glucosidase with potential for lignocellulose hydrolysis shows strong glucose tolerance and stimulation by glucose and xylose. J Mol Catal B: Enz. 2015;122:131-40.
    • (2015) J Mol Catal B: Enz. , vol.122 , pp. 131-140
    • Meleiro, L.P.1    Salgado, J.C.S.2    Maldonado, R.F.3    Alponti, J.S.4    Zimbardi, A.L.R.L.5    Jorge, J.A.6    Ward, R.J.7    Furriel, R.P.M.8
  • 30
    • 84976512619 scopus 로고    scopus 로고
    • Crystal structure and identification of a key amino acid for glucose tolerance, substrate specificity, and transglycosylation activity of metagenomic β-glucosidase TdF2
    • 1:CAS:528:DC%2BC28XntlSru7g%3D
    • Matsuzawa T, Jo T, Uchiyama T, Manninen JA, Arakawa T, Miyazaki K, Fushinobu S, Yaoi K. Crystal structure and identification of a key amino acid for glucose tolerance, substrate specificity, and transglycosylation activity of metagenomic β-glucosidase TdF2. FEBS J. 2016;283:2340-53.
    • (2016) FEBS J , vol.283 , pp. 2340-2353
    • Matsuzawa, T.1    Jo, T.2    Uchiyama, T.3    Manninen, J.A.4    Arakawa, T.5    Miyazaki, K.6    Fushinobu, S.7    Yaoi, K.8
  • 31
    • 84983451652 scopus 로고    scopus 로고
    • Screening, identification, and characterization of a novel saccharide-stimulated β-glucosidase from a soil metagenomic library
    • 10.1007/s00253-016-7803-2
    • Matsuzawa T, Yaoi K. Screening, identification, and characterization of a novel saccharide-stimulated β-glucosidase from a soil metagenomic library. Appl Microbiol Biotechnol. 2016. doi: 10.1007/s00253-016-7803-2.
    • (2016) Appl Microbiol Biotechnol.
    • Matsuzawa, T.1    Yaoi, K.2
  • 32
    • 84963976814 scopus 로고    scopus 로고
    • Crystal structure and biochemical characterization of the recombinant ThBgl, a GH1 β-glucosidase overexpressed in Trichoderma harzianum under biomass degradation conditions
    • Santos CA, Zanphorlin LM, Crucello A, Tonoli CCC, Ruller R, Horta MAC, Murakami MT, de Souza AP. Crystal structure and biochemical characterization of the recombinant ThBgl, a GH1 β-glucosidase overexpressed in Trichoderma harzianum under biomass degradation conditions. Biotechnol Biofuels. 2016;9:71.
    • (2016) Biotechnol Biofuels , vol.9 , pp. 71
    • Santos, C.A.1    Zanphorlin, L.M.2    Crucello, A.3    Tonoli, C.C.C.4    Ruller, R.5    Horta, M.A.C.6    Murakami, M.T.7    De Souza, A.P.8
  • 35
    • 84969849732 scopus 로고    scopus 로고
    • β-Glucosidase from the hyperthermophilic archaeon Thermococcus sp is a salt-tolerant enzyme that is stabilized by its reaction product glucose
    • 1:CAS:528:DC%2BC28Xot1KitL8%3D
    • Sinha SK, Datta S. β-Glucosidase from the hyperthermophilic archaeon Thermococcus sp. is a salt-tolerant enzyme that is stabilized by its reaction product glucose. Appl Microbiol Biotechnol. 2016;100:8399-409.
    • (2016) Appl Microbiol Biotechnol , vol.100 , pp. 8399-8409
    • Sinha, S.K.1    Datta, S.2
  • 36
    • 84990858995 scopus 로고    scopus 로고
    • Expression of two novel β-glucosidases from Chaetomium atrobrunneum in Trichoderma reesei and characterization of the heterologous protein products
    • 1:CAS:528:DC%2BC28Xhs1eiu7nP
    • Colabardini AC, Valkonen M, Huuskonen A, Siika-aho M, Koivula A, Goldman GH, Saloheimo M. Expression of two novel β-glucosidases from Chaetomium atrobrunneum in Trichoderma reesei and characterization of the heterologous protein products. Mol Biotechnol. 2016;58:821-31.
    • (2016) Mol Biotechnol , vol.58 , pp. 821-831
    • Colabardini, A.C.1    Valkonen, M.2    Huuskonen, A.3    Siika-Aho, M.4    Koivula, A.5    Goldman, G.H.6    Saloheimo, M.7
  • 37
    • 80052261669 scopus 로고    scopus 로고
    • Purification and biochemical characterization of an atypical β-glucosidase from Stachybotrys microspora
    • 1:CAS:528:DC%2BC3MXhtV2ntb%2FE
    • Saibi W, Gargouri A. Purification and biochemical characterization of an atypical β-glucosidase from Stachybotrys microspora. J Mol Catal B: Enz. 2011;72:107-15.
    • (2011) J Mol Catal B: Enz. , vol.72 , pp. 107-115
    • Saibi, W.1    Gargouri, A.2
  • 38
    • 84958191042 scopus 로고    scopus 로고
    • Improvements in glucose sensitivity and stability of Trichoderma reesei β-glucosidase using site-directed mutagenesis
    • Guo B, Amano Y, Nozaki K. Improvements in glucose sensitivity and stability of Trichoderma reesei β-glucosidase using site-directed mutagenesis. PLoS ONE. 2016;11(1):e0147301.
    • (2016) PLoS ONE , vol.11 , Issue.1 , pp. e0147301
    • Guo, B.1    Amano, Y.2    Nozaki, K.3
  • 43
    • 0034850147 scopus 로고    scopus 로고
    • A structural basis of processivity
    • 1:CAS:528:DC%2BD3MXmsFSgtLc%3D
    • Breyer AW, Matthews WB. A structural basis of processivity. Protein Sci. 2001;10:1699-711.
    • (2001) Protein Sci , vol.10 , pp. 1699-1711
    • Breyer, A.W.1    Matthews, W.B.2
  • 45
    • 84892174650 scopus 로고    scopus 로고
    • The mechanism of cellulose hydrolysis by a two-step, retaining cellobiohydrolase elucidated by structural and transition path sampling studies
    • 1:CAS:528:DC%2BC3sXhvFWltbjM
    • Knott BC, Momeni MH, Crowley MF, Mackenzie LF, Götz AW, Sandgren M, Withers SG, Ståhlberg J, Beckham GT. The mechanism of cellulose hydrolysis by a two-step, retaining cellobiohydrolase elucidated by structural and transition path sampling studies. J Am Chem Soc. 2014;136:321-9.
    • (2014) J Am Chem Soc , vol.136 , pp. 321-329
    • Knott, B.C.1    Momeni, M.H.2    Crowley, M.F.3    Mackenzie, L.F.4    Götz, A.W.5    Sandgren, M.6    Withers, S.G.7    Ståhlberg, J.8    Beckham, G.T.9
  • 46
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • 1:CAS:528:DyaK2sXotFOnsQ%3D%3D
    • Davies GJ, Wilson KS, Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J. 1997;321:557-9.
    • (1997) Biochem J , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 47
    • 0024402815 scopus 로고
    • Fungal cellulase systems: Comparison of the specificities of the cellobiohydrolases isolated from Penicillium pinophilum and Trichoderma reesei
    • 1:CAS:528:DyaL1MXlsV2gt7g%3D
    • Claeyssens M, van Tilbeurgh H, Tomme P, Wood TM, McRae SI. Fungal cellulase systems: comparison of the specificities of the cellobiohydrolases isolated from Penicillium pinophilum and Trichoderma reesei. Biochem J. 1989;261:819-25.
    • (1989) Biochem J , vol.261 , pp. 819-825
    • Claeyssens, M.1    Van Tilbeurgh, H.2    Tomme, P.3    Wood, T.M.4    McRae, S.I.5
  • 48
    • 84902689475 scopus 로고    scopus 로고
    • Carbohydrate-protein interactions that drive processive polysaccharide translocation in enzymes revealed from a computational study of cellobiohydrolase processivity
    • 1:CAS:528:DC%2BC2cXos1Wqu7o%3D
    • Knott BC, Crowley MF, Himmel ME, Ståhlberg J, Beckham GT. Carbohydrate-protein interactions that drive processive polysaccharide translocation in enzymes revealed from a computational study of cellobiohydrolase processivity. J Am Chem Soc. 2014;136:8810-9.
    • (2014) J Am Chem Soc , vol.136 , pp. 8810-8819
    • Knott, B.C.1    Crowley, M.F.2    Himmel, M.E.3    Ståhlberg, J.4    Beckham, G.T.5
  • 49
    • 33646270203 scopus 로고    scopus 로고
    • Molecular basis of substrate specificity in family 1 glycoside hydrolases
    • 1:CAS:528:DC%2BD28XjtlKqt7k%3D
    • Marana SR. Molecular basis of substrate specificity in family 1 glycoside hydrolases. IUBMB Life. 2006;58:63-73.
    • (2006) IUBMB Life , vol.58 , pp. 63-73
    • Marana, S.R.1
  • 50
    • 0023187895 scopus 로고
    • 3H]cello-oligosaccharides
    • 1:CAS:528:DyaL2sXmtFCis78%3D
    • 3H]cello-oligosaccharides. Eur J Biochem. 1987;165:343-51.
    • (1987) Eur J Biochem , vol.165 , pp. 343-351
    • Chirico, W.J.1    Brown, R.D.2
  • 51
    • 0032079561 scopus 로고    scopus 로고
    • Substrate binding and catalytic mechanism of a barley β-d-glucosidase/(1,4)-β-d-glucan exohydrolase
    • 1:CAS:528:DyaK1cXjtFGkurk%3D
    • Hrmova M, MacGregor EA, Biely P, Stewart RJ, Fincher GB. Substrate binding and catalytic mechanism of a barley β-d-glucosidase/(1,4)-β-d-glucan exohydrolase. J Biol Chem. 1998;273:11134-43.
    • (1998) J Biol Chem , vol.273 , pp. 11134-11143
    • Hrmova, M.1    MacGregor, E.A.2    Biely, P.3    Stewart, R.J.4    Fincher, G.B.5
  • 52
    • 0033388102 scopus 로고    scopus 로고
    • Basic subsite theory assumptions may not be applicable to hydrolysis of cellooligosaccharides by almond β-glucosidase
    • 1:CAS:528:DC%2BD3cXhslygtw%3D%3D
    • Tanaka A, Nakagawa C, Kodaira K, Senoo K, Obata H. Basic subsite theory assumptions may not be applicable to hydrolysis of cellooligosaccharides by almond β-glucosidase. J Biosci Bioeng. 1999;88:664-6.
    • (1999) J Biosci Bioeng , vol.88 , pp. 664-666
    • Tanaka, A.1    Nakagawa, C.2    Kodaira, K.3    Senoo, K.4    Obata, H.5
  • 54
    • 1842866212 scopus 로고    scopus 로고
    • β-Glucosidase, exo-β-glucanase and pyridoxine transglucosylase activities of rice BGlu1
    • 1:CAS:528:DC%2BD2cXisVyrsrY%3D
    • Opassiri R, Hua Y, Wara-Aswapati O, Akiyama T, Svasti J, Esen A, Cairns JRK. β-Glucosidase, exo-β-glucanase and pyridoxine transglucosylase activities of rice BGlu1. Biochem J. 2004;379:125-31.
    • (2004) Biochem J , vol.379 , pp. 125-131
    • Opassiri, R.1    Hua, Y.2    Wara-Aswapati, O.3    Akiyama, T.4    Svasti, J.5    Esen, A.6    Cairns, J.R.K.7
  • 55
    • 84928949306 scopus 로고    scopus 로고
    • Effects of active site cleft residues on oligosaccharide binding, hydrolysis, and glycosynthase activities of rice BGlu1 and its mutants
    • 1:CAS:528:DC%2BC2cXitVamtbfK
    • Pengthaisong S, Cairns JRK. Effects of active site cleft residues on oligosaccharide binding, hydrolysis, and glycosynthase activities of rice BGlu1 and its mutants. Prot Sci. 2014;23:1738-52.
    • (2014) Prot Sci. , vol.23 , pp. 1738-1752
    • Pengthaisong, S.1    Cairns, J.R.K.2
  • 56
    • 84921898800 scopus 로고    scopus 로고
    • Characterization of Aspergillus aculeatus β-glucosidase 1 accelerating cellulose hydrolysis with Trichoderma cellulase system
    • Baba Y, Sumitani J, Tani S, Kawaguchi T. Characterization of Aspergillus aculeatus β-glucosidase 1 accelerating cellulose hydrolysis with Trichoderma cellulase system. AMB Express. 2015;5:3.
    • (2015) AMB Express. , vol.5 , pp. 3
    • Baba, Y.1    Sumitani, J.2    Tani, S.3    Kawaguchi, T.4
  • 57
    • 0014943898 scopus 로고
    • Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exo-enzyme
    • 1:CAS:528:DyaE3cXkvVCit70%3D
    • Hiromi K. Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exo-enzyme. Biochem Biophys Res Commun. 1970;40:1-6.
    • (1970) Biochem Biophys Res Commun. , vol.40 , pp. 1-6
    • Hiromi, K.1
  • 58
    • 0015240182 scopus 로고
    • Subsite mapping of enzymes. Correlation of product patterns with Michaelis parameters and substrate-induced strain
    • 1:CAS:528:DyaE3MXltVGnsr0%3D
    • Thoma JA, Rao GVK, Brothers C, Spradlin J, Li LH. Subsite mapping of enzymes. Correlation of product patterns with Michaelis parameters and substrate-induced strain. J Biol Chem. 1971;246:5621-35.
    • (1971) J Biol Chem , vol.246 , pp. 5621-5635
    • Thoma, J.A.1    Rao, G.V.K.2    Brothers, C.3    Spradlin, J.4    Li, L.H.5
  • 59
    • 0015921531 scopus 로고
    • Subsite affinities of glucoamylase: Examination of the validity of the subsite theory
    • 1:CAS:528:DyaE3sXktl2ltLs%3D
    • Hiromi K, Nitta Y, Numata C, Ono S. Subsite affinities of glucoamylase: examination of the validity of the subsite theory. Biochim Biophys Acta. 1973;302:362-75.
    • (1973) Biochim Biophys Acta , vol.302 , pp. 362-375
    • Hiromi, K.1    Nitta, Y.2    Numata, C.3    Ono, S.4
  • 60
    • 84929941359 scopus 로고    scopus 로고
    • Glycosynthesis in a waterworld: New insight into the molecular basis of transglycosylation in retaining glycoside hydrolases
    • 1:CAS:528:DC%2BC2MXkvVOrsr0%3D
    • Bissaro B, Monsan P, Faure R, O'Donohue MJ. Glycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases. Biochem J. 2015;467:17-35.
    • (2015) Biochem J , vol.467 , pp. 17-35
    • Bissaro, B.1    Monsan, P.2    Faure, R.3    O'Donohue, M.J.4
  • 61
    • 0032503519 scopus 로고    scopus 로고
    • Glycosynthases: Mutant glycosidases for oligosaccharide synthesis
    • 1:CAS:528:DyaK1cXjtlWks7s%3D
    • Mackenzie LF, Wang Q, Warren RAJ, Withers SG. Glycosynthases: mutant glycosidases for oligosaccharide synthesis. J Am Chem Soc. 1998;120:5583-4.
    • (1998) J Am Chem Soc , vol.120 , pp. 5583-5584
    • Mackenzie, L.F.1    Wang, Q.2    Warren, R.A.J.3    Withers, S.G.4
  • 62
    • 69049085645 scopus 로고    scopus 로고
    • Generating rate equations for complex enzyme systems by a computer-assisted systematic method
    • Qi F, Dash RK, Han Y, Beard DA. Generating rate equations for complex enzyme systems by a computer-assisted systematic method. BMC Bioinform. 2009;10:238.
    • (2009) BMC Bioinform. , vol.10 , pp. 238
    • Qi, F.1    Dash, R.K.2    Han, Y.3    Beard, D.A.4
  • 64
    • 81255135961 scopus 로고    scopus 로고
    • The 184th residue of β-glucosidase Bgl1B plays an important role in glucose tolerance
    • 1:CAS:528:DC%2BC38XhsFyjtbY%3D
    • Liu J, Zhang X, Fang Z, Fang W, Peng H, Xiao Y. The 184th residue of β-glucosidase Bgl1B plays an important role in glucose tolerance. J Biosci Bioeng. 2011;112:447-50.
    • (2011) J Biosci Bioeng , vol.112 , pp. 447-450
    • Liu, J.1    Zhang, X.2    Fang, Z.3    Fang, W.4    Peng, H.5    Xiao, Y.6
  • 66
    • 34547597634 scopus 로고    scopus 로고
    • Crystal structures of Paenibacillus polymyxa β-glucosidase B complexes reveal the molecular basis of substrate specificity and give a new insights into the catalytic machinery of family 1 glycosidases
    • 1:CAS:528:DC%2BD2sXovFeqsL8%3D
    • Isorna P, Polaina J, Latorre-Garcia L, Canada FJ, Gonzalez B, Sanz-Aparicio J. Crystal structures of Paenibacillus polymyxa β-glucosidase B complexes reveal the molecular basis of substrate specificity and give a new insights into the catalytic machinery of family 1 glycosidases. J Mol Biol. 2007;371:1204-18.
    • (2007) J Mol Biol , vol.371 , pp. 1204-1218
    • Isorna, P.1    Polaina, J.2    Latorre-Garcia, L.3    Canada, F.J.4    Gonzalez, B.5    Sanz-Aparicio, J.6
  • 68
    • 78649905870 scopus 로고    scopus 로고
    • Structural and functional analysis of three β-glucosidases from bacterium Clostridium cellulovorans, Trichoderma reesei and termite Neotermes koshunensis
    • 1:CAS:528:DC%2BC3cXhsFCqurzM
    • Jeng W-Y, Wang N-C, Lin M-H, Lin C-T, Liaw Y-C, Chang W-J, Liu C-I, Liang P-H, Wang AH-J. Structural and functional analysis of three β-glucosidases from bacterium Clostridium cellulovorans, Trichoderma reesei and termite Neotermes koshunensis. J Struct Biol. 2011;173:46-56.
    • (2011) J Struct Biol , vol.173 , pp. 46-56
    • Jeng, W.-Y.1    Wang, N.-C.2    Lin, M.-H.3    Lin, C.-T.4    Liaw, Y.-C.5    Chang, W.-J.6    Liu, C.-I.7    Liang, P.-H.8    Wang, A.H.-J.9
  • 69
    • 84858075955 scopus 로고    scopus 로고
    • Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases
    • 1:CAS:528:DC%2BC38Xjt1Wnt7Y%3D
    • Sansenya S, Maneesan J, Cairns JRK. Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases. Carbohydr Res. 2012;351:130-3.
    • (2012) Carbohydr Res , vol.351 , pp. 130-133
    • Sansenya, S.1    Maneesan, J.2    Cairns, J.R.K.3
  • 71
    • 80054683331 scopus 로고    scopus 로고
    • Single mutations outside the active site affect the substrate specificity in a β-glucosidase
    • 1:CAS:528:DC%2BC3MXhsFSjtLbP
    • Mendonca LMF, Marana SM. Single mutations outside the active site affect the substrate specificity in a β-glucosidase. Biochim Biophys Acta. 2011;1814:1616-23.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 1616-1623
    • Mendonca, L.M.F.1    Marana, S.M.2
  • 72
    • 84868600048 scopus 로고    scopus 로고
    • Mutations in the substrate entrance region of β-glucosidase from Trichoderma reesei improve enzyme activity and thermostability
    • 1:CAS:528:DC%2BC38Xhs1WqsL3P
    • Lee H-L, Chang C-K, Jeng W-Y, Wang AH-J, Liang P-H. Mutations in the substrate entrance region of β-glucosidase from Trichoderma reesei improve enzyme activity and thermostability. Prot Eng Des Select. 2012;25:733-40.
    • (2012) Prot Eng des Select , vol.25 , pp. 733-740
    • Lee, H.-L.1    Chang, C.-K.2    Jeng, W.-Y.3    Wang, A.H.-J.4    Liang, P.-H.5
  • 73
    • 84969822593 scopus 로고    scopus 로고
    • A mutant β-glucosidase increases the rate of the cellulose enzymatic hydrolysis
    • Tamaki FK, Araujo EM, Rozenberg R, Marana SR. A mutant β-glucosidase increases the rate of the cellulose enzymatic hydrolysis. Biochem Biophys Rep. 2016;7:52-5.
    • (2016) Biochem Biophys Rep. , vol.7 , pp. 52-55
    • Tamaki, F.K.1    Araujo, E.M.2    Rozenberg, R.3    Marana, S.R.4
  • 74
    • 0028848613 scopus 로고
    • Identification of the acid/base catalyst in Agrobacterium faecalis β-glucosidase by kinetic analysis of mutants
    • 1:CAS:528:DyaK2MXoslGhs74%3D
    • Wang Q, Trimbur D, Graham R, Warren RAJ, Withers SG. Identification of the acid/base catalyst in Agrobacterium faecalis β-glucosidase by kinetic analysis of mutants. Biochemistry. 1995;34:14554-62.
    • (1995) Biochemistry , vol.34 , pp. 14554-14562
    • Wang, Q.1    Trimbur, D.2    Graham, R.3    Warren, R.A.J.4    Withers, S.G.5
  • 75
    • 0032568560 scopus 로고    scopus 로고
    • Pre-steady state kinetic analysis of an enzymatic reaction monitored by time-resolved electrospray ionization mass spectrometry
    • 1:CAS:528:DyaK1cXis12rsro%3D
    • Zechel DL, Konermann L, Withers SG, Douglas DJ. Pre-steady state kinetic analysis of an enzymatic reaction monitored by time-resolved electrospray ionization mass spectrometry. Biochemistry. 1998;37:7664-9.
    • (1998) Biochemistry , vol.37 , pp. 7664-7669
    • Zechel, D.L.1    Konermann, L.2    Withers, S.G.3    Douglas, D.J.4
  • 76
    • 0015010669 scopus 로고
    • Kinetic studies by stopped-flow method of hydrolysis of o-nitrophenyl α-maltoside catalyzed by saccharifying α-amylase from Bacillus subtilis
    • 1:CAS:528:DyaE3MXhtlGmurw%3D
    • Suetsugu N, Hiromi K, Ono S. Kinetic studies by stopped-flow method of hydrolysis of o-nitrophenyl α-maltoside catalyzed by saccharifying α-amylase from Bacillus subtilis. J Biochem. 1971;69:421-4.
    • (1971) J Biochem , vol.69 , pp. 421-424
    • Suetsugu, N.1    Hiromi, K.2    Ono, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.