메뉴 건너뛰기




Volumn 52, Issue 49, 2013, Pages 8938-8948

Transient kinetics and rate-limiting steps for the processive cellobiohydrolase Cel7A: Effects of substrate structure and carbohydrate binding domain

Author keywords

[No Author keywords available]

Indexed keywords

AMORPHOUS SUBSTRATE; CARBOHYDRATE BINDING; CELLOBIOHYDROLASE CEL7A; CRYSTALLINE CELLULOSE; DETERMINISTIC MODELING; HIGH TEMPORAL RESOLUTION; INTRINSIC REACTIVITY; SUBSTRATE STRUCTURE;

EID: 84890537940     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401210n     Document Type: Article
Times cited : (74)

References (48)
  • 1
    • 0035314098 scopus 로고    scopus 로고
    • Mechanisms of glycosyl transferases and hydrolases
    • Withers, S. G. (2001) Mechanisms of glycosyl transferases and hydrolases Carbohydr. Polym. 44, 325-337
    • (2001) Carbohydr. Polym. , vol.44 , pp. 325-337
    • Withers, S.G.1
  • 2
    • 0031149857 scopus 로고    scopus 로고
    • Crystalline cellulose degradation: New insight into the function of cellobiohydrolases
    • Teeri, T. T. (1997) Crystalline cellulose degradation: New insight into the function of cellobiohydrolases Trends Biotechnol. 15, 160-167
    • (1997) Trends Biotechnol. , vol.15 , pp. 160-167
    • Teeri, T.T.1
  • 4
    • 0003013146 scopus 로고
    • Transient-state kinetic analysis of enzymes reaction pathways
    • (Sigman, D. S. Ed.) 3 rd ed. Academic Press Inc. Salt Lake City, UT
    • Johnson, K. A. (1992) Transient-state kinetic analysis of enzymes reaction pathways in The Enzymes: Mechanisms of Catalysis (Sigman, D. S., Ed.) 3 rd ed., Academic Press Inc.: Salt Lake City, UT
    • (1992) The Enzymes: Mechanisms of Catalysis
    • Johnson, K.A.1
  • 8
    • 80054976342 scopus 로고    scopus 로고
    • Xylan oligosaccharides and cellobiohydrolase i (TrCeI7A) interaction and effect on activity
    • 10.1186/1754-6834-4-45
    • Baumann, M. J., Borch, K., and Westh, P. (2011) Xylan oligosaccharides and cellobiohydrolase I (TrCeI7A) interaction and effect on activity Biotechnol. Biofuels 4 10.1186/1754-6834-4-45
    • (2011) Biotechnol. Biofuels , vol.4
    • Baumann, M.J.1    Borch, K.2    Westh, P.3
  • 9
    • 77954459285 scopus 로고    scopus 로고
    • An enzymatic signal amplification system for calorimetric studies of cellobiohydrolases
    • Murphy, L., Baumann, M. J., Borch, K., Sweeney, M., and Westh, P. (2010) An enzymatic signal amplification system for calorimetric studies of cellobiohydrolases Anal. Biochem. 404, 140-148
    • (2010) Anal. Biochem. , vol.404 , pp. 140-148
    • Murphy, L.1    Baumann, M.J.2    Borch, K.3    Sweeney, M.4    Westh, P.5
  • 10
    • 33644633124 scopus 로고    scopus 로고
    • A transition from cellulose swelling to cellulose dissolution by o-phosphoric acid: Evidence from enzymatic hydrolysis and supramolecular structure
    • Zhang, Y. H. P., Cui, J. B., Lynd, L. R., and Kuang, L. R. (2006) A transition from cellulose swelling to cellulose dissolution by o-phosphoric acid: Evidence from enzymatic hydrolysis and supramolecular structure Biomacromolecules 7, 644-648
    • (2006) Biomacromolecules , vol.7 , pp. 644-648
    • Zhang, Y.H.P.1    Cui, J.B.2    Lynd, L.R.3    Kuang, L.R.4
  • 11
    • 0033485705 scopus 로고    scopus 로고
    • Acid hydrolosis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase i and endoglucanase i
    • Väljamäe, P., Sild, V., Nutt, A., Pettersson, G., and Johansson, G. (1999) Acid hydrolosis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I Eur. J. Biochem. 266, 327-334
    • (1999) Eur. J. Biochem. , vol.266 , pp. 327-334
    • Väljamäe, P.1    Sild, V.2    Nutt, A.3    Pettersson, G.4    Johansson, G.5
  • 12
    • 20344363170 scopus 로고    scopus 로고
    • Determination of the number-average degree of polymerization of cellodextrins and cellulose with application to enzymatic hydrolysis
    • Zhang, Y. H. P. and Lynd, L. R. (2005) Determination of the number-average degree of polymerization of cellodextrins and cellulose with application to enzymatic hydrolysis Biomacromolecules 6, 1510-1515
    • (2005) Biomacromolecules , vol.6 , pp. 1510-1515
    • Zhang, Y.H.P.1    Lynd, L.R.2
  • 13
    • 33845471928 scopus 로고
    • Studies of microstructure in native celluloses using solid-state C-13 NMR
    • Vanderhart, D. L. and Atalla, R. H. (1984) Studies of microstructure in native celluloses using solid-state C-13 NMR Macromolecules 17, 1465-1472
    • (1984) Macromolecules , vol.17 , pp. 1465-1472
    • Vanderhart, D.L.1    Atalla, R.H.2
  • 16
    • 2542418037 scopus 로고    scopus 로고
    • Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate
    • Gruno, M., Väljamäe, P., Pettersson, G., and Johansson, G. (2004) Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate Biotechnol. Bioeng. 86, 503-511
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 503-511
    • Gruno, M.1    Väljamäe, P.2    Pettersson, G.3    Johansson, G.4
  • 17
    • 84881116511 scopus 로고    scopus 로고
    • Product inhibition of cellulases studied with C-14-labeled cellulose substrates
    • 10.1186/1754-6834-6-104
    • Teugjas, H. and Väljamäe, P. (2013) Product inhibition of cellulases studied with C-14-labeled cellulose substrates Biotechnol. Biofuels 6 10.1186/1754-6834-6-104
    • (2013) Biotechnol. Biofuels , vol.6
    • Teugjas, H.1    Väljamäe, P.2
  • 19
    • 73649106924 scopus 로고    scopus 로고
    • High Speed Atomic Force Microscopy Visualizes Processive Movement of Trichoderma reesei Cellobiohydrolase i on Crystalline Cellulose
    • Igarashi, K., Koivula, A., Wada, M., Kimura, S., Penttila, M., and Samejima, M. (2009) High Speed Atomic Force Microscopy Visualizes Processive Movement of Trichoderma reesei Cellobiohydrolase I on Crystalline Cellulose J. Biol. Chem. 284, 36186-36190
    • (2009) J. Biol. Chem. , vol.284 , pp. 36186-36190
    • Igarashi, K.1    Koivula, A.2    Wada, M.3    Kimura, S.4    Penttila, M.5    Samejima, M.6
  • 21
    • 78650950110 scopus 로고    scopus 로고
    • Processivity of Cellobiohydrolases Is Limited by the Substrate
    • Kurasin, M. and Väljamäe, P. (2011) Processivity of Cellobiohydrolases Is Limited by the Substrate J. Biol. Chem. 286, 169-177
    • (2011) J. Biol. Chem. , vol.286 , pp. 169-177
    • Kurasin, M.1    Väljamäe, P.2
  • 22
    • 84865224370 scopus 로고    scopus 로고
    • Endo-exo Synergism in Cellulose Hydrolysis Revisited
    • Jalak, J., Kurasin, M., Teugjas, H., and Väljamäe, P. (2012) Endo-exo Synergism in Cellulose Hydrolysis Revisited J. Biol. Chem. 287, 28802-28815
    • (2012) J. Biol. Chem. , vol.287 , pp. 28802-28815
    • Jalak, J.1    Kurasin, M.2    Teugjas, H.3    Väljamäe, P.4
  • 23
    • 12844278017 scopus 로고    scopus 로고
    • Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as 'burst' kinetics on fluorescent polymeric model substrates
    • Kipper, K., Väljamäe, P., and Johansson, G. (2005) Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as 'burst' kinetics on fluorescent polymeric model substrates Biochem. J. 385, 527-535
    • (2005) Biochem. J. , vol.385 , pp. 527-535
    • Kipper, K.1    Väljamäe, P.2    Johansson, G.3
  • 25
    • 84856839149 scopus 로고    scopus 로고
    • Initial- and Processive-Cut Products Reveal Cellobiohydrolase Rate Limitations and the Role of Companion Enzymes
    • Fox, J. M., Levine, S. E., Clark, D. S., and Blanch, H. W. (2012) Initial- and Processive-Cut Products Reveal Cellobiohydrolase Rate Limitations and the Role of Companion Enzymes Biochemistry 51, 442-452
    • (2012) Biochemistry , vol.51 , pp. 442-452
    • Fox, J.M.1    Levine, S.E.2    Clark, D.S.3    Blanch, H.W.4
  • 26
    • 84865841852 scopus 로고    scopus 로고
    • Cellulase Adsorption and Reactivity on a Cellulose Surface from Flow Ellipsometry
    • Maurer, S. A., Bedbrook, C. N., and Radke, C. J. (2012) Cellulase Adsorption and Reactivity on a Cellulose Surface from Flow Ellipsometry Ind. Eng. Chem. Res. 51, 11389-11400
    • (2012) Ind. Eng. Chem. Res. , vol.51 , pp. 11389-11400
    • Maurer, S.A.1    Bedbrook, C.N.2    Radke, C.J.3
  • 27
    • 67649815010 scopus 로고    scopus 로고
    • Cellulases and biofuels
    • Wilson, D. B. (2009) Cellulases and biofuels Curr. Opin. Biotechnol. 20, 295-299
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 295-299
    • Wilson, D.B.1
  • 28
    • 84885157743 scopus 로고    scopus 로고
    • Systems-level modeling with molecular resolution elucidates the rate-limiting mechanisms of cellulose decomposition by cellobiohydrolases
    • 10.1074/jbc.M1113.497412
    • Shang, B. Z., Chang, R., and Chu, J. (2013) Systems-level modeling with molecular resolution elucidates the rate-limiting mechanisms of cellulose decomposition by cellobiohydrolases J. Biol. Chem. 10.1074/jbc.M1113.497412
    • (2013) J. Biol. Chem.
    • Shang, B.Z.1    Chang, R.2    Chu, J.3
  • 29
    • 77955691535 scopus 로고    scopus 로고
    • Mechanism of Initial Rapid Rate Retardation in Cellobiohydrolase Catalyzed Cellulose Hydrolysis
    • Jalak, J. and Väljamäe, P. (2010) Mechanism of Initial Rapid Rate Retardation in Cellobiohydrolase Catalyzed Cellulose Hydrolysis Biotechnol. Bioeng. 106, 871-883
    • (2010) Biotechnol. Bioeng. , vol.106 , pp. 871-883
    • Jalak, J.1    Väljamäe, P.2
  • 31
    • 79953781576 scopus 로고    scopus 로고
    • Molecular-Level Origins of Biomass Recalcitrance: Decrystallization Free Energies for Four Common Cellulose Polymorphs
    • Beckham, G. T., Matthews, J. F., Peters, B., Bomble, Y. J., Himmel, M. E., and Crowley, M. F. (2011) Molecular-Level Origins of Biomass Recalcitrance: Decrystallization Free Energies for Four Common Cellulose Polymorphs J. Phys. Chem. B 115, 4118-4127
    • (2011) J. Phys. Chem. B , vol.115 , pp. 4118-4127
    • Beckham, G.T.1    Matthews, J.F.2    Peters, B.3    Bomble, Y.J.4    Himmel, M.E.5    Crowley, M.F.6
  • 33
    • 79959386497 scopus 로고    scopus 로고
    • Deconstruction of Lignocellulosic Biomass to Fuels and Chemicals
    • (Prausnitz, J. M. Ed.); Annual Reviews: Palo Alto, CA
    • Chundawat, S. P. S., Beckham, G. T., Himmel, M. E., and Dale, B. E. (2011) Deconstruction of Lignocellulosic Biomass to Fuels and Chemicals in Annual Review of Chemical and Biomolecular Engineering, Vol 2 (Prausnitz, J. M., Ed.); Annual Reviews: Palo Alto, CA, pp 121-145.
    • (2011) Annual Review of Chemical and Biomolecular Engineering , vol.2 , pp. 121-145
    • Chundawat, S.P.S.1    Beckham, G.T.2    Himmel, M.E.3    Dale, B.E.4
  • 34
    • 81455141379 scopus 로고    scopus 로고
    • Determination of the molecular states of the processive endocellulase Thermobifida fusca Cel9A during crystalline cellulose depolymerization
    • Kostylev, M., Moran-Mirabal, J. M., Walker, L. P., and Wilson, D. B. (2012) Determination of the molecular states of the processive endocellulase Thermobifida fusca Cel9A during crystalline cellulose depolymerization Biotechnol. Bioeng. 109, 295-299
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 295-299
    • Kostylev, M.1    Moran-Mirabal, J.M.2    Walker, L.P.3    Wilson, D.B.4
  • 35
    • 84856578303 scopus 로고    scopus 로고
    • Elucidation of cellulose accessibility, hydrolysability and reactivity as the major limitations in the enzymatic hydrolysis of cellulose
    • Bansal, P., Vowell, B. J., Hall, M., Realff, M. J., Lee, J. H., and Bommarius, A. S. (2012) Elucidation of cellulose accessibility, hydrolysability and reactivity as the major limitations in the enzymatic hydrolysis of cellulose Bioresour. Technol. 107, 243-250
    • (2012) Bioresour. Technol. , vol.107 , pp. 243-250
    • Bansal, P.1    Vowell, B.J.2    Hall, M.3    Realff, M.J.4    Lee, J.H.5    Bommarius, A.S.6
  • 36
    • 77950356429 scopus 로고    scopus 로고
    • Access to cellulose limits the efficiency of enzymatic hydrolysis: The role of amorphogenesis
    • Arantes, V. and Saddler, J. N. (2010) Access to cellulose limits the efficiency of enzymatic hydrolysis: the role of amorphogenesis Biotechnol. Biofuels 3, 11
    • (2010) Biotechnol. Biofuels , vol.3 , pp. 11
    • Arantes, V.1    Saddler, J.N.2
  • 37
    • 78650839737 scopus 로고    scopus 로고
    • Biological pretreatment of cellulose: Enhancing enzymatic hydrolysis rate using cellulose-binding domains from cellulases
    • Hall, M., Bansal, P., Lee, J. H., Realff, M. J., and Bommarius, A. S. (2011) Biological pretreatment of cellulose: Enhancing enzymatic hydrolysis rate using cellulose-binding domains from cellulases Bioresour. Technol. 102, 2910-2915
    • (2011) Bioresour. Technol. , vol.102 , pp. 2910-2915
    • Hall, M.1    Bansal, P.2    Lee, J.H.3    Realff, M.J.4    Bommarius, A.S.5
  • 38
    • 84877736930 scopus 로고    scopus 로고
    • Binding Specificity and Thermodynamics of Cellulose-Binding Modules from Trichoderma reesei Cel7A and Cel6A
    • Guo, J. and Catchmark, J. M. (2013) Binding Specificity and Thermodynamics of Cellulose-Binding Modules from Trichoderma reesei Cel7A and Cel6A Biomacromolecules 14, 1268-1277
    • (2013) Biomacromolecules , vol.14 , pp. 1268-1277
    • Guo, J.1    Catchmark, J.M.2
  • 39
    • 0024277381 scopus 로고
    • Studies of the cellulolytic system of trichoderma-reesei QM-9414 - Analysis of domian function in2 cellobiohydrolases by limitied proteolysis
    • Tomme, P., Vantilbeurgh, H., Pettersson, G., Vandamme, J., Vandekerckhove, J., Knowles, J., Teeri, T., and Claeyssens, M. (1988) Studies of the cellulolytic system of trichoderma-reesei QM-9414-Analysis of domian function in2 cellobiohydrolases by limitied proteolysis Eur. J. Biochem. 170, 575-581
    • (1988) Eur. J. Biochem. , vol.170 , pp. 575-581
    • Tomme, P.1    Vantilbeurgh, H.2    Pettersson, G.3    Vandamme, J.4    Vandekerckhove, J.5    Knowles, J.6    Teeri, T.7    Claeyssens, M.8
  • 40
    • 0141865611 scopus 로고    scopus 로고
    • General methods for analysis of sequential ″n-step'' kinetic mechanisms: Application to single turnover kinetics of helicase-catalyzed DNA unwinding
    • Lucius, A. L., Maluf, N. K., Fischer, C. J., and Lohman, T. M. (2003) General methods for analysis of sequential ″n-step'' kinetic mechanisms: Application to single turnover kinetics of helicase-catalyzed DNA unwinding Biophys. J. 85, 2224-2239
    • (2003) Biophys. J. , vol.85 , pp. 2224-2239
    • Lucius, A.L.1    Maluf, N.K.2    Fischer, C.J.3    Lohman, T.M.4
  • 41
    • 84882415685 scopus 로고    scopus 로고
    • Binding and movement of individual Cel7A cellobiohydrolases on crystalline cellulose surfaces revealed by single-molecule fluorescence imaging
    • 10.1074/jbc.M113.455758
    • Jung, J., Sethi, A., Gaiotto, T., Jeoh, T., Gnanakaran, S., and Goodwin, P. M. (2013) Binding and movement of individual Cel7A cellobiohydrolases on crystalline cellulose surfaces revealed by single-molecule fluorescence imaging J. Biol. Chem. 10.1074/jbc.M113.455758
    • (2013) J. Biol. Chem.
    • Jung, J.1    Sethi, A.2    Gaiotto, T.3    Jeoh, T.4    Gnanakaran, S.5    Goodwin, P.M.6
  • 42
    • 0141839655 scopus 로고    scopus 로고
    • Synergistic cellulose hydrolysis can be described in terms of fractal-like kinetics
    • Väljamäe, P., Kipper, K., Pettersson, G., and Johansson, G. (2003) Synergistic cellulose hydrolysis can be described in terms of fractal-like kinetics Biotechnol. Bioeng. 84, 254-257
    • (2003) Biotechnol. Bioeng. , vol.84 , pp. 254-257
    • Väljamäe, P.1    Kipper, K.2    Pettersson, G.3    Johansson, G.4
  • 43
    • 33845390022 scopus 로고    scopus 로고
    • A new kinetic model for heterogeneous (or spatially confined) enzymatic catalysis: Contributions from the fractal and jamming (overcrowding) effects
    • Xu, F. and Ding, H. S. (2007) A new kinetic model for heterogeneous (or spatially confined) enzymatic catalysis: Contributions from the fractal and jamming (overcrowding) effects Appl. Catal., A 317, 70-81
    • (2007) Appl. Catal., A , vol.317 , pp. 70-81
    • Xu, F.1    Ding, H.S.2
  • 44
    • 84882710777 scopus 로고    scopus 로고
    • Two-Parameter Kinetic Model Based on a Time-Dependent Activity Coefficient Accurately Describes Enzymatic Cellulose Digestion
    • Kostylev, M. and Wilson, D. B. (2013) Two-Parameter Kinetic Model Based on a Time-Dependent Activity Coefficient Accurately Describes Enzymatic Cellulose Digestion Biochemistry 52, 5656-5664
    • (2013) Biochemistry , vol.52 , pp. 5656-5664
    • Kostylev, M.1    Wilson, D.B.2
  • 45
    • 3042648985 scopus 로고    scopus 로고
    • Kinetic models of sorption: A theoretical analysis
    • Azizian, S. (2004) Kinetic models of sorption: a theoretical analysis J. Colloid Interface Sci. 276, 47-52
    • (2004) J. Colloid Interface Sci. , vol.276 , pp. 47-52
    • Azizian, S.1
  • 46
    • 80052713583 scopus 로고    scopus 로고
    • Colloidal Stability of Aqueous Nanofibrillated Cellulose Dispersions
    • Fall, A. B., Lindstrom, S. B., Sundman, O., Odberg, L., and Wagberg, L. (2011) Colloidal Stability of Aqueous Nanofibrillated Cellulose Dispersions Langmuir 27, 11332-11338
    • (2011) Langmuir , vol.27 , pp. 11332-11338
    • Fall, A.B.1    Lindstrom, S.B.2    Sundman, O.3    Odberg, L.4    Wagberg, L.5
  • 47
    • 79960078984 scopus 로고    scopus 로고
    • Study on the Decreased Sugar Yield in Enzymatic Hydrolysis of Cellulosic Substrate at High Solid Loading
    • Wang, W., Kang, L., Wei, H., Arora, R., and Lee, Y. Y. (2011) Study on the Decreased Sugar Yield in Enzymatic Hydrolysis of Cellulosic Substrate at High Solid Loading Appl. Biochem. Biotechnol. 164, 1139-1149
    • (2011) Appl. Biochem. Biotechnol. , vol.164 , pp. 1139-1149
    • Wang, W.1    Kang, L.2    Wei, H.3    Arora, R.4    Lee, Y.Y.5
  • 48
    • 0023645345 scopus 로고
    • Adsorption and Kinetic-Behavior of Purified Endoglucanases and Exoglucanases from Trichoderma-Viride
    • Beldman, G., Voragen, A. G. J., Rombouts, F. M., Searlevanleeuwen, M. F., and Pilnik, W. (1987) Adsorption and Kinetic-Behavior of Purified Endoglucanases and Exoglucanases from Trichoderma-Viride Biotechnol. Bioeng. 30, 251-257 Technology
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 251
    • Beldman, G.1    Voragen, A.G.J.2    Rombouts, F.M.3    Searlevanleeuwen, M.F.4    Pilnik, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.