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Volumn 51, Issue 5, 2008, Pages 459-469

Structural changes of cellobiohydrolase I (1,4-β-D-glucan- cellobiohydrolase I, CBHI) and PNPC (p-nitrophenyl-β-D-cellobioside) during the binding process

Author keywords

Cellobiohydrolase I; Conformation configuration; p nitrophenyl D cellobioside; Saturated binding point

Indexed keywords

4 NITROPHENYL BETA CELLOBIOSIDE; 4-NITROPHENYL BETA-CELLOBIOSIDE; CELLULOSE 1,4 BETA CELLOBIOSIDASE; GLUCOSIDE;

EID: 43149111600     PISSN: 10069305     EISSN: 18622798     Source Type: Journal    
DOI: 10.1007/s11427-008-0064-2     Document Type: Article
Times cited : (1)

References (45)
  • 1
    • 0006298689 scopus 로고
    • Correlation of structure and function in enzyme action
    • Koshland D E Jr. Correlation of structure and function in enzyme action. Science, 1963, 142: 1533-1541
    • (1963) Science , vol.142 , pp. 1533-1541
    • Koshland Jr., D.E.1
  • 2
    • 0015537695 scopus 로고
    • Conformational adaptability in enzymes
    • Citri N. Conformational adaptability in enzymes. Adv Enzymol. Relat Areas Mol Biol, 1973, 37: 397-648
    • (1973) Adv Enzymol. Relat Areas Mol Biol , vol.37 , pp. 397-648
    • Citri, N.1
  • 3
    • 0014235891 scopus 로고
    • The catalytic and regulatory properties of enzymes
    • Koshland D E Jr, Neet K E. The catalytic and regulatory properties of enzymes. Annul Rev Biochem, 1968, 37: 359-410
    • (1968) Annul Rev Biochem , vol.37 , pp. 359-410
    • Koshland Jr., D.E.1    Neet, K.E.2
  • 4
    • 0031800353 scopus 로고    scopus 로고
    • Trichoderma reesei cellobiohydrolases: Why so efficient on crystalline cellulose?
    • Teeri T T, Koivula A, Linder M, et al. Trichoderma reesei cellobiohydrolases: Why so efficient on crystalline cellulose? Biochem Soc Trans, 1998, 26: 173-178
    • (1998) Biochem Soc Trans , vol.26 , pp. 173-178
    • Teeri, T.T.1    Koivula, A.2    Linder, M.3
  • 5
    • 0029023464 scopus 로고
    • Identification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase I
    • Linder M, Mattinen M L, Kontteli M, et al. Identification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase I. Protein Sci, 1995, 4: 1056-1064
    • (1995) Protein Sci , vol.4 , pp. 1056-1064
    • Linder, M.1    Mattinen, M.L.2    Kontteli, M.3
  • 6
    • 0032537565 scopus 로고    scopus 로고
    • Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A
    • Koivula A, Kinnari T, Harjunpaa V, et al. Tryptophan 272: An essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A. FEBS Lett, 1998, 429: 341-346
    • (1998) FEBS Lett , vol.429 , pp. 341-346
    • Koivula, A.1    Kinnari, T.2    Harjunpaa, V.3
  • 7
    • 0036180898 scopus 로고    scopus 로고
    • Identification and glucan-binding properties of a new carbohydrate-binding module family
    • Boraston A B, Ghaffari M, Warren R A J, et al. Identification and glucan-binding properties of a new carbohydrate-binding module family. Biochem J, 2002, 361: 45-40
    • (2002) Biochem J , vol.361 , pp. 45-40
    • Boraston, A.B.1    Ghaffari, M.2    Warren, R.A.J.3
  • 8
    • 4544354845 scopus 로고    scopus 로고
    • The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4-and beta-1,3-1,4-mixed linked glucans at a single binding site
    • Carvalho A L, Goyal A, Prates J A, et al. The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4-and beta-1,3-1,4-mixed linked glucans at a single binding site. J Biol Chem, 2004, 279: 34785-34793
    • (2004) J Biol Chem , vol.279 , pp. 34785-34793
    • Carvalho, A.L.1    Goyal, A.2    Prates, J.A.3
  • 9
    • 12844278693 scopus 로고    scopus 로고
    • The interaction of carbohydrate-binding modules with insoluble non-crystalline cellulose is enthalpically driven
    • Boraston A B. The interaction of carbohydrate-binding modules with insoluble non-crystalline cellulose is enthalpically driven, Biochem J, 2005, 385: 479-484
    • (2005) Biochem J , vol.385 , pp. 479-484
    • Boraston, A.B.1
  • 10
    • 12344307441 scopus 로고    scopus 로고
    • Conformational changes observed in enzyme crystal structures upon substrate binding
    • Gutteridge A, Thornton J. Conformational changes observed in enzyme crystal structures upon substrate binding. J Mol Biol, 2005, 346: 21-28
    • (2005) J Mol Biol , vol.346 , pp. 21-28
    • Gutteridge, A.1    Thornton, J.2
  • 11
    • 0042099120 scopus 로고    scopus 로고
    • Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellum
    • Gao P J, Chen G J, Wang T H, et al. Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellum. Acta Biochim Biophys Sin, 2001, 33: 13-18
    • (2001) Acta Biochim Biophys Sin , vol.33 , pp. 13-18
    • Gao, P.J.1    Chen, G.J.2    Wang, T.H.3
  • 12
    • 17644439305 scopus 로고    scopus 로고
    • Comparison of domains function between cellobiohydrolase I and endoglucanase I from Trichoderma pseudokoningii S38 by limited proteolysis
    • Wang L S, Liu J, Zhang Y Z, et al. Comparison of domains function between cellobiohydrolase I and endoglucanase I from Trichoderma pseudokoningii S38 by limited proteolysis. J Mol Catalysis B-Enzyme, 2003, 24-25: 27-28
    • (2003) J Mol Catalysis B-Enzyme , vol.24-25 , pp. 27-28
    • Wang, L.S.1    Liu, J.2    Zhang, Y.Z.3
  • 13
    • 32544437997 scopus 로고    scopus 로고
    • Changes in the structural properties and rate of hydrolysis of cotton fibers during extended enzymatic hydrolysis
    • Wang L S, Zhang Y Z, Gao P J, et al. Changes in the structural properties and rate of hydrolysis of cotton fibers during extended enzymatic hydrolysis. Biotech Bioeng, 2006, 93: 443-456
    • (2006) Biotech Bioeng , vol.93 , pp. 443-456
    • Wang, L.S.1    Zhang, Y.Z.2    Gao, P.J.3
  • 14
    • 33745154796 scopus 로고    scopus 로고
    • Estimation of cellobiohydrolase I activity by numerical differentiation of dynamic ultraviolet spectroscopy
    • Wu B, Zhao Y, Gao P J. Estimation of cellobiohydrolase I activity by numerical differentiation of dynamic ultraviolet spectroscopy. Acta Biochim Biophys Sin (Shanghai), 2006, 38: 372-378
    • (2006) Acta Biochim Biophys Sin (Shanghai) , vol.38 , pp. 372-378
    • Wu, B.1    Zhao, Y.2    Gao, P.J.3
  • 15
    • 0348198534 scopus 로고    scopus 로고
    • Correlation between the UV spectra of glycated peptides and amino acids
    • Argirova M C, Argirov O K. Correlation between the UV spectra of glycated peptides and amino acids. Spectrochim Acta A, 1999, 55: 245-250
    • (1999) Spectrochim Acta a , vol.55 , pp. 245-250
    • Argirova, M.C.1    Argirov, O.K.2
  • 16
    • 0028797276 scopus 로고
    • Analysis of equilibrium binding data obtained by linear-response spectroscopic techniques
    • Toptygin D, Brand L. Analysis of equilibrium binding data obtained by linear-response spectroscopic techniques. Anal Biochem, 1995, 234: 330-338
    • (1995) Anal Biochem , vol.234 , pp. 330-338
    • Toptygin, D.1    Brand, L.2
  • 17
    • 0025469223 scopus 로고
    • Preliminary studies on the mechanism of cellulose formation by Trichoderma pseudokoningii S-38
    • Ma D B, Gao P J, Wang Z N. Preliminary studies on the mechanism of cellulose formation by Trichoderma pseudokoningii S-38. Enzyme Microb Technol, 1990, 12: 631-635
    • (1990) Enzyme Microb Technol , vol.12 , pp. 631-635
    • Ma, D.B.1    Gao, P.J.2    Wang, Z.N.3
  • 18
    • 0030823674 scopus 로고    scopus 로고
    • Intrinsic fluorescence in endoglucanase and cellobiohydrolase from Trichoderma pseudokiningii S-38: Effects of pH, quenching agents, and ligand binding
    • Yan B X, Sun Y Q, Gao P J. Intrinsic fluorescence in endoglucanase and cellobiohydrolase from Trichoderma pseudokiningii S-38: Effects of pH, quenching agents, and ligand binding. J Protein Chem, 1997, 16: 681-688
    • (1997) J Protein Chem , vol.16 , pp. 681-688
    • Yan, B.X.1    Sun, Y.Q.2    Gao, P.J.3
  • 19
    • 16244362365 scopus 로고    scopus 로고
    • Second derivative tryptophan fluorescence spectroscopy as a tool to characterize partially unfolded intermediates of proteins
    • Kumar V, Sharma V K, Kalonia D S. Second derivative tryptophan fluorescence spectroscopy as a tool to characterize partially unfolded intermediates of proteins. Int J Pharm, 2005, 294: 193-199
    • (2005) Int J Pharm , vol.294 , pp. 193-199
    • Kumar, V.1    Sharma, V.K.2    Kalonia, D.S.3
  • 20
    • 0037016375 scopus 로고    scopus 로고
    • Second derivative fluorescence spectroscopy of tryptophan in proteins
    • Mozo-Villarias A. Second derivative fluorescence spectroscopy of tryptophan in proteins. J Biochem Biophys Methods, 2002, 50: 163-178
    • (2002) J Biochem Biophys Methods , vol.50 , pp. 163-178
    • Mozo-Villarias, A.1
  • 22
    • 0027052236 scopus 로고
    • Optimum numerical integration methods for estimation of area-under-the-curve (AUC) and area-under-the-moment-curve (AUMC)
    • Purves R D. Optimum numerical integration methods for estimation of area-under-the-curve (AUC) and area-under-the-moment-curve (AUMC). J Pharmacokinet Biopharm, 1992, 20: 211-226
    • (1992) J Pharmacokinet Biopharm , vol.20 , pp. 211-226
    • Purves, R.D.1
  • 23
    • 0001326918 scopus 로고    scopus 로고
    • Determination of instantaneous growth rates using a cubic spline approximation
    • Parchevsky K V, Parchcevsky V P. Determination of instantaneous growth rates using a cubic spline approximation. Thermochima ACTA, 1998, 309: 181-192
    • (1998) Thermochima ACTA , vol.309 , pp. 181-192
    • Parchevsky, K.V.1    Parchcevsky, V.P.2
  • 24
    • 0030888470 scopus 로고    scopus 로고
    • Quantitative analysis of ligand-macromolecule interactions using differential dynamic quenching of the ligand fluorescence to monitor the binding
    • Jezewska M J, Bujalowski W. Quantitative analysis of ligand-macromolecule interactions using differential dynamic quenching of the ligand fluorescence to monitor the binding. Biophys Chem, 1997, 64: 253-269
    • (1997) Biophys Chem , vol.64 , pp. 253-269
    • Jezewska, M.J.1    Bujalowski, W.2
  • 25
    • 0027378450 scopus 로고
    • Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants
    • Royer C A, Mann C J, Matthews C R. Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants. Protein Sci, 1993, 2: 1844-1852
    • (1993) Protein Sci , vol.2 , pp. 1844-1852
    • Royer, C.A.1    Mann, C.J.2    Matthews, C.R.3
  • 26
    • 0037691729 scopus 로고    scopus 로고
    • Fluorescence study of ligand binding to potato tuber pyrophosphate- dependent phosphofructokinase: Evidence for competitive binding between fructose-1,6-bisphosphate and fructose-2,6-bisphosphate
    • Podesta F E, Plaxton W C. Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: Evidence for competitive binding between fructose-1,6-bisphosphate and fructose-2,6-bisphosphate. Arch Biochem Biophys, 2003, 414: 101-107
    • (2003) Arch Biochem Biophys , vol.414 , pp. 101-107
    • Podesta, F.E.1    Plaxton, W.C.2
  • 27
    • 4143130272 scopus 로고    scopus 로고
    • Effect of guanidine hydrochloride on bovine serum albumin complex with anti-thyroid drugs: Fluorescence study
    • Sulkowska A, Równicka J, Bojko B, et al. Effect of guanidine hydrochloride on bovine serum albumin complex with anti-thyroid drugs: Fluorescence study. J Mol Struct, 2004, 704: 291-295
    • (2004) J Mol Struct , vol.704 , pp. 291-295
    • Sulkowska, A.1    Równicka, J.2    Bojko, B.3
  • 28
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T, Williston S, Brandts J F, et al. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem, 1989, 179: 131-137
    • (1989) Anal Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3
  • 29
    • 0029112951 scopus 로고
    • Calorimetric methods for interpreting protein-ligand interactions
    • Fisher H F, Singh N. Calorimetric methods for interpreting protein-ligand interactions. Methods Enzymol, 1995, 259: 194-221
    • (1995) Methods Enzymol , vol.259 , pp. 194-221
    • Fisher, H.F.1    Singh, N.2
  • 30
    • 43149095433 scopus 로고    scopus 로고
    • Mechanism of cellobiose inhibition in cellulose hydrolysis by cellobiohydrolase
    • Zhao Y, Wu B, Gao P J. Mechanism of cellobiose inhibition in cellulose hydrolysis by cellobiohydrolase. Sci China Ser C-Life Sci, 2004, 47: 18-24
    • (2004) Sci China Ser C-Life Sci , vol.47 , pp. 18-24
    • Zhao, Y.1    Wu, B.2    Gao, P.J.3
  • 31
    • 10644273997 scopus 로고    scopus 로고
    • Nonequilibrium and nonlinear chemistry
    • Li R S, Wan R. Nonequilibrium and nonlinear chemistry. Prog Chem, 1996, 8: 17-29
    • (1996) Prog Chem , vol.8 , pp. 17-29
    • Li, R.S.1    Wan, R.2
  • 32
    • 10644257518 scopus 로고    scopus 로고
    • Thermodynamics of irreversible process in homogeneous single chemical reaction
    • Zhai Y C, Wang J X. Thermodynamics of irreversible process in homogeneous single chemical reaction. J Northeastern Univ (Nature Science), 2004, 25: 994-997
    • (2004) J Northeastern Univ (Nature Science) , vol.25 , pp. 994-997
    • Zhai, Y.C.1    Wang, J.X.2
  • 33
    • 0023647288 scopus 로고
    • Kinetics of substrate reaction during irreversible modification of enzyme activity for enzymes involving two substrates
    • 3
    • Wang Z X, Tsou C L. Kinetics of substrate reaction during irreversible modification of enzyme activity for enzymes involving two substrates. J Theor Biol, 1987, 127(3): 253-270
    • (1987) J Theor Biol , vol.127 , pp. 253-270
    • Wang, Z.X.1    Tsou, C.L.2
  • 34
    • 0000166289 scopus 로고
    • Treatment of enzyme kinetic data
    • Frieden C. Treatment of enzyme kinetic data. J Biol chem, 1964, 239: 3522-3531
    • (1964) J Biol Chem , vol.239 , pp. 3522-3531
    • Frieden, C.1
  • 35
    • 0024299430 scopus 로고
    • Half-time analysis of the kinetics of irreversible enzyme inhibition by unstable site-specific reagent
    • Topham C M. Half-time analysis of the kinetics of irreversible enzyme inhibition by unstable site-specific reagent. Biochem Biophys Acta, 1988, 955: 65-76
    • (1988) Biochem Biophys Acta , vol.955 , pp. 65-76
    • Topham, C.M.1
  • 36
    • 0642315208 scopus 로고
    • Transient-state kinetic analysis of enzyme reaction pathways
    • Johnson K A. Transient-state kinetic analysis of enzyme reaction pathways. The Enzyme, 1992, 20: 1-61
    • (1992) The Enzyme , vol.20 , pp. 1-61
    • Johnson, K.A.1
  • 37
    • 0141959705 scopus 로고    scopus 로고
    • Generalization theoretical and practical treatment of the kinetics of an enzyme-catalyzed reaction in the presence of an enzyme equimolar irreversible inhibitor
    • Golicnik M, Stojan J. Generalization theoretical and practical treatment of the kinetics of an enzyme-catalyzed reaction in the presence of an enzyme equimolar irreversible inhibitor. J Chem Inf Comput Sci, 2003, 43: 1486-1493
    • (2003) J Chem Inf Comput Sci , vol.43 , pp. 1486-1493
    • Golicnik, M.1    Stojan, J.2
  • 38
    • 12344320206 scopus 로고    scopus 로고
    • The comparison of the estimation of enzyme kinetic parameters by fitting reaction curve to the integrated Michaelis-Menten rate equations of different predictor variables
    • Liao F, Zhu X Y, Wang Y M, et al. The comparison of the estimation of enzyme kinetic parameters by fitting reaction curve to the integrated Michaelis-Menten rate equations of different predictor variables. J Biochem and Biophys Methods, 2005, 62: 13-24
    • (2005) J Biochem and Biophys Methods , vol.62 , pp. 13-24
    • Liao, F.1    Zhu, X.Y.2    Wang, Y.M.3
  • 39
    • 36949075170 scopus 로고
    • Acceleration of chemical reaction
    • Ray C T G, Yourgra W. Acceleration of chemical reaction. Nature, 1956, 178: 809
    • (1956) Nature , vol.178 , pp. 809
    • Ray, C.T.G.1    Yourgra, W.2
  • 40
    • 43149100879 scopus 로고
    • Time variation of chemical affinity
    • Yourgra W, Ray C T G. Time variation of chemical affinity. Nature, 1958, 181: 80
    • (1958) Nature , vol.181 , pp. 80
    • Yourgra, W.1    Ray, C.T.G.2
  • 41
    • 0043199004 scopus 로고
    • Thermochemistry of reaction materials
    • Bowen R M. Thermochemistry of reaction materials. J Chem Phys, 1968, 49: 1625-1637
    • (1968) J Chem Phys , vol.49 , pp. 1625-1637
    • Bowen, R.M.1
  • 42
    • 31344462177 scopus 로고    scopus 로고
    • Conformational diversity of ligands bound to proteins
    • Stockwell G R, Thornton J M. Conformational diversity of ligands bound to proteins. J Mol Biol, 2006, 356: 928-944
    • (2006) J Mol Biol , vol.356 , pp. 928-944
    • Stockwell, G.R.1    Thornton, J.M.2
  • 43
    • 0034248114 scopus 로고    scopus 로고
    • Conformational cycle of a single working enzyme
    • Agmon N. Conformational cycle of a single working enzyme. J Phys Chem B, 2000, 104: 7830-7834
    • (2000) J Phys Chem B , vol.104 , pp. 7830-7834
    • Agmon, N.1
  • 44
    • 0035543093 scopus 로고    scopus 로고
    • The depth of chemical time and the power of enzymes as catalysts
    • Wolfenden R, Snider M J. The depth of chemical time and the power of enzymes as catalysts. Acc Chem Res, 2001, 34: 938-945
    • (2001) Acc Chem Res , vol.34 , pp. 938-945
    • Wolfenden, R.1    Snider, M.J.2
  • 45
    • 0001290941 scopus 로고
    • Conformational energy calculations on polypeptide and proteins
    • Vasquez M, Nemethy G, Scheraga H A. Conformational energy calculations on polypeptide and proteins. Chem Rev, 1994, 94: 2183-2239
    • (1994) Chem Rev , vol.94 , pp. 2183-2239
    • Vasquez, M.1    Nemethy, G.2    Scheraga, H.A.3


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