Kinetics of Cellobiohydrolase ( Cel 7 A ) Variants with Lowered Substrate

Background: To elucidate the rate-determining steps of cellobiohydrolase Cel7A from T. reesei, variants with lower substrate affinity were designed. Results: Mutant (W38A) had reduced substrate affinity but a 2-fold increase in the maximum quasi-steady-state rate. Conclusion: Dissociation of stalled TrCel7A is the rate-limiting step in the initial phase of hydrolysis. Significance: This work offers a new perspective for the design of faster cellulases.

[1]  K. Jensen,et al.  In situ stability of substrate-associated cellulases studied by DSC. , 2014, Langmuir : the ACS journal of surfaces and colloids.

[2]  Christina M. Payne,et al.  Towards a molecular-level theory of carbohydrate processivity in glycoside hydrolases. , 2014, Current opinion in biotechnology.

[3]  M. Himmel,et al.  Cel48A from Thermobifida fusca: Structure and site directed mutagenesis of key residues , 2014, Biotechnology and bioengineering.

[4]  A. Suurnäkki,et al.  Cellulose hydrolysis and binding with Trichoderma reesei Cel5A and Cel7A and their core domains in ionic liquid solutions , 2014, Biotechnology and bioengineering.

[5]  T. Ando,et al.  Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose. , 2014, Journal of the American Chemical Society.

[6]  P. Westh,et al.  A graphene screen-printed carbon electrode for real-time measurements of unoccupied active sites in a cellulase. , 2014, Analytical biochemistry.

[7]  S. Withers,et al.  The mechanism of cellulose hydrolysis by a two-step, retaining cellobiohydrolase elucidated by structural and transition path sampling studies. , 2014, Journal of the American Chemical Society.

[8]  Christina M. Payne,et al.  Glycoside hydrolase processivity is directly related to oligosaccharide binding free energy. , 2013, Journal of the American Chemical Society.

[9]  P. Westh,et al.  Transient kinetics and rate-limiting steps for the processive cellobiohydrolase Cel7A: effects of substrate structure and carbohydrate binding domain. , 2013, Biochemistry.

[10]  Maxim Kostylev,et al.  Two-parameter kinetic model based on a time-dependent activity coefficient accurately describes enzymatic cellulose digestion. , 2013, Biochemistry.

[11]  J. Chu,et al.  Systems-level Modeling with Molecular Resolution Elucidates the Rate-limiting Mechanisms of Cellulose Decomposition by Cellobiohydrolases* , 2013, The Journal of Biological Chemistry.

[12]  P. Westh,et al.  A steady‐state theory for processive cellulases , 2013, The FEBS journal.

[13]  Harvey W Blanch,et al.  A single-molecule analysis reveals morphological targets for cellulase synergy. , 2013, Nature chemical biology.

[14]  Christina M. Payne,et al.  Binding site dynamics and aromatic-carbohydrate interactions in processive and non-processive family 7 glycoside hydrolases. , 2013, The journal of physical chemistry. B.

[15]  A. Koivula,et al.  The Tryptophan Residue at the Active Site Tunnel Entrance of Trichoderma reesei Cellobiohydrolase Cel7A Is Important for Initiation of Degradation of Crystalline Cellulose* , 2013, The Journal of Biological Chemistry.

[16]  E. Uberbacher,et al.  Initial recognition of a cellodextrin chain in the cellulose-binding tunnel may affect cellobiohydrolase directional specificity. , 2013, Biophysical journal.

[17]  B. Nidetzky,et al.  Enzymatic hydrolysis of microcrystalline cellulose and pretreated wheat straw: a detailed comparison using convenient kinetic analysis. , 2013, Bioresource technology.

[18]  L. Gorton,et al.  An amperometric enzyme biosensor for real-time measurements of cellobiohydrolase activity on insoluble cellulose. , 2012, Biotechnology and bioengineering.

[19]  Clayton J. Radke,et al.  Cellulase Adsorption and Reactivity on a Cellulose Surface from Flow Ellipsometry , 2012 .

[20]  P. Väljamäe,et al.  Endo-exo Synergism in Cellulose Hydrolysis Revisited* , 2012, The Journal of Biological Chemistry.

[21]  Anne Line Norberg,et al.  Processivity and substrate-binding in family 18 chitinases , 2012 .

[22]  Peter Westh,et al.  Pre-steady-state Kinetics for Hydrolysis of Insoluble Cellulose by Cellobiohydrolase Cel7A* , 2012, The Journal of Biological Chemistry.

[23]  Harvey W Blanch,et al.  Initial- and processive-cut products reveal cellobiohydrolase rate limitations and the role of companion enzymes. , 2012, Biochemistry.

[24]  D. Wilson,et al.  Cellulase processivity. , 2012, Methods in molecular biology.

[25]  M. Himmel,et al.  Computational Investigation of Glycosylation Effects on a Family 1 Carbohydrate-binding Module * □ S , 2022 .

[26]  T. Ando,et al.  Traffic Jams Reduce Hydrolytic Efficiency of Cellulase on Cellulose Surface , 2011, Science.

[27]  Bruce E Dale,et al.  Deconstruction of lignocellulosic biomass to fuels and chemicals. , 2011, Annual review of chemical and biomolecular engineering.

[28]  Peter Westh,et al.  A kinetic model for the burst phase of processive cellulases , 2011, The FEBS journal.

[29]  Baron Peters,et al.  Molecular-level origins of biomass recalcitrance: decrystallization free energies for four common cellulose polymorphs. , 2011, The journal of physical chemistry. B.

[30]  P. Westh,et al.  Kinetics of Enzymatic High-Solid Hydrolysis of Lignocellulosic Biomass Studied by Calorimetry , 2011, Applied biochemistry and biotechnology.

[31]  P. Väljamäe,et al.  Processivity of Cellobiohydrolases Is Limited by the Substrate* , 2010, The Journal of Biological Chemistry.

[32]  Martin J. Baumann,et al.  An enzymatic signal amplification system for calorimetric studies of cellobiohydrolases. , 2010, Analytical biochemistry.

[33]  P. Väljamäe,et al.  Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis , 2010, Biotechnology and bioengineering.

[34]  Jay H. Lee,et al.  Modeling cellulase kinetics on lignocellulosic substrates. , 2009, Biotechnology advances.

[35]  M. Penttilä,et al.  High Speed Atomic Force Microscopy Visualizes Processive Movement of Trichoderma reesei Cellobiohydrolase I on Crystalline Cellulose* , 2009, The Journal of Biological Chemistry.

[36]  D. Wilson,et al.  Processivity, Synergism, and Substrate Specificity of Thermobifida fusca Cel6B , 2009, Applied and Environmental Microbiology.

[37]  D. Wilson Cellulases and biofuels. , 2009, Current opinion in biotechnology.

[38]  V. Eijsink,et al.  Aromatic Residues in the Catalytic Center of Chitinase A from Serratia marcescens Affect Processivity, Enzyme Activity, and Biomass Converting Efficiency* , 2009, Journal of Biological Chemistry.

[39]  Sarah E. Kiehna,et al.  Carbohydrate-pi interactions: what are they worth? , 2008, Journal of the American Chemical Society.

[40]  Jan Larsen,et al.  The IBUS Process – Lignocellulosic Bioethanol Close to a Commercial Reality , 2008 .

[41]  R. Haser,et al.  Structures of mutants of cellulase Cel48F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action. , 2008, Journal of molecular biology.

[42]  Sarah E. Kiehna,et al.  Evaluation of a carbohydrate-pi interaction in a peptide model system. , 2007, Chemical communications.

[43]  C. Felby,et al.  Enzymatic conversion of lignocellulose into fermentable sugars: challenges and opportunities , 2007 .

[44]  David K. Johnson,et al.  Biomass Recalcitrance: Engineering Plants and Enzymes for Biofuels Production , 2007, Science.

[45]  B. Synstad,et al.  Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides , 2006, Proceedings of the National Academy of Sciences.

[46]  M. Wada,et al.  Surface density of cellobiohydrolase on crystalline celluloses , 2006, The FEBS journal.

[47]  G. Johansson,et al.  Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as 'burst' kinetics on fluorescent polymeric model substrates. , 2005, The Biochemical journal.

[48]  L. Lynd,et al.  Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems , 2004, Biotechnology and bioengineering.

[49]  Göran Pettersson,et al.  Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate , 2004, Biotechnology and bioengineering.

[50]  M. Claeyssens,et al.  Structural and functional domains of cellobiohydrolase I from trichoderma reesei , 1988, European Biophysics Journal.

[51]  M. Hashimoto,et al.  Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin. , 2003, The Biochemical journal.

[52]  M. Harris,et al.  Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D. , 2003, Journal of molecular biology.

[53]  J. Sugiyama,et al.  The binding specificity and affinity determinants of family 1 and family 3 cellulose binding modules , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[54]  Johan Karlsson,et al.  A model explaining declining rate in hydrolysis of lignocellulose substrates with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) of Trichoderma reesei , 2002, Applied biochemistry and biotechnology.

[55]  B. Matthews,et al.  A structural basis for processivity , 2001, Protein science : a publication of the Protein Society.

[56]  Shenmin Zhang,et al.  Site-directed mutation of noncatalytic residues of Thermobifida fusca exocellulase Cel6B. , 2000, European journal of biochemistry.

[57]  B. Synstad,et al.  Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[58]  R. Haser,et al.  Crystal structures of the cellulase Cel48F in complex with inhibitors and substrates give insights into its processive action. , 2000, Biochemistry.

[59]  M. Tenkanen,et al.  Dynamic Interaction of Trichoderma reesei Cellobiohydrolases Cel6A and Cel7A and Cellulose at Equilibrium and during Hydrolysis , 1999, Applied and Environmental Microbiology.

[60]  L. Ruohonen,et al.  Tryptophan 272: an essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A , 1998, FEBS letters.

[61]  T. A. Jones,et al.  High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei. , 1998, Journal of molecular biology.

[62]  Tuula T. Teeri,et al.  Crystalline cellulose degradation : new insight into the function of cellobiohydrolases , 1997 .

[63]  T. Reinikainen,et al.  The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. , 1994, Science.

[64]  J. Ståhlberg,et al.  A New Model For Enzymatic Hydrolysis of Cellulose Based on the Two-Domain Structure of Cellobiohydrolase I , 1991, Bio/Technology.

[65]  J. Knowles,et al.  Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. , 1990, Science.