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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cruys-bagger, Nicolaj Kari, Jeppe Borch, Kim Olsen, Johan Jensen, Kenneth Westh, Peter |
| Description | Author Affiliation: Kari J ( From Department of Science, Systems and Models, Research Unit for Functional Biomaterials, Roskilde University, 1 Universitetsvej, DK-4000 Roskilde, Denmark and.); Olsen J ( From Department of Science, Systems and Models, Research Unit for Functional Biomaterials, Roskilde University, 1 Universitetsvej, DK-4000 Roskilde, Denmark and.); Borch K ( Novozymes A/S, Krogshøjvej 36, Bagsværd DK-2880, Denmark.); Cruys-Bagger N ( From Department of Science, Systems and Models, Research Unit for Functional Biomaterials, Roskilde University, 1 Universitetsvej, DK-4000 Roskilde, Denmark and.); Jensen K ( Novozymes A/S, Krogshøjvej 36, Bagsværd DK-2880, Denmark.); Westh P ( From Department of Science, Systems and Models, Research Unit for Functional Biomaterials, Roskilde University, 1 Universitetsvej, DK-4000 Roskilde, Denmark and pwesth@ruc.dk.) |
| Abstract | Cellobiohydrolases are exo-active glycosyl hydrolases that processively convert cellulose to soluble sugars, typically cellobiose. They effectively break down crystalline cellulose and make up a major component in industrial enzyme mixtures used for deconstruction of lignocellulosic biomass. Identification of the rate-limiting step for cellobiohydrolases remains controversial, and recent reports have alternately suggested either association (on-rate) or dissociation (off-rate) as the overall bottleneck. Obviously, this uncertainty hampers both fundamental mechanistic understanding and rational design of enzymes with improved industrial applicability. To elucidate the role of on- and off-rates, respectively, on the overall kinetics, we have expressed a variant in which a tryptophan residue (Trp-38) in the middle of the active tunnel has been replaced with an alanine. This mutation weakens complex formation, and the population of substrate-bound W38A was only about half of the wild type. Nevertheless, the maximal, steady-state rate was twice as high for the variant enzyme. It is argued that these opposite effects on binding and activity can be reconciled if the rate-limiting step is after the catalysis (i.e. in the dissociation process). |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 47 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-11-21 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cellulose 1,4-beta-Cellobiosidase Genetics Fungal Proteins Mutation Trichoderma Alanine Chemistry Metabolism Amino Acid Substitution Binding Sites Binding, Competitive Biocatalysis Catalytic Domain Cellobiose Cellulose Kinetics Models, Molecular Protein Binding Substrate Specificity Thermodynamics Enzymology Tryptophan Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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