Physical constraints and functional plasticity of cellulases
Enzyme reactions at interfaces are common in both Nature and industrial applications but no general kinetic framework exists for interfacial enzymes. Here, the authors kinetically characterize 83 cellulases and identify a scaling relationship between ligand binding strength and maximal turnover, a s...
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Nature Publishing Group
2021-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-24075-y |
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doaj-57fe6ad3515b457c841b93644728432e2021-06-27T11:11:41ZengNature Publishing GroupNature Communications2041-17232021-06-0112111010.1038/s41467-021-24075-yPhysical constraints and functional plasticity of cellulasesJeppe Kari0Gustavo A. Molina1Kay S. Schaller2Corinna Schiano-di-Cola3Stefan J. Christensen4Silke F. Badino5Trine H. Sørensen6Nanna S. Røjel7Malene B. Keller8Nanna Rolsted Sørensen9Bartlomiej Kolaczkowski10Johan P. Olsen11Kristian B. R. M. Krogh12Kenneth Jensen13Ana M. Cavaleiro14Günther H. J. Peters15Nikolaj Spodsberg16Kim Borch17Peter Westh18Department of Biotechnology and Biomedicine, Technical University of DenmarkDepartment of Biotechnology and Biomedicine, Technical University of DenmarkDepartment of Biotechnology and Biomedicine, Technical University of DenmarkDepartment of Biotechnology and Biomedicine, Technical University of DenmarkDepartment of Biotechnology and Biomedicine, Technical University of DenmarkDepartment of Biotechnology and Biomedicine, Technical University of DenmarkNovozymes A/SDepartment of Science and Environment, Roskilde University, Universitetsvej 1Department of Geosciences and Natural Resource Management, University of CopenhagenDepartment of Science and Environment, Roskilde University, Universitetsvej 1Department of Science and Environment, Roskilde University, Universitetsvej 1Novozymes A/SNovozymes A/SNovozymes A/SNovozymes A/SDepartment of Chemistry, Technical University of DenmarkNovozymes A/SNovozymes A/SDepartment of Biotechnology and Biomedicine, Technical University of DenmarkEnzyme reactions at interfaces are common in both Nature and industrial applications but no general kinetic framework exists for interfacial enzymes. Here, the authors kinetically characterize 83 cellulases and identify a scaling relationship between ligand binding strength and maximal turnover, a so-called linear free energy relationship, which may help rationalize cellulolytic mechanisms and guide the selection of technical enzymes.https://doi.org/10.1038/s41467-021-24075-y |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Jeppe Kari Gustavo A. Molina Kay S. Schaller Corinna Schiano-di-Cola Stefan J. Christensen Silke F. Badino Trine H. Sørensen Nanna S. Røjel Malene B. Keller Nanna Rolsted Sørensen Bartlomiej Kolaczkowski Johan P. Olsen Kristian B. R. M. Krogh Kenneth Jensen Ana M. Cavaleiro Günther H. J. Peters Nikolaj Spodsberg Kim Borch Peter Westh |
| spellingShingle |
Jeppe Kari Gustavo A. Molina Kay S. Schaller Corinna Schiano-di-Cola Stefan J. Christensen Silke F. Badino Trine H. Sørensen Nanna S. Røjel Malene B. Keller Nanna Rolsted Sørensen Bartlomiej Kolaczkowski Johan P. Olsen Kristian B. R. M. Krogh Kenneth Jensen Ana M. Cavaleiro Günther H. J. Peters Nikolaj Spodsberg Kim Borch Peter Westh Physical constraints and functional plasticity of cellulases Nature Communications |
| author_facet |
Jeppe Kari Gustavo A. Molina Kay S. Schaller Corinna Schiano-di-Cola Stefan J. Christensen Silke F. Badino Trine H. Sørensen Nanna S. Røjel Malene B. Keller Nanna Rolsted Sørensen Bartlomiej Kolaczkowski Johan P. Olsen Kristian B. R. M. Krogh Kenneth Jensen Ana M. Cavaleiro Günther H. J. Peters Nikolaj Spodsberg Kim Borch Peter Westh |
| author_sort |
Jeppe Kari |
| title |
Physical constraints and functional plasticity of cellulases |
| title_short |
Physical constraints and functional plasticity of cellulases |
| title_full |
Physical constraints and functional plasticity of cellulases |
| title_fullStr |
Physical constraints and functional plasticity of cellulases |
| title_full_unstemmed |
Physical constraints and functional plasticity of cellulases |
| title_sort |
physical constraints and functional plasticity of cellulases |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2021-06-01 |
| description |
Enzyme reactions at interfaces are common in both Nature and industrial applications but no general kinetic framework exists for interfacial enzymes. Here, the authors kinetically characterize 83 cellulases and identify a scaling relationship between ligand binding strength and maximal turnover, a so-called linear free energy relationship, which may help rationalize cellulolytic mechanisms and guide the selection of technical enzymes. |
| url |
https://doi.org/10.1038/s41467-021-24075-y |
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