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 Portfolio
2021
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oai:doaj.org-article:57fe6ad3515b457c841b93644728432e2021-12-02T18:02:46ZPhysical constraints and functional plasticity of cellulases10.1038/s41467-021-24075-y2041-1723https://doaj.org/article/57fe6ad3515b457c841b93644728432e2021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24075-yhttps://doaj.org/toc/2041-1723Enzyme 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.Jeppe KariGustavo A. MolinaKay S. SchallerCorinna Schiano-di-ColaStefan J. ChristensenSilke F. BadinoTrine H. SørensenNanna S. RøjelMalene B. KellerNanna Rolsted SørensenBartlomiej KolaczkowskiJohan P. OlsenKristian B. R. M. KroghKenneth JensenAna M. CavaleiroGünther H. J. PetersNikolaj SpodsbergKim BorchPeter WesthNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021) |
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DOAJ |
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DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q 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 |
| 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. |
| format |
article |
| 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 |
| 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 Portfolio |
| publishDate |
2021 |
| url |
https://doaj.org/article/57fe6ad3515b457c841b93644728432e |
| work_keys_str_mv |
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| _version_ |
1718378867807223808 |