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Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface
Efficient depolymerization of crystalline cellulose requires cooperation between multiple cellulolytic enzymes. Through biochemical approaches, molecular dynamics (MD) simulation, and single-molecule observations using high-speed atomic force microscopy (HS-AFM), we quantify and track synergistic ac...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Association for the Advancement of Science
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9788756/ https://www.ncbi.nlm.nih.gov/pubmed/36563138 http://dx.doi.org/10.1126/sciadv.ade5155 |
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author | Uchiyama, Taku Uchihashi, Takayuki Ishida, Takuya Nakamura, Akihiko Vermaas, Josh V. Crowley, Michael F. Samejima, Masahiro Beckham, Gregg T. Igarashi, Kiyohiko |
author_facet | Uchiyama, Taku Uchihashi, Takayuki Ishida, Takuya Nakamura, Akihiko Vermaas, Josh V. Crowley, Michael F. Samejima, Masahiro Beckham, Gregg T. Igarashi, Kiyohiko |
author_sort | Uchiyama, Taku |
collection | PubMed |
description | Efficient depolymerization of crystalline cellulose requires cooperation between multiple cellulolytic enzymes. Through biochemical approaches, molecular dynamics (MD) simulation, and single-molecule observations using high-speed atomic force microscopy (HS-AFM), we quantify and track synergistic activity for cellobiohydrolases (CBHs) with a lytic polysaccharide monooxygenase (LPMO) from Phanerochaete chrysosporium. Increasing concentrations of LPMO (AA9D) increased the activity of a glycoside hydrolase family 6 CBH, Cel6A, whereas the activity of a family 7 CBH (Cel7D) was enhanced only at lower concentrations of AA9D. MD simulation suggests that the result of AA9D action to produce chain breaks in crystalline cellulose can oxidatively disturb the crystalline surface by disrupting hydrogen bonds. HS-AFM observations showed that AA9D increased the number of Cel7D molecules moving on the substrate surface and increased the processivity of Cel7D, thereby increasing the depolymerization performance, suggesting that AA9D not only generates chain ends but also amorphizes the crystalline surface, thereby increasing the activity of CBHs. |
format | Online Article Text |
id | pubmed-9788756 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-97887562022-12-29 Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface Uchiyama, Taku Uchihashi, Takayuki Ishida, Takuya Nakamura, Akihiko Vermaas, Josh V. Crowley, Michael F. Samejima, Masahiro Beckham, Gregg T. Igarashi, Kiyohiko Sci Adv Physical and Materials Sciences Efficient depolymerization of crystalline cellulose requires cooperation between multiple cellulolytic enzymes. Through biochemical approaches, molecular dynamics (MD) simulation, and single-molecule observations using high-speed atomic force microscopy (HS-AFM), we quantify and track synergistic activity for cellobiohydrolases (CBHs) with a lytic polysaccharide monooxygenase (LPMO) from Phanerochaete chrysosporium. Increasing concentrations of LPMO (AA9D) increased the activity of a glycoside hydrolase family 6 CBH, Cel6A, whereas the activity of a family 7 CBH (Cel7D) was enhanced only at lower concentrations of AA9D. MD simulation suggests that the result of AA9D action to produce chain breaks in crystalline cellulose can oxidatively disturb the crystalline surface by disrupting hydrogen bonds. HS-AFM observations showed that AA9D increased the number of Cel7D molecules moving on the substrate surface and increased the processivity of Cel7D, thereby increasing the depolymerization performance, suggesting that AA9D not only generates chain ends but also amorphizes the crystalline surface, thereby increasing the activity of CBHs. American Association for the Advancement of Science 2022-12-23 /pmc/articles/PMC9788756/ /pubmed/36563138 http://dx.doi.org/10.1126/sciadv.ade5155 Text en Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Physical and Materials Sciences Uchiyama, Taku Uchihashi, Takayuki Ishida, Takuya Nakamura, Akihiko Vermaas, Josh V. Crowley, Michael F. Samejima, Masahiro Beckham, Gregg T. Igarashi, Kiyohiko Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface |
title | Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface |
title_full | Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface |
title_fullStr | Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface |
title_full_unstemmed | Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface |
title_short | Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface |
title_sort | lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface |
topic | Physical and Materials Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9788756/ https://www.ncbi.nlm.nih.gov/pubmed/36563138 http://dx.doi.org/10.1126/sciadv.ade5155 |
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