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Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes

BACKGROUND: Since its inception, the carbohydrate-active enzymes database (CAZy; http://www.cazy.org) has described the families of enzymes that cleave or build complex carbohydrates, namely the glycoside hydrolases (GH), the polysaccharide lyases (PL), the carbohydrate esterases (CE), the glycosylt...

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Autores principales: Levasseur, Anthony, Drula, Elodie, Lombard, Vincent, Coutinho, Pedro M, Henrissat, Bernard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3620520/
https://www.ncbi.nlm.nih.gov/pubmed/23514094
http://dx.doi.org/10.1186/1754-6834-6-41
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author Levasseur, Anthony
Drula, Elodie
Lombard, Vincent
Coutinho, Pedro M
Henrissat, Bernard
author_facet Levasseur, Anthony
Drula, Elodie
Lombard, Vincent
Coutinho, Pedro M
Henrissat, Bernard
author_sort Levasseur, Anthony
collection PubMed
description BACKGROUND: Since its inception, the carbohydrate-active enzymes database (CAZy; http://www.cazy.org) has described the families of enzymes that cleave or build complex carbohydrates, namely the glycoside hydrolases (GH), the polysaccharide lyases (PL), the carbohydrate esterases (CE), the glycosyltransferases (GT) and their appended non-catalytic carbohydrate-binding modules (CBM). The recent discovery that members of families CBM33 and family GH61 are in fact lytic polysaccharide monooxygenases (LPMO), demands a reclassification of these families into a suitable category. RESULTS: Because lignin is invariably found together with polysaccharides in the plant cell wall and because lignin fragments are likely to act in concert with (LPMO), we have decided to join the families of lignin degradation enzymes to the LPMO families and launch a new CAZy class that we name “Auxiliary Activities” in order to accommodate a range of enzyme mechanisms and substrates related to lignocellulose conversion. Comparative analyses of these auxiliary activities in 41 fungal genomes reveal a pertinent division of several fungal groups and subgroups combining their phylogenetic origin and their nutritional mode (white vs. brown rot). CONCLUSIONS: The new class introduced in the CAZy database extends the traditional CAZy families, and provides a better coverage of the full extent of the lignocellulose breakdown machinery.
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spelling pubmed-36205202013-04-10 Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes Levasseur, Anthony Drula, Elodie Lombard, Vincent Coutinho, Pedro M Henrissat, Bernard Biotechnol Biofuels Research BACKGROUND: Since its inception, the carbohydrate-active enzymes database (CAZy; http://www.cazy.org) has described the families of enzymes that cleave or build complex carbohydrates, namely the glycoside hydrolases (GH), the polysaccharide lyases (PL), the carbohydrate esterases (CE), the glycosyltransferases (GT) and their appended non-catalytic carbohydrate-binding modules (CBM). The recent discovery that members of families CBM33 and family GH61 are in fact lytic polysaccharide monooxygenases (LPMO), demands a reclassification of these families into a suitable category. RESULTS: Because lignin is invariably found together with polysaccharides in the plant cell wall and because lignin fragments are likely to act in concert with (LPMO), we have decided to join the families of lignin degradation enzymes to the LPMO families and launch a new CAZy class that we name “Auxiliary Activities” in order to accommodate a range of enzyme mechanisms and substrates related to lignocellulose conversion. Comparative analyses of these auxiliary activities in 41 fungal genomes reveal a pertinent division of several fungal groups and subgroups combining their phylogenetic origin and their nutritional mode (white vs. brown rot). CONCLUSIONS: The new class introduced in the CAZy database extends the traditional CAZy families, and provides a better coverage of the full extent of the lignocellulose breakdown machinery. BioMed Central 2013-03-21 /pmc/articles/PMC3620520/ /pubmed/23514094 http://dx.doi.org/10.1186/1754-6834-6-41 Text en Copyright © 2013 Levasseur et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Levasseur, Anthony
Drula, Elodie
Lombard, Vincent
Coutinho, Pedro M
Henrissat, Bernard
Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
title Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
title_full Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
title_fullStr Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
title_full_unstemmed Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
title_short Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
title_sort expansion of the enzymatic repertoire of the cazy database to integrate auxiliary redox enzymes
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3620520/
https://www.ncbi.nlm.nih.gov/pubmed/23514094
http://dx.doi.org/10.1186/1754-6834-6-41
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