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Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
- Source :
- Biotechnology for Biofuels, Biotechnology for Biofuels, BioMed Central, 2013, 6 (41), pp.1-14. ⟨10.1186/1754-6834-6-41⟩, Biotechnology for Biofuels 41 (6), 1-14. (2013), Biotechnology for Biofuels, 2013, 6 (41), pp.1-14. ⟨10.1186/1754-6834-6-41⟩
- Publication Year :
- 2013
- Publisher :
- BioMed Central, 2013.
-
Abstract
- 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. 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). 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.
- Subjects :
- [SDV.BIO]Life Sciences [q-bio]/Biotechnology
Ligninolytic enzymes
lyase
Lytic polysaccharide monooxygenases
computer.software_genre
Applied Microbiology and Biotechnology
Genome
dégradation de la lignocellulose
chemistry.chemical_compound
enzyme lytique
lignocellulose
Lignin
glycoside hydrolase
Glycoside hydrolase
base de données
chemistry.chemical_classification
0303 health sciences
Database
biology
Repertoire
monooxygénase
enzyme de dégradation
analyse comparative
lignine
CAZy database
General Energy
Biochemistry
substrat
génome fongique
paroi cellulaire végétale
Biotechnology
estérase
CAZy
glycosyltransférase
Biotechnologies
enzyme lignolytique
Management, Monitoring, Policy and Law
analyse phylogénétique
Cell wall
03 medical and health sciences
Glycosyltransferase
Evolution of lignocellulose breakdown
030304 developmental biology
030306 microbiology
Renewable Energy, Sustainability and the Environment
Research
enzyme
Enzyme
chemistry
polysaccharide
biology.protein
glucide complexe
computer
Subjects
Details
- Language :
- English
- ISSN :
- 17546834
- Volume :
- 6
- Database :
- OpenAIRE
- Journal :
- Biotechnology for Biofuels
- Accession number :
- edsair.doi.dedup.....47c1ab766fd517775d4e8e985a2aee95