CNRS - AIX MARSEILLE UNIV: UMR7257

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Glycogenomics

Head Bernard HENRISSAT

Latest Publications

  1. A fungal family of lytic polysaccharide monooxygenase-like copper proteins. (2020) Labourel A, Frandsen KEH, Zhang F, Brouilly N, Grisel S, Haon M, Ciano L, Ropartz D, Fanuel M, Martin F, Navarro D, Rosso MN, Tandrup T, Bissaro B, Johansen KS, Zerva A, Walton PH, Henrissat B, Leggio LL, Berrin JG. Nat Chem Biol in press PMID:31932718
  2. At the nexus of three kingdoms: the genome of the mycorrhizal fungus Gigaspora margarita provides insights into plant, endobacterial and fungal interactions. (2020) Venice F, Ghignone S, Salvioli di Fossalunga A, Amselem J, Novero M, Xie X, SEdzielewska Toro K, Morin E, Lipzen A, Grigoriev IV, Henrissat B, Martin FM, Bonfante P. Environ Microbiol 22 122-141 PMID:31621176
  3. Fungal ecological strategies reflected in gene transcription - a case study of two litter decomposers. (2019) Barbi F, Kohler A, Barry K, Baskaran P, Daum C, Fauchery L, Ihrmark K, Kuo A, LaButti K, Lipzen A, Morin E, Grigoriev IV, Henrissat B, Lindahl B, Martin F. Environ Microbiol in press PMID:31760680
  4. Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action. (2019) Bule P, Chuzel L, Blagova E, Wu L, Gray MA, Henrissat B, Rapp E, Bertozzi CR, Taron CH, Davies GJ. Nat Commun 10 4816 PMID:31645552
  5. The functional and structural characterization of Trichoderma reesei dehydrogenase belonging to the PQQ dependent family of Carbohydrate-Active Enzymes Family AA12. (2019) Turbe-Doan A, Record E, Lombard V, Kumar R, Levasseur A, Henrissat B, Garron ML. Appl Environ Microbiol 85 e00964-19 PMID:31604773
  6. Comparative genomic analyses reveal diverse virulence factors and antimicrobial resistance mechanisms in clinical Elizabethkingia meningoseptica strains. (2019) Chen S, Soehnlen M, Blom J, Terrapon N, Henrissat B, Walker ED. PLoS One 14 e0222648 PMID:31600234
...All publications

Our team aims at establishing the relationships between the aminoacid sequence of carbohydrate-active enzymes and their precise specificity. This work find developments in various areas, from the exploration of the gut microbiota to the search of novel enzymes for biofuel production or for the conversion of blood groups.

Cazymes classification within CAZy

Carbohydrates are crucial for most organisms as carbon sources or as signaling molecules, but also for cell wall synthesis, host pathogen interactions, energy storage etc. We term carbohydrate-active enzymes (CAZymes) the enzymes that assemble and breakdown complex carbohydrates and carbohydrate polymers. Unlike most other classes of enzymes whose sequences carry limited informative power, the peculiarities of CAZymes and of their substrates turn these enzymes into extremely powerful probes to examine and explain the lifestyle of living organisms. During the last 20 years we have developed a classification in sequence-based families that correlate with the structure and catalytic mechanism of CAZymes. This classification currently includes 5 enzyme categories (glycoside hydrolases, glycosyltransferases, carbohydrate esterases, polysaccharide lyases and auxiliary activities) and their appended carbohydrate-binding modules. To make the classification available to the community, we have created the CAZy database (www.cazy.org), which has been meticulously curated and updated since its first version in 1998. Recently, we have coupled various bioinformatics tools to our database explore the CAZyme content of hundreds of eukaryotic and prokaryotic genomes, as well as many metagenomic datasets


Pedro M COUTINHO
Elodie DRULA
Marie-Line GARRON
Bernard HENRISSAT
Aurore LABOUREL
Vincent LOMBARD
Nicolas TERRAPON

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