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Head Bernard HENRISSAT

Latest Publications

  1. Poplar carbohydrate-active enzymes - whole genome annotation and functional analyses based on RNA expression data. (2019) Kumar V, Hainaut M, Delhomme N, Mannapperuma C, Immerzeel P, Street NR, Henrissat B, Mellerowicz EJ. Plant J in press PMID:31111606
  2. Bacteroidetes use thousands of enzyme combinations to break down glycans. (2019) Lapebie P, Lombard V, Drula E, Terrapon N, Henrissat B. Nat Commun 10 2043 PMID:31053724
  3. Sucrose 6(F)-phosphate phosphorylase: a novel insight in the human gut microbiome. (2019) Tauzin AS, Bruel L, Laville E, Nicoletti C, Navarro D, Henrissat B, Perrier J, Potocki-Veronese G, Giardina T, Lafond M. Microb Genom 5(4) PMID:30913025
  4. AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes. (2019) Filiatrault-Chastel C, Navarro D, Haon M, Grisel S, Herpoel-Gimbert I, Chevret D, Fanuel M, Henrissat B, Heiss-Blanquet S, Margeot A, Berrin JG. Biotechnol Biofuels 12 55 PMID:30923563
  5. Transcriptomic atlas of mushroom development reveals conserved genes behind complex multicellularity in fungi. (2019) Krizsan K, Almasi E, Merenyi Z, Sahu N, Viragh M, Koszo T, Mondo S, Kiss B, Balint B, Kues U, Barry K, Cseklye J, Hegedus B, Henrissat B, Johnson J, Lipzen A, Ohm RA, Nagy I, Pangilinan J, Yan J, Xiong Y, Grigoriev IV, Hibbett DS, Nagy LG. Proc Natl Acad Sci U S A 116 7409-7418 PMID:30902897
  6. Broad-specificity GH131 beta-glucanases are a hallmark of Fungi and Oomycetes that colonise plants. (2019) Anasontzis GE, Lebrun MH, Haon M, Champion C, Kohler A, Lenfant N, Martin F, O'Connell RJ, Riley R, Grigoriev IV, Henrissat B, Berrin JG, Rosso MN. Environ Microbiol in press PMID:30887618
...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 (, 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

Alexandre ALBANI
Elodie DRULA
Marie-Line GARRON

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