CNRS - AIX MARSEILLE UNIV: UMR7257

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Glycogenomics

Head Bernard HENRISSAT

Latest Publications

  1. Integrative visual omics of the white-rot fungus Polyporus brumalis exposes the biotechnological potential of its oxidative enzymes for delignifying raw plant biomass. (2018) Miyauchi S, Rancon A, Drula E, Hage H, Chaduli D, Favel A, Grisel S, Henrissat B, Herpoel-Gimbert I, Ruiz-Duenas FJ, Chevret D, Hainaut M, Lin J, Wang M, Pangilinan J, Lipzen A, Lesage-Meessen L, Navarro D, Riley R, Grigoriev IV, Zhou S, Raouche S, Rosso MN. Biotechnol Biofuels 11 201 PMID:30061923
  2. Production of alpha-1,3-L-arabinofuranosidase active on substituted xylan does not improve compost degradation by Agaricus bisporus. (2018) Vos AM, Jurak E, de Gijsel P, Ohm RA, Henrissat B, Lugones LG, Kabel MA, Wosten HAB. PLoS One 13 e0201090 PMID:30040824
  3. Genome Sequencing and analyses of Two Marine Fungi from the North Sea Unraveled a Plethora of Novel Biosynthetic Gene Clusters. (2018) Kumar A, Sorensen JL, Hansen FT, Arvas M, Syed MF, Hassan L, Benz JP, Record E, Henrissat B, Poggeler S, Kempken F. Sci Rep 8 10187 PMID:29976990
  4. Talaromyces borbonicus, sp. nov., a novel fungus from biodegraded Arundo donax with potential abilities in lignocellulose conversion. (2018) Varriale S, Houbraken J, Granchi Z, Pepe O, Cerullo G, Ventorino V, Chin-A-Woeng T, Meijer M, Riley R, Grigoriev IV, Henrissat B, de Vries RP, Faraco V. Mycologia 110 316-324 PMID:29843575
  5. Broad genomic sampling reveals a smut pathogenic ancestry of the fungal clade Ustilaginomycotina. (2018) Kijpornyongpan T, Mondo SJ, Barry K, Sandor L, Lee J, Lipzen A, Pangilinan J, LaButti K, Hainaut M, Henrissat B, Grigoriev IV, Spatafora JW, Aime MC. Mol Biol Evol 35 1840-1854 PMID:29771364
  6. Ancient acquisition of "alginate utilization loci" by human gut microbiota. (2018) Mathieu S, Touvrey-Loiodice M, Poulet L, Drouillard S, Vincentelli R, Henrissat B, Skjak-Braek G, Helbert W. Sci Rep 8 8075 PMID:29795267
...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


Elodie DRULA
Marie-Line GARRON
Bernard HENRISSAT
Pascal LAPEBIE
Vincent LOMBARD
Pedro MALDONADO COUTINHO
Nicolas TERRAPON

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