CNRS - AIX MARSEILLE UNIV: UMR7257

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Glycogenomics

Head Bernard HENRISSAT

Latest Publications

  1. De novo assembly of the complex genome of Nippostrongylus brasiliensis using MinION long reads. (2018) Eccles D, Chandler J, Camberis M, Henrissat B, Koren S, Le Gros G, Ewbank JJ. BMC Biol 16 6 PMID:29325570
  2. Identification of Euglena gracilis beta-1,3-glucan phosphorylase and establishment of a new glycoside hydrolase (GH) family GH149. (2018) Kuhaudomlarp S, Patron NJ, Henrissat B, Rejzek M, Saalbach G, Field RA. J Biol Chem in press PMID:29317507
  3. Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi as versatile saprotrophs and plant mutualists. (2018) Martino E, Morin E, Grelet GA, Kuo A, Kohler A, Daghino S, Barry KW, Cichocki N, Clum A, Dockter RB, Hainaut M, Kuo RC, LaButti K, Lindahl BD, Lindquist EA, Lipzen A, Khouja HR, Magnuson J, Murat C, Ohm RA, Singer SW, Spatafora JW, Wang M, Veneault-Fourrey C, Henrissat B, Grigoriev IV, Martin FM, Perotto S. New Phytol in press PMID:29315638
  4. Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides. (2018) Luis AS, Briggs J, Zhang X, Farnell B, Ndeh D, Labourel A, Basle A, Cartmell A, Terrapon N, Stott K, Lowe EC, McLean R, Shearer K, Schuckel J, Venditto I, Ralet MC, Henrissat B, Martens EC, Mosimann SC, Abbott DW, Gilbert HJ. Nat Microbiol in press PMID:29255254
  5. Novel carbohydrate binding modules in the surface anchored a-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut. (2018) Cockburn DW, Suh C, Medina KP, Duvall RM, Wawrzak Z, Henrissat B, Koropatkin NM. Mol Microbiol 107 249-264 PMID:29139580
  6. PULDB: the expanded database of Polysaccharide Utilization Loci. (2018) Terrapon N, Lombard V, Drula E, Lapebie P, Al-Masaudi S, Gilbert HJ, Henrissat B. Nucleic Acids Res 46 D677-D683 PMID:29088389
...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 Maldonado COUTINHO
Elodie DRULA
Marie-Line GARRON
Bernard HENRISSAT
Pascal LAPEBIE
Vincent LOMBARD
Nicolas TERRAPON

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