CNRS - AIX MARSEILLE UNIV: UMR7257

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Glycogenomics

Head Bernard HENRISSAT

Latest Publications

  1. A bioinformatics analysis of 3400 lytic polysaccharide oxidases from family AA9. (2017) Lenfant N, Hainaut M, Terrapon N, Drula E, Lombard V, Henrissat B. Carbohydr Res in press PMID:28434716
  2. A Metagenomics Investigation of Carbohydrate-Active Enzymes along the Gastrointestinal Tract of Saudi Sheep. (2017) Al-Masaudi S, El Kaoutari A, Drula E, Al-Mehdar H, Redwan EM, Lombard V, Henrissat B. Front Microbiol 8 666 PMID:28473812
  3. Unusual active site location and catalytic apparatus in a glycoside hydrolase family. (2017) Munoz-Munoz J, Cartmell A, Terrapon N, Henrissat B, Gilbert HJ. Proc Natl Acad Sci U S A 114 4936-4941 PMID:28396425
  4. Archaea: essential inhabitants of the human digestive microbiota (2017) Demonfort-Nkamga V, Henrissat B, Drancourt M. Human Microbiome Journal 3 1-8 PMID:0
  5. Exploring the genomic diversity of black yeasts and relatives (Chaetothyriales, Ascomycota). (2017) Teixeira MM, Moreno LF, Stielow BJ, Muszewska A, Hainaut M, Gonzaga L, Abouelleil A, Patane JS, Priest M, Souza R, Young S, Ferreira KS, Zeng Q, da Cunha MM, Gladki A, Barker B, Vicente VA, de Souza EM, Almeida S, Henrissat B, Vasconcelos AT, Deng S, Voglmayr H, Moussa TA, Gorbushina A, Felipe MS, Cuomo CA, de Hoog GS. Stud Mycol 86 1-28 PMID:28348446
  6. Complex pectin metabolism by gut bacteria reveals novel catalytic functions. (2017) Ndeh D, Rogowski A, Cartmell A, Luis AS, Basle A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neill MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, Gilbert HJ. Nature 544 65-70 PMID:28329766
...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
Matthieu HAINAUT
Bernard HENRISSAT
UNK
Denise HENRISSAT
Pascal LAPEBIE
Vincent LOMBARD
Pedro MALDONADO COUTINHO
Rajender KUMAR
Nicolas TERRAPON

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