Attention CAZymologists: Registration for CBM11 - The 11th Carbohydrate Bioengineering Meeting (Helsinki, 10-13 May 2015) - is now open!
CAZypedia maintains a history of the CBMs, including links to previous conference proceedings.
Also: Applications are now being accepted to attend the 2015 GRC on Cellulosomes, Cellulases & Other Carbohydrate Modifying Enzymes.
From 1998 to 2001, I did my PhD in the group of Christian Cambillau in Marseille working on the structure-function relationships of several mammalian odorant binding proteins (OBPs). In January 2002 I joined the group of Gideon Davies in the YSBL laboratory as a postdoctoral fellow to study various carbohydrate esterases and their role in bacterial cell wall formation and breakdown. We worked on family CE7 , CE9 , and also GH5  as well as other carbohydrate active enzymes like NagA  from Bacillus subtilis a N-acetylglucosamine-6-phophate deacetylase and NagB  a glucosamine-6-phosphate deaminase.
I returned to Marseille in 2004 to join the group of structural glycobiology directed by Yves Bourne at the AFMB laboratory in CNRS. Since then I’ve been interested in a GH73; an isoprenoid binding module appended to a CBM2  and possibly involved in oxydoreduction events during plant cell wall breakdown; two putative carbohydrate binding domain appended to two global regulators  as well as several GT2 and GT4, all involved in biofilm formation in Pseudomonas aeruginosa.
- Vincent F, Charnock SJ, Verschueren KH, Turkenburg JP, Scott DJ, Offen WA, Roberts S, Pell G, Gilbert HJ, Davies GJ, and Brannigan JA. Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9A resolution. J Mol Biol. 2003 Jul 11;330(3):593-606.
- Taylor EJ, Gloster TM, Turkenburg JP, Vincent F, Brzozowski AM, Dupont C, Shareck F, Centeno MS, Prates JA, Puchart V, Ferreira LM, Fontes CM, Biely P, and Davies GJ. Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases. J Biol Chem. 2006 Apr 21;281(16):10968-75. DOI:10.1074/jbc.M513066200 |
- Dias FM, Vincent F, Pell G, Prates JA, Centeno MS, Tailford LE, Ferreira LM, Fontes CM, Davies GJ, and Gilbert HJ. Insights into the molecular determinants of substrate specificity in glycoside hydrolase family 5 revealed by the crystal structure and kinetics of Cellvibrio mixtus mannosidase 5A. J Biol Chem. 2004 Jun 11;279(24):25517-26. DOI:10.1074/jbc.M401647200 |
- Vincent F, Yates D, Garman E, Davies GJ, and Brannigan JA. The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily. J Biol Chem. 2004 Jan 23;279(4):2809-16. DOI:10.1074/jbc.M310165200 |
- Vincent F, Davies GJ, and Brannigan JA. Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?. J Biol Chem. 2005 May 20;280(20):19649-55. DOI:10.1074/jbc.M502131200 |
- Vincent F, Molin DD, Weiner RM, Bourne Y, and Henrissat B. Structure of a polyisoprenoid binding domain from Saccharophagus degradans implicated in plant cell wall breakdown. FEBS Lett. 2010 Apr 16;584(8):1577-84. DOI:10.1016/j.febslet.2010.03.015 |
- Vincent F, Round A, Reynaud A, Bordi C, Filloux A, and Bourne Y. Distinct oligomeric forms of the Pseudomonas aeruginosa RetS sensor domain modulate accessibility to the ligand binding site. Environ Microbiol. 2010 Jun;12(6):1775-86. DOI:10.1111/j.1462-2920.2010.02264.x |