User:Magali Remaud-Simeon

  800x600     Normal  0      21      false  false  false    FR  X-NONE  X-NONE                                 MicrosoftInternetExplorer4

Magali Remaud-Simeon graduated from the National Institute of Applied Science of Toulouse in 1985 and received her PhD in 1988. Then she was as Post-Doctotal Fellow at the University of Pensylvania where she worked with Prof D. Graves in the department of Chemical and Biomolecular Engineering. From 1990 to 2000, she was an associate professor at the Institute of Technology of the University of Toulouse in the department of Applied Biology. She joined the group of Biocatalysis of Prof. P. MONSAN at the "laboratoire d'Ingénierie des systèmes et des procédés" in 1994. Since 2001, she is a professor at the National Institute of Applied Science of Toulouse. As the head of the Enzyme Molecular Engineering and Catalysis group since 2001, she focuses her research activities on enzyme engineering for white biotechnology, green chemistry, Food/Feed industries and synthetic biology. Her areas of interest cover enzyme structure/activity relationship studies, kinetic resolution, evolution combining both rational and combinatorial approaches, and applications to the synthesis of new polysaccharides, oligosaccharides, glycoonjugates, esters and enantiopure compounds. She has been working on glucansucrases from GH family 70 and 13 since 1985. With her collaborators, she has investigated the mechanism of dextran, alternan and amylose biosynthesis by dextransucrase, alternansucrase and amylosucrase, respectively. Her work is currently focused on the search and generation of enzymes displaying new specificities and improved properties towards unnatural substrates.

E-mail: magali.remaud@insa-toulouse.fr http://www.lisbp.insa-toulouse.fr

Glucansucrases from GH 70 Family

         Normal  0      21      false  false  false    FR  X-NONE  X-NONE

André I, Potocki-Véronèse G, Morel S, Monsan P, Remaud-Siméon M. 2010. Sucrose-acting transglucosidases for biocatalysis. Top. Curr. Chem. carbohydrates in sustainable development II. Eds Rauter AP, Vogel P, Queneau Y. Vol. 294, pp 25-48 PMID:21626747

Normal 0 21 false false false FR X-NONE X-NONE

Fabre E, Bozonnet S, Arcache A, Willemot RM, Vignon M, Monsan P, Remaud-Simeon, M. Role of the two catalytic domains of DSR-E dextransucrase and their involvement in the formation of highly alpha-1,2 branched dextran. J Bacteriol 2005 Jan; 187(1) 296-303. doi: 10.1128/JB.187.1.296-303.2005 PMID:15601714

Normal 0 21 false false false FR X-NONE X-NONE

Moulis C, Joucla G, Harrison D, Fabre E, Potocki-Veronese G, Monsan P, Remaud-Simeon M. Understanding the polymerization mechanism of glycoside-hydrolase family 70 glucansucrases. J Biol. Chem 2006 Oct 20; 281 (42) 31254-31267. DOI: 10.1074/jbc.M604850200 PMID:16864576

Brison Y, Pijning T, Malbert Y, Fabre E, Morel S, Potocki-Veronese G, Monsan P, Tranier S, Remaud-Simeon M, Dijkstra BW. Functional and Structural Characterization of alpha-(1 -> 2) Branching Sucrase Derived from DSR-E Glucansucrase. J Biol Chem 2012 March 9; 287(11) 7915-7924. doi: 10.1074/jbc.M111.305078 PMID:22262856

Glucansucrases from GH13 Family

         Normal  0      21      false  false  false    FR  X-NONE  X-NONE

Guérin F, Barbe S., Pizzut-Serin S, Potocki-Véronèse G, Guieysse D, Guillet V, Monsan P, Mourey L, Remaud-Simeon M, André I and Tranier S.. Structural investigation of the thermostability and product specificity of amylosucrase from the bacterium Deinococcus geothermalis. J. Biol Chem 2012; 287(9):6642-6654

Champion E, André I, Moulis C, Boutet J, Descroix K, Morel S, Monsan P, Mulard LA, Remaud-Simeon M. 2009a. Design of alpha-transglucosidases of controlled specificity for programmed chemoenzymatic synthesis of antigenic oligosaccharides. J Am Chem Soc 2009; 131(21):7379-89

Albenne C, Skov LK, Mirza O, Gajhede M, Feller G, D’Amico S, Andre G, Potocki-Véronèse G, Van Der Veen B, Monsan P, Remaud-Simeon M. Molecular basis of the amylose-like polymer formation catalysed by Neisseria polysaccharea amylosucrase. J Biol Chem 2004; 279, 726-734.

       Normal  0      21      false  false  false    FR  X-NONE  X-NONE