O. Sullivan, C. Tompson, and F. W. , J. Chem. Soc, vol.57, pp.854-870, 1890.

D. E. Koshland, . Jr, and S. S. Stein, J. Biol. Chem, vol.208, pp.139-148, 1954.

A. Sturm, Invertases. Primary Structures, Functions, and Roles in Plant Development and Sucrose Partitioning, Plant Physiology, vol.121, issue.1, pp.1-8, 1999.
DOI : 10.1104/pp.121.1.1

A. Sturm and G. Q. Tang, The sucrose-cleaving enzymes of plants are crucial for development, growth and carbon partitioning, Trends in Plant Science, vol.4, issue.10, pp.401-407, 1999.
DOI : 10.1016/S1360-1385(99)01470-3

J. Xu, M. K. Bjursell, J. Himrod, S. Deng, L. K. Carmichael et al., A Genomic View of the Human-Bacteroides thetaiotaomicron Symbiosis, Science, vol.299, issue.5615, pp.2074-2076, 2003.
DOI : 10.1126/science.1080029

M. A. Schell, M. Karmirantzou, B. Snel, D. Vilanova, B. Berger et al., Proc. Natl. Acad. Sci. U. S. A. 99, pp.14422-14427, 2002.

B. Henrissat, A classification of glycosyl hydrolases based on amino acid sequence similarities, Biochemical Journal, vol.280, issue.2, pp.309-316, 1991.
DOI : 10.1042/bj2800309

URL : https://hal.archives-ouvertes.fr/hal-00310263

V. A. Reddy and F. Maley, J. Biol. Chem, vol.265, pp.10817-10820, 1990.

A. Reddy and F. Maley, Studies on Identifying the Catalytic Role of Glu-204 in the Active Site of Yeast Invertase, Journal of Biological Chemistry, vol.56, issue.24, pp.13953-13957, 1996.
DOI : 10.1016/0378-1119(89)90249-7

G. Davies and B. Henrissat, Structures and mechanisms of glycosyl hydrolases, Structure, vol.3, issue.9, pp.853-859, 1995.
DOI : 10.1016/S0969-2126(01)00220-9

URL : https://hal.archives-ouvertes.fr/hal-00310748

J. Gebler, N. R. Gilkes, M. Claeyssens, D. B. Wilson, P. Beguin et al., J. Biol. Chem, vol.267, pp.12559-12561, 1992.

B. Henrissat, I. Callebaut, S. Fabrega, P. Lehn, J. P. Mornon et al., Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases., Proceedings of the National Academy of Sciences, vol.92, issue.15, pp.7090-7094, 1995.
DOI : 10.1073/pnas.92.15.7090

URL : https://hal.archives-ouvertes.fr/hal-00310754

T. Pons, O. Olmea, G. Chinea, A. Beldarrain, G. Marquez et al., Structural model for family 32 of glycosyl-hydrolase enzymes, Proteins: Structure, Function, and Genetics, vol.4, issue.3, pp.383-395, 1998.
DOI : 10.1016/S0969-2126(96)00005-6

G. Meng and K. Futterer, Structural framework of fructosyl transfer in Bacillus subtilis levansucrase, Nature Structural & Molecular Biology, vol.47, issue.3, pp.935-941, 2003.
DOI : 10.1107/S0108767391001071

H. G. Beisel, S. Kawabata, S. Iwanaga, R. Huber, and W. Bode, Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus, The EMBO Journal, vol.18, issue.9, pp.2313-2322, 1999.
DOI : 10.1093/emboj/18.9.2313

D. Nurizzo, J. P. Turkenburg, S. J. Charnock, S. M. Roberts, E. J. Dodson et al., Cellvibrio japonicus ??-L-arabinanase 43A has a novel five-blade ??-propeller fold, Nature Structural Biology, vol.9, issue.9, pp.665-668, 2002.
DOI : 10.1038/nsb835

D. G. Naumoff, ?-Fructosidase superfamily: Homology with some ?-L-arabinases and ?-D-xylosidases, Proteins: Structure, Function, and Genetics, vol.174, issue.65, pp.66-76, 2001.
DOI : 10.1128/jb.174.10.3227-3235.1992

S. M. Pitson, A. G. Voragen, and G. Beldman, Stereochemical course of hydrolysis catalyzed by arabinofuranosyl hydrolases, FEBS Letters, vol.4, issue.1, pp.7-11, 1996.
DOI : 10.1016/0959-440X(94)90271-2

C. Braun, A. Meinke, L. Ziser, and S. G. Withers, Simultaneous High-Performance Liquid Chromatographic Determination of Both the Cleavage Pattern and the Stereochemical Outcome of the Hydrolysis Reactions Catalyzed by Various Glycosidases, Analytical Biochemistry, vol.212, issue.1, pp.259-262, 1993.
DOI : 10.1006/abio.1993.1320

H. Kersters-hilderson, M. Claeyssens, E. Van-doorslaer, and C. K. De-bruyne, Determination of the anomeric configuration of D -xylose with D -xylose isomerases, Carbohydrate Research, vol.47, issue.2, pp.269-273, 1976.
DOI : 10.1016/S0008-6215(00)84192-0

W. Liebl, D. Brem, and A. Gotschlich, Analysis of the gene for ??-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima , and characterisation of the enzyme expressed in Escherichia coli, Applied Microbiology and Biotechnology, vol.50, issue.1, pp.55-64, 1998.
DOI : 10.1007/s002530051256

, Gateway? Technology, a Universal Technology to Clone DNA Sequences for Functional Analysis and Expression in Multiple Systems, Invitrogen, 2002.

D. K. Kidby, D. , and D. J. , Anal. Biochem, vol.55, pp.312-325, 1973.

G. M. Sheldrick, Phase annealing in SHELX-90: direct methods for larger structures, Acta Crystallographica Section A Foundations of Crystallography, vol.46, issue.6, pp.467-473, 1990.
DOI : 10.1107/S0108767390000277

E. De-la-fortelle and G. Bricogne, [27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods, Methods Enzymol, vol.276, pp.472-494, 1997.
DOI : 10.1016/S0076-6879(97)76073-7

K. Cowtan and P. Main, Miscellaneous Algorithms for Density Modification, Acta Crystallographica Section D Biological Crystallography, vol.54, issue.4, pp.487-493, 1998.
DOI : 10.1107/S0907444997011980

T. C. Terwilliger, Acta Crystallogr. Sect. D Biol. Crystallogr, vol.58, 1937.

A. Roussel and C. Cambillau, Silicon Graphics Geometry Partners Directory Silicon Graphics, Mountain View, CA 29, Navaza, J. Acta Crystallogr. Sect. A, vol.88, issue.50, pp.157-163, 1991.

, Computational Collaborative Project Acta Crystallogr. Sect. D Biol. Crystallogr, vol.4, issue.50, pp.760-763, 1994.

H. S. Lee and A. Sturm, Purification and Characterization of Neutral and Alkaline Invertase from Carrot, Plant Physiology, vol.112, issue.4, pp.1513-1522, 1996.
DOI : 10.1104/pp.112.4.1513

Y. Li and T. Ferenci, , pp.1651-1657, 1996.

A. V. Reddy, R. Maccoll, and F. Maley, Effect of oligosaccharides and chloride on the oligomeric structures of external, internal, and deglycosylated invertase, Biochemistry, vol.29, issue.10, pp.2482-2487, 1990.
DOI : 10.1021/bi00462a007

W. P. Burmeister, R. W. Ruigrok, C. , and S. , EMBO J, vol.11, pp.49-56, 1992.

Z. Jawad and M. Paoli, Novel Sequences Propel Familiar Folds, Structure, vol.10, issue.4, pp.447-454, 2002.
DOI : 10.1016/S0969-2126(02)00750-5

S. Crennell, E. Garman, G. Laver, E. Vimr, T. et al., , pp.535-544, 1994.

P. Gunasekaran, T. Karunakaran, B. Cami, A. G. Mukundan, L. Preziosi et al., Cloning and sequencing of the sacA gene: characterization of a sucrase from Zymomonas mobilis., Journal of Bacteriology, vol.172, issue.12, pp.6727-6735, 1990.
DOI : 10.1128/jb.172.12.6727-6735.1990

S. W. Cho, S. Lee, and W. Shin, The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex, Journal of Molecular Biology, vol.311, issue.4, pp.863-878, 2001.
DOI : 10.1006/jmbi.2001.4919

G. Michel, L. Chantalat, E. Fanchon, B. Henrissat, B. Kloareg et al., Journal of Biological Chemistry, vol.321, issue.43, pp.40202-40209, 2001.
DOI : 10.1107/S0021889891004399

C. S. Rye and S. G. Withers, Glycosidase mechanisms, Current Opinion in Chemical Biology, vol.4, issue.5, pp.573-580, 2000.
DOI : 10.1016/S1367-5931(00)00135-6

A. Vasella, G. J. Davies, and M. Böhm, Glycosidase mechanisms, Current Opinion in Chemical Biology, vol.6, issue.5, pp.619-629, 2002.
DOI : 10.1016/S1367-5931(02)00380-0

L. Holm and C. Sander, Touring protein fold space with Dali/FSSP, Nucleic Acids Research, vol.26, issue.1, pp.316-319, 1998.
DOI : 10.1093/nar/26.1.316

URL : https://academic.oup.com/nar/article-pdf/26/1/316/7048683/26-1-316.pdf

L. A. Kelley, R. M. Maccallum, and M. J. Sternberg, J. Mol. Biol, vol.299, pp.499-520, 2000.

S. J. Ackerman, L. Liu, M. A. Kwatia, M. P. Savage, D. D. Leonidas et al., Charcot-Leyden Crystal Protein (Galectin-10) Is Not a Dual Function Galectin with Lysophospholipase Activity but Binds a Lysophospholipase Inhibitor in a Novel Structural Fashion, Journal of Biological Chemistry, vol.1439, issue.17, pp.14859-14868, 2002.
DOI : 10.1038/355472a0

A. Gaskell, S. Crennell, T. , and G. , The three domains of a bacterial sialidase: a ??-propeller, an immunoglobulin module and a galactose-binding jelly-roll, Structure, vol.3, issue.11, pp.1197-1205, 1995.
DOI : 10.1016/S0969-2126(01)00255-6

J. D. Thompson, T. J. Gibson, F. Plewniak, F. Jeanmougin, H. et al., The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools, Nucleic Acids Research, vol.25, issue.24, pp.4876-4882, 1997.
DOI : 10.1093/nar/25.24.4876

G. J. Barton, ALSCRIPT: a tool to format multiple sequence alignments, "Protein Engineering, Design and Selection", vol.6, issue.1, pp.37-40, 1993.
DOI : 10.1093/protein/6.1.37

G. J. Davies, K. S. Wilson, and B. Henrissat, Nomenclature for sugar-binding subsites in glycosyl hydrolases, Biochemical Journal, vol.321, issue.2, pp.557-559, 1997.
DOI : 10.1042/bj3210557

URL : https://hal.archives-ouvertes.fr/hal-00309901