. Lyon, France ? Electronic Supplementary Information (ESI) available: Copies of 1 H NMR spectra

J. Du, M. A. Meledeo, Z. Wang, H. S. Khanna, V. D. Paruchuri et al., Metabolic glycoengineering: Sialic acid and beyond, Glycobiology, vol.19, issue.12, pp.1382-1401, 2009.
DOI : 10.1093/glycob/cwp115
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2770326

Z. Wang, J. Du, P. L. Che, M. A. Meledeo, and K. J. Yarema, Hexosamine analogs: from metabolic glycoengineering to drug discovery, Current Opinion in Chemical Biology, vol.13, issue.5-6, pp.565-572, 2009.
DOI : 10.1016/j.cbpa.2009.08.001

H. C. Hang, C. Yu, D. L. Kato, and C. R. Bertozzi, A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation, Proceedings of the National Academy of Sciences, vol.100, issue.25, pp.14846-14851, 2003.
DOI : 10.1073/pnas.2335201100

S. T. Laughlin and C. R. Bertozzi, Glycans, ACS Chemical Biology, vol.4, issue.12, pp.1068-1072, 2009.
DOI : 10.1021/cb900254y

S. T. Laughlin and C. R. Bertozzi, Metabolic labeling of glycans with azido sugars and subsequent glycan-profiling and visualization via Staudinger ligation, Nature Protocols, vol.5, issue.11, pp.2930-2944, 2007.
DOI : 10.1038/nprot.2007.422

L. Descheny, M. E. Gainers, B. Walcheck, and C. J. Dimitroff, Ameliorating Skin-Homing Receptors on Malignant T Cells with a Fluorosugar Analog of N-acetylglucosamine: P-Selectin Ligand Is a More Sensitive Target than E-Selectin Ligand, Journal of Investigative Dermatology, vol.126, issue.9, pp.2065-2073, 2006.
DOI : 10.1038/sj.jid.5700364

Z. Guo and Q. Wang, Recent development in carbohydrate-based cancer vaccines, Current Opinion in Chemical Biology, vol.13, issue.5-6, pp.608-617, 2009.
DOI : 10.1016/j.cbpa.2009.08.010

F. Maley, A. L. Tarentino, J. F. Mcgarrahan, and R. Delgiacco, -acetyl-d-galactosamine in rat liver, Biochemical Journal, vol.107, issue.5, pp.637-644, 1968.
DOI : 10.1042/bj1070637
URL : https://hal.archives-ouvertes.fr/in2p3-00003573

D. P. Gamblin, E. M. Scanlan, and B. G. Davis, Glycoprotein Synthesis: An Update, Chemical Reviews, vol.109, issue.1, pp.131-163, 2009.
DOI : 10.1021/cr078291i

V. Bourgeaux, F. Piller, and V. Piller, Two-step enzymatic synthesis of UDP-N-acetylgalactosamine, Bioorganic & Medicinal Chemistry Letters, vol.15, issue.24, pp.5459-5462, 2005.
DOI : 10.1016/j.bmcl.2005.08.088
URL : https://hal.archives-ouvertes.fr/hal-00088511

P. Busca and O. R. Martin, Synthesis of UDP-GalNAc analogues as probes for the study of polypeptide-??-GalNAc-transferases. Part 2, Tetrahedron Letters, vol.45, issue.23, pp.4433-4436, 2004.
DOI : 10.1016/j.tetlet.2004.04.074

I. Pastuszak, R. Drake, and A. D. Elbein, Kidney N-Acetylgalactosamine (GalNAc)-1-phosphate Kinase, a New Pathway of GalNAc Activation, Journal of Biological Chemistry, vol.271, issue.34, pp.20776-20782, 1996.
DOI : 10.1074/jbc.271.34.20776

J. B. Thoden and H. M. Holden, The Molecular Architecture of Human N-Acetylgalactosamine Kinase, Journal of Biological Chemistry, vol.280, issue.38, pp.32784-32791, 2005.
DOI : 10.1074/jbc.M505730200

M. Nishimoto and M. Kitaoka, Identification of N-Acetylhexosamine 1-Kinase in the Complete Lacto-N-Biose I/Galacto-N-Biose Metabolic Pathway in Bifidobacterium longum, Applied and Environmental Microbiology, vol.73, issue.20, pp.6444-6449, 2007.
DOI : 10.1128/AEM.01425-07

L. Cai, W. Guan, W. Wang, W. Zhao, M. Kitaoka et al., Substrate specificity of N-acetylhexosamine kinase towards N-acetylgalactosamine derivatives, Bioorganic & Medicinal Chemistry Letters, vol.19, issue.18, pp.5433-5435, 2009.
DOI : 10.1016/j.bmcl.2009.07.104

P. D. Kingsley, K. G. Hagen, K. M. Maltby, J. Zara, and L. A. Tabak, Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase family member mRNAs during mouse development, Glycobiology, vol.10, issue.12, pp.1317-1323, 2000.
DOI : 10.1093/glycob/10.12.1317

P. Busca, V. Piller, F. Piller, and O. R. Martin, Synthesis and biological evaluation of new UDP-GalNAc analogues for the study of polypeptide-??-GalNAc-transferases, Bioorganic & Medicinal Chemistry Letters, vol.13, issue.11, pp.1853-1856, 2003.
DOI : 10.1016/S0960-894X(03)00287-7

H. C. Hang, C. Yu, M. R. Pratt, and C. R. Bertozzi, Probing Glycosyltransferase Activities with the Staudinger Ligation, Journal of the American Chemical Society, vol.126, issue.1, pp.6-7, 2004.
DOI : 10.1021/ja037692m

K. G. Ten-hagen, T. A. Fritz, and L. A. Tabak, All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases, Glycobiology, vol.13, issue.1, pp.1-16, 2003.
DOI : 10.1093/glycob/cwg007

T. A. Fritz, J. H. Hurley, L. B. Trinh, J. Shiloach, and L. A. Tabak, The beginnings of mucin biosynthesis: The crystal structure of UDP-GalNAc:polypeptide ??-N-acetylgalactosaminyltransferase-T1, Proceedings of the National Academy of Sciences, vol.101, issue.43, pp.15307-15312, 2004.
DOI : 10.1073/pnas.0405657101

F. K. Hagen, B. Hazes, R. Raffo, D. Desa, and L. A. Tabak, Structure-Function Analysis of the UDP-N-acetyl-D-galactosamine:PolypeptideN-acetylgalactosaminyltransferase: ESSENTIAL RESIDUES LIE IN A PREDICTED ACTIVE SITE CLEFT RESEMBLING A LACTOSE REPRESSOR FOLD, Journal of Biological Chemistry, vol.274, issue.10, pp.6797-6803, 1999.
DOI : 10.1074/jbc.274.10.6797

V. Bourgeaux, M. Cadene, F. Piller, and V. Piller, Efficient Enzymatic Glycosylation of Peptides and Oligosaccharides from GalNAc and UTP, ChemBioChem, vol.1, issue.1, pp.37-40, 2007.
DOI : 10.1002/cbic.200600369
URL : https://hal.archives-ouvertes.fr/hal-00158348

O. T. Keppler, P. Stehling, M. Herrmann, H. Kayser, D. Grunow et al., Biosynthetic Modulation of Sialic Acid-dependent Virus-Receptor Interactions of Two Primate Polyoma Viruses, Journal of Biological Chemistry, vol.270, issue.3, pp.1308-1314, 1995.
DOI : 10.1074/jbc.270.3.1308

H. Ohfwlq, *. , G. , %. Ffpgp0duv@, and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