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Efficient chemoenzymatic synthesis of O-linked sialyl oligosaccharides. 2002

Ola Blixt, and Kirk Allin, and Laura Pereira, and Arun Datta, and James C Paulson
The Scripps Research Institute, Department of Molecular Biology, MEM-L71, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.

The tumor associated Tn (GalNAcalpha(1-1)-Thr/Ser)- and T (Galbeta(1-3)-GalNAcalpha(1-1)Thr/Ser)-antigens and their sialylated derivatives are present on the surface of many cancer cells. Preparative synthesis of these sialylated T- and Tn-structures has been achieved mainly from a chemical synthetic approach due to the lack of the required glycosyltransferases. We demonstrate a flexible and efficient chemoenzymatic approach for using recombinant sialyltransferases including a chicken GalNAcalpha2,6-sialyltransferase (chST6GalNAc I) and a porcine Galbeta(1-3)GalNAcalpha-2,3-sialyltransferase (pST3Gal I). Using these enzymes, the common O-linked sialosides Neu5Acalpha(2-6)GalNAcalpha(1-1)Thr, Galbeta(1-3)[Neu5Acalpha(2-6)]GalNAcalpha(1-1)Thr, Neu5Acalpha(2-3)Galbeta(1-3)GalNAcalpha(1-1)Thr, and Neu5Acalpha(2-3)Galbeta(1-3)[Neu5Acalpha(2-6)]GalNAcalpha(1-1)Thr were readily prepared at preparative scale. The chST6GalNAc I was found to require at least one amino acid (Thr/Ser) for optimal activity, and is thus an ideal catalyst for synthesis of synthetic glycopeptides and glycoconjugates with O-linked glycans.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009077 Mucins High molecular weight mucoproteins that protect the surface of EPITHELIAL CELLS by providing a barrier to particulate matter and microorganisms. Membrane-anchored mucins may have additional roles concerned with protein interactions at the cell surface. Mucin
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002240 Carbohydrate Sequence The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS. Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D000094663 beta-Galactoside alpha-2,3-Sialyltransferase Sialyltransferases that catalyze the transfer of N-ACETYLNEURAMINIC ACID from CYTIDINE MONOPHOSPHATE N-ACETYLNEURAMINIC ACID to the 3-OH of the GALACTOSE residue of N-GLYCANS. Asialofetuin Sialyltransferase,CMP N-Acetylneuraminate-beta-Galactoside alpha-2,3-Sialyltransferase,CMP-ANGS-Transferase,CMP-Acetylneuraminate-Galactoside (alpha 2-3)-Sialyltransferase,CMP-Neu5Ac-GAl beta1-3GalNAc alpha-2,3-Sialyltransferase,CMP-Neu5Ac-Gal1-3GalNAc alpha-2,3-Sialyltransferase,CMP-NeuAc-Galactoside (alpha 2-3)-Sialyltransferase,CMPSialic Acid beta-Galactosyl-1-3-N-Acetylgalactosaminide alpha 2-3-Sialyltransferase,Gal beta1,3GalNAc alpha2,3-Sialyltransferase,alpha 2-3-Sialyltransferase,beta-D-Galactoside 3-alpha-Sialyltransferase,ST3Gal I,ST3Gal II,ST3Gal III,ST3Gal IV,ST3Gal VI,alpha-2,3-ST(O),2-3-Sialyltransferase, alpha,3-alpha-Sialyltransferase, beta-D-Galactoside,CMP ANGS Transferase,CMP N Acetylneuraminate beta Galactoside alpha 2,3 Sialyltransferase,CMP Neu5Ac GAl beta1 3GalNAc alpha 2,3 Sialyltransferase,CMP Neu5Ac Gal1 3GalNAc alpha 2,3 Sialyltransferase,CMPSialic Acid beta Galactosyl 1 3 N Acetylgalactosaminide alpha 2 3 Sialyltransferase,N-Acetylneuraminate-beta-Galactoside alpha-2,3-Sialyltransferase, CMP,Sialyltransferase, Asialofetuin,alpha 2 3 Sialyltransferase,alpha-2,3-Sialyltransferase, CMP N-Acetylneuraminate-beta-Galactoside,alpha-2,3-Sialyltransferase, CMP-Neu5Ac-GAl beta1-3GalNAc,alpha-2,3-Sialyltransferase, CMP-Neu5Ac-Gal1-3GalNAc,alpha-2,3-Sialyltransferase, beta-Galactoside,beta D Galactoside 3 alpha Sialyltransferase,beta Galactoside alpha 2,3 Sialyltransferase,beta1-3GalNAc alpha-2,3-Sialyltransferase, CMP-Neu5Ac-GAl
D000094802 beta-D-Galactoside alpha 2-6-Sialyltransferase Sialyltransferases that catalyze the transfer of N-ACETYLNEURAMINIC ACID from CYTIDINE MONOPHOSPHATE N-ACETYLNEURAMINIC ACID to the 6-OH of the GALACTOSE residue of N-GLYCANS. CMP-Acetylneuraminate Galactoside (alpha 2-6)-Sialyltransferase,CMP-N-Acetylneuraminate-Galactosylglycoprotein Sialyltransferase ST6GAL,CMP-N-Acetylneuraminate-beta-Galactoside alpha-2,6-Sialyltransferase,CMP-N-Acetylneuraminic Acid-Lactose Sialytransferase,CMP-NeuAc-Galactoside (alpha 2-6)-Sialyltransferase,CMP-Sialic Acid-N-Acetyllactosaminide alpha (2-6)-Sialyltransferase,Gal-1-4-GlcNAc alpha(2-6)-Sialyltransferase,alpha 2-6-Sialyltransferase,alpha2,6(N) Sialyltransferase,alpha6-Sialyltransferase,beta-D-Galactoside alpha-2-6-Sialyltransferase,beta-Galactoside alpha2,6-Sialyltransferase,beta-Galactosyl(1-4)N-Acetylglucosaminide alpha(2-6)-Sialyltransferase,Gal-GlcNAc(2-6)-sialyltransferase,SIAT-1,ST6(N),ST6Gal I,ST6Gal-1,2-6-Sialyltransferase, alpha,2-6-Sialyltransferase, beta-D-Galactoside alpha,Acid-Lactose Sialytransferase, CMP-N-Acetylneuraminic,CMP N Acetylneuraminate Galactosylglycoprotein Sialyltransferase ST6GAL,CMP N Acetylneuraminate beta Galactoside alpha 2,6 Sialyltransferase,CMP N Acetylneuraminic Acid Lactose Sialytransferase,SIAT 1,ST6GAL, CMP-N-Acetylneuraminate-Galactosylglycoprotein Sialyltransferase,ST6Gal 1,Sialyltransferase ST6GAL, CMP-N-Acetylneuraminate-Galactosylglycoprotein,Sialytransferase, CMP-N-Acetylneuraminic Acid-Lactose,alpha 2 6 Sialyltransferase,alpha 2-6-Sialyltransferase, beta-D-Galactoside,alpha-2,6-Sialyltransferase, CMP-N-Acetylneuraminate-beta-Galactoside,alpha-2-6-Sialyltransferase, beta-D-Galactoside,alpha2,6-Sialyltransferase, beta-Galactoside,alpha6 Sialyltransferase,beta D Galactoside alpha 2 6 Sialyltransferase,beta Galactoside alpha2,6 Sialyltransferase
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012799 Sialyltransferases A group of enzymes with the general activity CMP-N-acetylneuraminate:acceptor N-acetylneuraminyl transferase. They catalyze the transfer of N-ACETYLNEURAMINIC ACID from CMP-N-ACETYLNEURAMINIC ACID to an acceptor, which is usually the terminal sugar residue of an oligosaccharide, a glycoprotein, or a glycolipid. Glycoprotein Sialyltransferases,Glycosyltransferase Family 29,Sialyltransferase,Ectosialyltransferase,Glycoprotein Sialyltransferase,Sialyltransferase, Glycoprotein,Sialyltransferases, Glycoprotein
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities

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