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Characterization of α2,3- and α2,6-sialyltransferases from Helicobacter acinonychis. 2012

Melissa J Schur, and Emilie Lameignere, and Natalie C J Strynadka, and Warren W Wakarchuk
National Research Council Canada, Institute for Biological Sciences, Ottawa, ON, Canada.

Genome sequence data were used to clone and express two sialyltransferase enzymes of the GT-42 family from Helicobacter acinonychis ATCC 51104, a gastric disease isolate from Cheetahs. The deposited genome sequence for these genes contains a large number of tandem repeat sequences in each of them: HAC1267 (RQKELE)(15) and HAC1268 (EEKLLEFKNI)(13). We obtained two clones with different numbers of repeat sequences for the HAC1267 gene homolog and a single clone for the HAC1268 gene homolog. Both genes could be expressed in Escherichia coli and sialyltransferase activity was measured using synthetic acceptor substrates containing a variety of terminal sugars. Both enzymes were shown to have a preference for N-acetyllactosamine, and they each made a product with a different linkage to the terminal galactose. HAC1267 is a mono-functional α2,3-sialyltransferase, whereas HAC1268 is a mono-functional α2,6-sialyltransferase and is the first member of GT-42 to show α2,6-sialyltransferase activity.

UI MeSH Term Description Entries
D008274 Magnesium A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
D008345 Manganese A trace element with atomic symbol Mn, atomic number 25, and atomic weight 54.94. It is concentrated in cell mitochondria, mostly in the pituitary gland, liver, pancreas, kidney, and bone, influences the synthesis of mucopolysaccharides, stimulates hepatic synthesis of cholesterol and fatty acids, and is a cofactor in many enzymes, including arginase and alkaline phosphatase in the liver. (From AMA Drug Evaluations Annual 1992, p2035)
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D002236 Carbohydrate Conformation The characteristic 3-dimensional shape of a carbohydrate. Carbohydrate Linkage,Carbohydrate Conformations,Carbohydrate Linkages,Conformation, Carbohydrate,Conformations, Carbohydrate,Linkage, Carbohydrate,Linkages, Carbohydrate
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D006031 Glycosylation The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). Protein Glycosylation,Glycosylation, Protein
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
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

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