Characterization of 2,3-and 2,6-sialyltransferases from Helicobacter acinonychis

  1. Get@NRC: Characterization of 2,3-and 2,6-sialyltransferases from Helicobacter acinonychis (Opens in a new window)
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Journal titleGlycobiology
Pages9971006; # of pages: 10
Subjectalpha 2,3 sialyltransferase; alpha 2,6 sialyltransferase; galactose; sialyltransferase; unclassified drug; aminosugar; bacterial protein; beta D galactoside alpha 2 6 sialyltransferase; beta galactoside alpha 2,3 sialyltransferase; beta-D-galactoside alpha 2-6-sialyltransferase; beta-galactoside alpha-2,3-sialyltransferase; hybrid protein; magnesium; manganese; n acetyllactosamine; N-acetyllactosamine; sialic acid derivative; sialyltransferase; article; bacterial genome; bacterium isolate; cheetah; controlled study; enzyme activation; enzyme analysis; enzyme substrate; Escherichia coli; gene expression; gene sequence; Helicobacter; Helicobacter acinonychis; molecular cloning; nonhuman; nucleotide sequence; priority journal; protein expression; sequence homology; tandem repeat; biosynthesis; chemical structure; chemistry; conformation; enzyme active site; enzyme specificity; enzymology; genetics; glycosylation; pH; structural homology; Escherichia coli; Helicobacter; Helicobacter acinonychis; Amino Sugars; Bacterial Proteins; Carbohydrate Conformation; Catalytic Domain; Cloning, Molecular; Glycosylation; Helicobacter; Hydrogen-Ion Concentration; Magnesium; Manganese; Models, Molecular; Recombinant Fusion Proteins; Sialic Acids; Sialyltransferases; Structural Homology, Protein; Substrate Specificity
AbstractGenome 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 2,3-sialyltransferase, whereas HAC1268 is a mono-functional α2,6- sialyltransferase and is the first member of GT-42 to show α2,6- sialyltransferase activity. © 2012 The Author.
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AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences (IBS-ISB)
Peer reviewedYes
NPARC number21269286
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Record identifiercc4e5c5d-dbaa-4045-88e7-abd3b5b11f35
Record created2013-12-12
Record modified2016-05-09
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