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Enzymatic characterization of beta-d-galactoside alpha-2- 3 sialytransferase from porcine sub-maxillary gland

Academic Article
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Overview

authors

  • Rearick, J. I.
  • Sadler, J. E.
  • Paulson, James
  • Hill, R. L.

publication date

  • 1979

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The substrate requirements, linkage specificity, and kinetic mechanism of a pure sialyltransferase from porcine submaxillary glands have been examined. The enzyme transfers sialic acid from the donor nucleotide, CMP-NeuAc, into the sequence NeuAcalpha2 leads to 3Galbeta1 leads to 3GalNAc, which is found in both glycoproteins and gangliosides. It forms only the alpha2 leads to 3 linkage with the disaccharide Gal/beta1 leads to 3GalNAc or antifreeze glycoprotein, which, along with asialoglycoproteins containing the sequence Gal/beta1 leads to 3GalNAcalpha1 leads to O-Thr/Ser, are the best acceptor substrates. Low molecular weight galactosides linked beta1 leads to 3 to glycose residues other than N-acetylgalactosamine are poor acceptors with relatively high Km values, while those in beta1 leads to 4 or beta1 leads to 6 linkages have both high Km and low Vmax. With glycoprotein and ganglioside acceptors this substrate specificity appears to be even more strict, with the sequence Gal/beta1 leads to 3GalNAc serving as the exclusive acceptor. Thus the present enzyme is not responsible either for the sequence, NeuAcalpha2 leads to 3Galbeta1 leads to 4GlcNAc, found in the asparagine-linked chains of certain glycoproteins, or for the synthesis of hematoside, NeuAcalpha2 leads to 3Galbeta1 leads to 4Glcbeta1 leads to 1Cer. Initial rate kinetic studies, with and without inhibitors, suggest that the transferase has an equilibrium random order mechanism.

subject areas

  • Animals
  • Galactosides
  • Kinetics
  • Molecular Conformation
  • Oligosaccharides
  • Sialyltransferases
  • Submandibular Gland
  • Substrate Specificity
  • Swine
  • Transferases
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 438198
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Additional Document Info

start page

  • 4444

end page

  • 4451

volume

  • 254

issue

  • 11

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