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The Hindsgaul group has reported the first inhibitor of α1,3-GalT which is an acceptor oligosaccharide analogue, see: Helland. A. C.; Hindsgaul, O.; Palcic, M. M.; Stults, C. L. M.; Macher, B. A. Carbohydr. Res. 1995, 276, 91-98.
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0345630662
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note
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This type of "two-step double-displacement transfer mechanism" has been proposed by Lowary and Hindsgaul for other α-glycosyltransferases, see: ref 2b.
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Takayama, S.; Chung, S. J.; Igarashi, Y.; Ichikawa, Y.; Sepp, A.; Lechler, R. I.; Wu, J.; Hayashi, T.; Siuzdak, G.; Wong, C.-H. Bioorg. Med. Chem., in press.
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0345630661
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note
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In the present study we used a recombinant porcine α-1,3-galacto-syltransferase obtained from Calbiochem (San Diego, CA). The inhibition assay was carried out as described in ref 12, except for the use of pH 7.0 and LacNAc as the acceptor.
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28
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0345630659
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note
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Synthesis of compounds 1, 4, 5, and 6 is described in Supporting Information.
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29
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0345630658
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note
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When a 5′-thio derivative of uridine was subjected to the coupling reaction with a tosyl derivative of the threiol, only a small amount of the coupling product was obtained, probably because of the competing intramolecular cyclization of the thio moiety to the uracil group.
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33
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33947478635
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0344768124
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note
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i of 13 μM, see: ref 12.
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36
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0345198682
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John Wiley & Sons: New York, Chapter 4. See also Supporting Information
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Segel, I. H. Enzyme Kinetics; John Wiley & Sons: New York, 1973; Chapter 4. See also Supporting Information.
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Enzyme Kinetics
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Segel, I.H.1
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