• Title of article

    Aglycon specificity profiling of α-glucosidases using synthetic probes

  • Author/Authors

    Wataru Hakamata، نويسنده , , Makoto Muroi، نويسنده , , Kazunari Kadokura، نويسنده , , Toshiyuki Nishio، نويسنده , , Tadatake Oku، نويسنده , , Atsuo Kimura، نويسنده , , Seiya Chiba، نويسنده , , Akira Takatsuki، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2005
  • Pages
    4
  • From page
    1489
  • To page
    1492
  • Abstract
    We designed and synthesized hydrogen bond based probes 1–8 with the exception of known glycosidase inhibition mechanisms, and aglycon specificity of 11 different sources of α-glucosidases were investigated using their probes. Probe 4 (2,6-anhydro-1-deoxy-1-[(1-oxopentyl-5-hydroxy)amino]-d-glycero-d-ido-heptitol) showed a potent inhibition of S. cerevisiae α-glucosidase among all α-glucosidases. Probe 4 was found to be a competitive inhibitor for S. cerevisiae α-glucosidase with Ki 0.13 mM.
  • Keywords
    ?-glucosidase , ER processing ?-glucosidase , inhibitor , Aglycon specificity
  • Journal title
    Bioorganic & Medicinal Chemistry Letters
  • Serial Year
    2005
  • Journal title
    Bioorganic & Medicinal Chemistry Letters
  • Record number

    795422