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
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