Two Proteins, Mn^<2+>, and Low Molecular Cofactor Are Required for C-Glucosyl-Cleavage of Mangiferin

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Abstract

<i>C</i>-Glucosides, in which sugars are attached to the aglycone by carbon–carbon bonds, are generally resistant to acid and enzyme hydrolysis. The <i>C</i>-glucosyl bond of mangiferin, a xanthone <i>C</i>-glucoside, was cleaved by anaerobic incubation with a human intestinal bacterium, <i>Bacteroides</i> sp. MANG, to give norathyriol. A cell-free extract obtained by sonication of <i>B.</i> sp. MANG demonstrated cleaving activity for mangiferin to norathyriol by adding NADH, diaphorase, and dithiothreitol. Both high molecular weight (>10 k) and low molecular weight (<10 k) fractions obtained from the cell-free extract were required for the activity. MnCl<sub>2</sub> was necessary for the activity, but other metal ions were not. By purification of the high molecular weight fraction using DEAE-cellulose and Phenyl Sepharose column chromatography, two fractions, designated as proteins A and B, were separated and required for the activity. Neither protein A nor protein B alone showed any activity. This is the first report describing a <i>C</i>-glucosyl-cleaving enzyme from human intestinal bacterium that seems to involve a novel enzyme mechanism.

Journal

  • Biological and Pharmaceutical Bulletin

    Biological and Pharmaceutical Bulletin 28(11), 2035-2039, 2005-11-01

    The Pharmaceutical Society of Japan

References:  24

Cited by:  1

Codes

  • NII Article ID (NAID)
    110003666392
  • NII NACSIS-CAT ID (NCID)
    AA10885497
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    09186158
  • NDL Article ID
    7675394
  • NDL Source Classification
    ZS51(科学技術--薬学)
  • NDL Call No.
    Z53-V41
  • Data Source
    CJP  CJPref  NDL  NII-ELS  J-STAGE 
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