Flavonoid glucuronides are substrates for human liver beta-glucuronidase

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TY  - JOUR
  - O'Leary, KA,Day, AJ,Needs, PW,Sly, WS,O'Brien, NM,Williamson, G
  - 2001
  - January
  - Febs Letters
  - Flavonoid glucuronides are substrates for human liver beta-glucuronidase
  - Validated
  - ()
  - human beta-glucuronidase flavonoid glucuronide quercetin turnover SMALL-INTESTINE QUERCETIN RATS EXPRESSION STORAGE BIOLOGY PLASMA KIDNEY ONION
  - 503
  - 103
  - 106
  - Quercetin glucuronides are the main circulating metabolites of quercetin in humans. We hypothesise that the potential availability of the aglycone within tissues depends on the substrate specificity of the deconjugating enzyme beta -glucuronidase towards circulating flavonoid glucuronides. Human tissues (small intestine, liver and neutrophils) exhibited beta -glucuronidase against quercetin glucuronides. The various quercetin glucuronides were deconjugated at similar rates, but liver cell-free extracts were the most efficient and the activity was completely inhibited by saccharo-1,4-lactone (a beta -glueuronidase inhibitor). Furthermore, pure recombinant human beta -glucuronidase hydrolysed various flavonoid glucuronides, with a 20-fold variation in catalytic efficiency (k(cat)/K-m = 1.3 x 10(3) M-1 s(-1) for equol-7-O-glucuronide and 26 x 10(3) M-1 s(-1) for kaempferol-O-glucuronide). Similar catalytic efficiencies were obtained for quercetin O-glucuronides substituted at different positions. These results show that flavonoid glucuronides can be deconjugated by microsomal beta -glucuronidase from various human cells. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
DA  - 2001/01
ER  - 
@article{V43338570,
   = {O'Leary,  KA and Day,  AJ and Needs,  PW and Sly,  WS and O'Brien,  NM and Williamson,  G },
   = {2001},
   = {January},
   = {Febs Letters},
   = {Flavonoid glucuronides are substrates for human liver beta-glucuronidase},
   = {Validated},
   = {()},
   = {human beta-glucuronidase flavonoid glucuronide quercetin turnover SMALL-INTESTINE QUERCETIN RATS EXPRESSION STORAGE BIOLOGY PLASMA KIDNEY ONION},
   = {503},
  pages = {103--106},
   = {{Quercetin glucuronides are the main circulating metabolites of quercetin in humans. We hypothesise that the potential availability of the aglycone within tissues depends on the substrate specificity of the deconjugating enzyme beta -glucuronidase towards circulating flavonoid glucuronides. Human tissues (small intestine, liver and neutrophils) exhibited beta -glucuronidase against quercetin glucuronides. The various quercetin glucuronides were deconjugated at similar rates, but liver cell-free extracts were the most efficient and the activity was completely inhibited by saccharo-1,4-lactone (a beta -glueuronidase inhibitor). Furthermore, pure recombinant human beta -glucuronidase hydrolysed various flavonoid glucuronides, with a 20-fold variation in catalytic efficiency (k(cat)/K-m = 1.3 x 10(3) M-1 s(-1) for equol-7-O-glucuronide and 26 x 10(3) M-1 s(-1) for kaempferol-O-glucuronide). Similar catalytic efficiencies were obtained for quercetin O-glucuronides substituted at different positions. These results show that flavonoid glucuronides can be deconjugated by microsomal beta -glucuronidase from various human cells. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.}},
  source = {IRIS}
}
AUTHORSO'Leary, KA,Day, AJ,Needs, PW,Sly, WS,O'Brien, NM,Williamson, G
YEAR2001
MONTHJanuary
JOURNAL_CODEFebs Letters
TITLEFlavonoid glucuronides are substrates for human liver beta-glucuronidase
STATUSValidated
TIMES_CITED()
SEARCH_KEYWORDhuman beta-glucuronidase flavonoid glucuronide quercetin turnover SMALL-INTESTINE QUERCETIN RATS EXPRESSION STORAGE BIOLOGY PLASMA KIDNEY ONION
VOLUME503
ISSUE
START_PAGE103
END_PAGE106
ABSTRACTQuercetin glucuronides are the main circulating metabolites of quercetin in humans. We hypothesise that the potential availability of the aglycone within tissues depends on the substrate specificity of the deconjugating enzyme beta -glucuronidase towards circulating flavonoid glucuronides. Human tissues (small intestine, liver and neutrophils) exhibited beta -glucuronidase against quercetin glucuronides. The various quercetin glucuronides were deconjugated at similar rates, but liver cell-free extracts were the most efficient and the activity was completely inhibited by saccharo-1,4-lactone (a beta -glueuronidase inhibitor). Furthermore, pure recombinant human beta -glucuronidase hydrolysed various flavonoid glucuronides, with a 20-fold variation in catalytic efficiency (k(cat)/K-m = 1.3 x 10(3) M-1 s(-1) for equol-7-O-glucuronide and 26 x 10(3) M-1 s(-1) for kaempferol-O-glucuronide). Similar catalytic efficiencies were obtained for quercetin O-glucuronides substituted at different positions. These results show that flavonoid glucuronides can be deconjugated by microsomal beta -glucuronidase from various human cells. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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