Literature DB >> 10220293

Biotransformation of glycyrrhizin to 18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide by Streptococcus LJ-22, a human intestinal bacterium.

D H Kim1, S W Lee, M J Han.   

Abstract

By human intestinal bacteria, glycyrrhizin (18beta-glycyrrhetinic acid-3-O-[beta-D-glucuronopyranosyl-(1-->2)-betaD-glucuro nopyranoside], GL) was metabolized to 18beta-glycyrrhetinic acid (GA): the main pathway metabolized GL to GA by glucuronidases of Bacteroides J-37 and Eubacterium sp. GLH and the minor pathway metabolized GL to 18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide (GAMG) by beta-glucuronidase of Streptococcus LJ-22. Beta-Glucuronidase from Streptococcus LJ-22 hydrolyzed GL to GAMG (not GA). The molecular weight and optimal pH of the enzyme were 240 kDa and 5-6.

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Year:  1999        PMID: 10220293     DOI: 10.1248/bpb.22.320

Source DB:  PubMed          Journal:  Biol Pharm Bull        ISSN: 0918-6158            Impact factor:   2.233


  13 in total

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9.  Identification of isoliquiritigenin as an activator that stimulates the enzymatic production of glycyrrhetinic acid monoglucuronide.

Authors:  Xiaoxue Wang; Dong Wang; Yixin Huo; Dazhang Dai; Chihua Li; Chun Li; Guiyan Liu
Journal:  Sci Rep       Date:  2017-10-02       Impact factor: 4.379

10.  Biocatalytic properties of a novel crude glycyrrhizin hydrolase from the liver of the domestic duck.

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Journal:  J Mol Catal B Enzym       Date:  2006-08-30
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