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  • Title: Microsomal UDP-glucuronyltransferase-catalyzed bilirubin diglucuronide formation in human liver.
    Author: Peters WH, Jansen PL.
    Journal: J Hepatol; 1986; 2(2):182-94. PubMed ID: 3082969.
    Abstract:
    Human liver microsomal bilirubin UDP-glucuronyltransferase catalyzes formation of bilirubin mono- and diglucuronide. KmUDPGA and Vmax of the enzyme are 0.6 mM and 1.69 nmol/mg protein X min. In vitro, bilirubin readily dissolves in the microsomal lipid phase. Taking this into account a Kmbilirubin of 60.6 microM was found, which is much higher than the in vivo microsomal UCB concentration of human liver (2.9-11.4 microM). The total capacity of human liver to form bilirubin mono- and diglucuronide in vitro exceeds the in vivo mono- and diglucuronide production rates by a factor 8 to 10. Radiation-inactivation studies reveal that human liver microsomal bilirubin UDP-glucuronyltransferase is a tetrameric enzyme with a molecular mass of 209 000 +/- 20 000 Da. The complete tetrameric enzyme catalyzes both glucuronidation steps, formation of bilirubin monoglucuronide and conversion of mono- to diglucuronide. In its monomeric form, the enzyme with molecular mass of 55 000 +/- 1 500 Da catalyzes only the first step of bilirubin glucuronidation, the formation of bilirubin monoglucuronide.
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