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Uridine diphosphate glucuronyltransferase

Mulder GJ, Scholtens E. 1977. Phenol sulphotransferase and uridine diphosphate glucuronyltransferase from rat liver in vivo and in vitro. Biochem J 165 553-559. [Pg.220]

A12. Attwood, D., Graham, A. B., and Wood, G. C., The phospholipid-dependence of uridine diphosphate glucuronyltransferase. Reactivation of phospholipase-inactivated enzyme by phospholipids and detergents. Biochem. J. 123, 875-882... [Pg.278]

HIO. Heirw h, K. P. M., Van De Vijver, M., and Fevery, J., Assay and properties of digitonin-activated bilirubin uridine diphosphate glucuronyltransferase from rat liver. Biochem. J. 129, 605-618 (1972). [Pg.283]

M15. Mulder, G. J., The heterogeneity of uridine diphosphate glucuronyltransferase from rat liver. Biockem. J. 125, 9-15 (1971). [Pg.286]

V4. Vessey, D. A., and Zakim, D., Regulation of microsomal enzymes by phospholipids. II. Activation of hepatic uridine diphosphate-glucuronyltransferase. J. Biol. Chem. 246, 4649-4656 (1971). [Pg.288]

Phenytoin also induces CYP3A4 and uridine diphosphate-glucuronyltransferases (UTPs increased glucuronidation). [Pg.774]

Altered sexual differentiation of hepatic uridine diphosphate glucuronyltransferase by neonatal hormone treatment in rats. Biochemistry J. 180 313, 1979. [Pg.524]

Figure 9-8. Pathway for metabolism of heme and excretion as bilirubin. Heme degradation begins with heme oxygenase, which catalyzes a complex set of reactions that simultaneously open the protoporphyrin ring structure and release iron in the ferric (Fe ) state. This is the only physiologic reaction that makes endogenous CO in the body a portion of the small amounts made is expired via the lungs. The structure of the main form of bilirubin is shown. Symbols for the side groups indicate M, methyl V, vinyl P, propyl. Formation of the diglucuronide is catalyzed by bilirubin uridine diphosphate (UDP) glucuronyltransferase. RE, reticuloendothelial. Figure 9-8. Pathway for metabolism of heme and excretion as bilirubin. Heme degradation begins with heme oxygenase, which catalyzes a complex set of reactions that simultaneously open the protoporphyrin ring structure and release iron in the ferric (Fe ) state. This is the only physiologic reaction that makes endogenous CO in the body a portion of the small amounts made is expired via the lungs. The structure of the main form of bilirubin is shown. Symbols for the side groups indicate M, methyl V, vinyl P, propyl. Formation of the diglucuronide is catalyzed by bilirubin uridine diphosphate (UDP) glucuronyltransferase. RE, reticuloendothelial.
A. Glucuronidation UDP-glucuronyltransferases (EC 2.4.1.17) The reaction may occur spontaneously with some substrates Phenols, alcohols carboxylic acids amines, amides, sulphonamides, thiols RXH + uridinediphospho-j8-D-glucuronic acid RX-glucoronide + uridine-5 -diphosphate where X is O, N or S (and more rarely C) to give 0-, N- and S-glucuronides. [Pg.52]


See other pages where Uridine diphosphate glucuronyltransferase is mentioned: [Pg.480]    [Pg.405]    [Pg.278]    [Pg.282]    [Pg.283]    [Pg.71]    [Pg.71]    [Pg.73]    [Pg.164]    [Pg.480]    [Pg.405]    [Pg.278]    [Pg.282]    [Pg.283]    [Pg.71]    [Pg.71]    [Pg.73]    [Pg.164]    [Pg.14]    [Pg.236]    [Pg.37]    [Pg.236]    [Pg.1195]    [Pg.88]    [Pg.581]   
See also in sourсe #XX -- [ Pg.405 ]




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