PT  - JOURNAL ARTICLE
AU  - M R Jackson
AU  - S Fournel-Gigleux
AU  - D Harding
AU  - B Burchell
TI  - Examination of the substrate specificity of cloned rat kidney phenol UDP-glucuronyltransferase expressed in COS-7 cells.
DP  - 1988 Nov 01
TA  - Molecular Pharmacology
PG  - 638--642
VI  - 34
IP  - 5
4099  - http://molpharm.aspetjournals.org/content/34/5/638.short
4100  - http://molpharm.aspetjournals.org/content/34/5/638.full
SO  - Mol Pharmacol1988 Nov 01; 34
AB  - A cDNA encoding a rat kidney UDP-glucuronyltransferase (UDPGT) was subcloned into the vector pKCRH2. Expression driven by the SV40 promoter produced enzymatically active UDPGT in COS-7 cells cultured in vitro. The appearance of enzyme activity was associated with an immunodetectable glycosylated UDPGT protein (Mr 53 kDa) in the cells. The expressed enzyme rapidly catalyzed the glucuronidation of 1-naphthol, 4-methylumbelliferone, and 4-nitrophenol. Studies using more than 20 compounds showed that the cloned UDPGT exhibited a restricted specificity towards planar phenols. A crude description of the molecular conformation of 4-alkylphenols accepted within the active site of the protein was obtained. The glucuronidation of morphine, thymol, menthol, testosterone, androsterone, or estrone was not catalyzed by this enzyme.