| First Author | Soars MG | Year | 2001 |
| Journal | Arch Biochem Biophys | Volume | 391 |
| Issue | 2 | Pages | 218-24 |
| PubMed ID | 11437353 | Mgi Jnum | J:70500 |
| Mgi Id | MGI:2137465 | Doi | 10.1006/abbi.2001.2383 |
| Citation | Soars MG, et al. (2001) Cloning and characterization of a canine UDP-glucuronosyltransferase. Arch Biochem Biophys 391(2):218-24 |
| abstractText | UDP-glucuronosyltransferases (UGTs) are a major family of enzymes catalyzing the transfer of glucuronic acid to a range of endogenous compounds and xenobiotics facilitating their elimination in either urine or bile. Although the dog is commonly used in drug metabolism studies, relatively little is known about the expression and activity of UGTs in this species. This report describes the molecular cloning and functional characterization of the first dog UGT, UGT1A6. The cloned protein is composed of 528 amino acids with the variable region demonstrating a 67-72% identity with the variable regions of mouse, rat, and human UGT1A6. The enzyme expressed stably in V79 cells predominantly catalyzed the glucuronidation of simple, planar phenols (e.g., for 1-naphthol, K(m) = 41 microM, V(max) = 0.07 nmol/min/mg protein), a class of compounds extensively glucuronidated by human UGT1A6. Based on sequence homology and common catalytic activity, this dog UGT1A protein appears to be the canine orthologue of human UGT1A6. Copyright 2001 Academic Press. |
