| First Author | Johansson M | Year | 2003 |
| Journal | Biochem Biophys Res Commun | Volume | 307 |
| Issue | 1 | Pages | 41-6 |
| PubMed ID | 12849978 | Mgi Jnum | J:113937 |
| Mgi Id | MGI:3687889 | Doi | 10.1016/s0006-291x(03)01062-3 |
| Citation | Johansson M (2003) Identification of a novel human uridine phosphorylase. Biochem Biophys Res Commun 307(1):41-6 |
| abstractText | Uridine phosphorylase catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The enzyme has an important role in the metabolism of pyrimidine analogs used in cancer chemotherapy. The cDNA of a novel 317 amino acid human uridine phosphorylase approximately 60% identical to the previously identified human uridine phosphorylase was cloned. The novel enzyme, named uridine phosphorylase-2 (UPase-2), showed broad substrate specificity and accepted uridine, deoxyuridine, and thymidine as well as the two pyrimidine nucleoside analogs 5-fluorouridine and 5-fluoro-2(')-deoxyuridine. The human UPase-2 gene was mapped to chromosome 2q24.1 and the 2.2-kb mRNA was predominantly expressed in kidney. The mouse UPase-2 cDNA was also identified and shown to be predominantly expressed in liver. The identification of a novel uridine phosphorylase with broad substrate specificity is important for studies on both nucleoside metabolism as well as for studies on the pharmacological mechanisms of therapeutic pyrimidine nucleoside analogs. |
