| First Author | Wu C | Year | 1996 |
| Journal | Mamm Genome | Volume | 7 |
| Issue | 5 | Pages | 349-52 |
| PubMed ID | 8661721 | Mgi Jnum | J:33171 |
| Mgi Id | MGI:80651 | Doi | 10.1007/s003359900101 |
| Citation | Wu C, et al. (1996) Mouse uroporphyrinogen decarboxylase: cDNA cloning, expression, and mapping. Mamm Genome 7(5):349-52 |
| abstractText | Uroporphyrinogen decarboxylase (URO-decarboxylase; EC 4.1.1.37), the heme biosynthetic enzyme responsible for the conversion of uroporphyrinogen III to coproporphyrinogen III, is the enzymatic defect in porphyria cutanea tarda, the most common porphyria. The mouse URO-decarboxylase cDNA was isolated from a mouse adult liver cDNA library. The longest clone of 1.5 kb, designated pmUROD-1, had 5' and 3' untranslated sequences of 281 and 97 bp, respectively, and an open reading frame of 1104 bp encoding a 367-amino acid polypeptide with a predicted molecular mass of 40,595 Da. The mouse and human coding sequences had 87.8% and 90.0% nucleotide and amino acid identity, respectively. The authenticity of the mouse cDNA was established by expression of the active enzyme in Escherichia coli. In addition, the analysis of two sets of multilocus genetic crosses localized the mouse gene, Urod, on Chromosome (Chr) 4, consistent with the map location of the human gene to a position of conserved synteny on Chr 1. The availability of the mouse URO-decarboxylase should facilitate studies of the structure and organization of the mouse genomic sequence and the development of a mouse model of this inherited porphyria. |
