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Publication : Mouse sepiapterin reductase: an enzyme involved in the final step of tetrahydrobiopterin biosynthesis. Primary structure deduced from the cDNA sequence.

First Author  Ota A Year  1995
Journal  Biochim Biophys Acta Volume  1260
Issue  3 Pages  320-2
PubMed ID  7873607 Mgi Jnum  J:23125
Mgi Id  MGI:70912 Doi  10.1016/0167-4781(94)00225-r
Citation  Ota A, et al. (1995) Mouse sepiapterin reductase: an enzyme involved in the final step of tetrahydrobiopterin biosynthesis. Primary structure deduced from the cDNA sequence. Biochim Biophys Acta 1260(3):320-2
abstractText  We carried out the cloning of a mouse cDNA encoding a sepiapterin reductase which is involved in the final step of tetrahydrobiopterin biosynthesis as a first step toward gene-targeting technique in mice. The sequence contained 1245 nucleotides consisting of an open reading frame of 783 nucleotides encoding a protein of 261 amino acid residues whose molecular weight was 27,851, a 5'-untranslated region of 21 nucleotides and a 3'-untranslated region of 441 nucleotides containing poly(A) tail. The amino acid sequence of mouse sepiapterin reductase revealed the identity of 88% with rat and 74% with human sequence.
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