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

Biochim Biophys Acta. 1995 Feb 21;1260(3):320-2. doi: 10.1016/0167-4781(94)00225-r.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / chemistry
  • Alcohol Oxidoreductases / genetics*
  • Alcohol Oxidoreductases / metabolism
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Biopterins / analogs & derivatives*
  • Biopterins / biosynthesis
  • DNA, Complementary
  • Humans
  • Mice
  • Molecular Sequence Data
  • Rats
  • Sequence Homology, Amino Acid

Substances

  • DNA, Complementary
  • Biopterins
  • Alcohol Oxidoreductases
  • sepiapterin reductase
  • sapropterin

Associated data

  • GENBANK/S77493