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  • Title: Purification of 6-pyruvoyl-tetrahydropterin synthase from human liver.
    Author: Takikawa S, Curtius HC, Redweik U, Ghisla S.
    Journal: Biochem Biophys Res Commun; 1986 Jan 29; 134(2):646-51. PubMed ID: 3511907.
    Abstract:
    The enzyme which catalyzes the first step in the conversion of dihydroneopterin triphosphate to tetrahydrobiopterin has been purified approx. 40,000-fold from human liver to apparent homogeneity. The enzyme has a native molecular weight of approximately 83,000 and consists of four identical subunits, each of which has a molecular weight of approximately 19,000. It contains carbohydrates and is remarkably stable to heat treatment. In the presence of purified sepiapterin reductase, Mg2+, and NADPH, this enzyme catalyzes efficiently the formation of tetrahydrobiopterin from dihydroneopterin triphosphate. This indicates that these two proteins are sufficient for the overall conversion.
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