title: Purification of 6-pyruvoyl-tetrahydropterin synthase from human liver.
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.
mesh_terms: D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D019761:Phosphorus-Oxygen Lyases
chemical_list: D000429:Alcohol Oxidoreductases; D019761:Phosphorus-Oxygen Lyases; C043497:6-pyruvoyltetrahydropterin synthase