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Eur J Biochem. 1986 Dec 1;161(2):295-302.

Biosynthesis of tetrahydrobiopterin. Purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from human liver.


6-Pyruvoyl-tetrahydropterin synthase, which catalyzes the first step in the conversion of 7,8-dihydroneopterin triphosphate to tetrahydrobiopterin, was purified approximately 140,000-fold to apparent homogeneity from human liver. The molecular mass of the enzyme is estimated to be 83 kDa. 7,8-Dihydroneopterin triphosphate was a substrate of the enzyme in the presence of Mg2+, and the pH optimum of the reaction was 7.5 in Tris HCl buffer. The Km value for 7,8-dihydroneopterin triphosphate was 10 microM. The product of this enzymatic reaction was the presumed intermediate 6-pyruvoyl-tetrahydropterin. This latter compound was converted to tetrahydrobiopterin in the presence of NADPH and partially purified sepiapterin reductase from human liver. The conditions and the effect of N-acetylserotonin on this reaction, and on the formation of the intermediates 6-(1'-hydroxy-2'-oxopropyl)-tetrahydropterin and 6-(1' oxo-2'-hydroxypropyl)-tetrahydropterin have been studied.

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