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. 1985 Feb 28;127(1):213-9.
doi: 10.1016/s0006-291x(85)80146-7.

Purification and properties of the phosphate eliminating enzyme involved in the biosynthesis of BH4 in man

D Heintel, W Leimbacher, U Redweik, B Zagalak, H C Curtius

Purification and properties of the phosphate eliminating enzyme involved in the biosynthesis of BH4 in man

D Heintel et al. Biochem Biophys Res Commun. .

Abstract

An enzyme catalyzing the elimination of triphosphate from 7,8-dihydroneopterin triphosphate in the presence of Mg2+ has been purified approx. 3000 fold from human liver. It has a molecular weight of approx. 63'000, a pI value of 4.4 - 4.6 and is stable at 80 degrees C for 5 min. This enzyme catalyzes the formation of tetrahydrobiopterin in the presence of sepiapterin reductase, Mg2+ and NADPH. It is thus possible, that it also catalyzes the internal oxidoreduction leading to formation of the intermediate 6-pyruvoyl-tetrahydropterin, suggesting that no further enzyme is obligatory for biosynthesis of tetrahydrobiopterin.

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