Biosynthesis of tetrahydrobiopterin : purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from human liver

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1986
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Takikawa, Shin-Ichiro
Curtius, Hans-Christoph
Redweik, Udo
Leimbacher, Walter
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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 μM. 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-acetyserotonin 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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ISO 690TAKIKAWA, Shin-Ichiro, Hans-Christoph CURTIUS, Udo REDWEIK, Walter LEIMBACHER, Sandro GHISLA, 1986. Biosynthesis of tetrahydrobiopterin : purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from human liver. In: European Journal of Biochemistry. 1986, 161(2), pp. 295-302. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1986.tb10446.x
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@article{Takikawa1986Biosy-7740,
  year={1986},
  doi={10.1111/j.1432-1033.1986.tb10446.x},
  title={Biosynthesis of tetrahydrobiopterin : purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from human liver},
  number={2},
  volume={161},
  issn={0014-2956},
  journal={European Journal of Biochemistry},
  pages={295--302},
  author={Takikawa, Shin-Ichiro and Curtius, Hans-Christoph and Redweik, Udo and Leimbacher, Walter and Ghisla, Sandro}
}
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