Tetrahydrobiopterin biosynthesis : Studies with specifically labeled (2H)NAD(P)H and 2H2O and of the enzymes involved

Curtius, Hans-Christoph; Heintel, Dorothee; Ghisla, Sandro; Kuster, Thomas; Leimbacher, Walter; Niederwieser, Alois

Tetrahydrobiopterin biosynthesis : Studies with specifically labeled (2H)NAD(P)H and 2H2O and of the enzymes involved

Dateien

Eur_J_Biochem_1985_CurtiusTetrahydrobiopterin_biosynthesis._Stud.pdfGröße: 1.45 MBDownloads: 519

Datum

1985

Autor:innen

Curtius, Hans-Christoph

Heintel, Dorothee

Ghisla, Sandro

Kuster, Thomas

Leimbacher, Walter

Niederwieser, Alois

URI (zitierfähiger Link)

http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-57148

Link zur Lizenz

Attribution-NonCommercial-NoDerivs 2.0 Generic

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

European Journal of Biochemistry. 1985, 148(3), pp. 413-419. ISSN 0014-2956. eISSN 1432-1033

Zusammenfassung

The biosynthesis of tetrahydrobiopterin from either dihydroneopterin triphosphate, sepiapterin, dihydrosepiapterin or dihydrobiopterin was investigated using extracts from human liver, dihydrofolate reductase and purified sepiapterin reductase from human liver and rat erythrocytes. The incorporation of hydrogen in tetrahydrobiopterin was studied in either 2H2O or in H2O using unlabeled NAD(P)H or (R)-(4-2H)NAD(P)H or (S)-(4-2H)NAD(P)H. Dihydrofolate reductase catalyzed the transfer of the pro-R hydrogen of NAD(P)H during the reduction of 7,8-dihydrobiopterin to tetrahydrobiopterin. Sepiapterin reductase catalyzed the transfer of the pro-S hydrogen of NADPH during the reduction of sepiapterin to 7,8-dihydrobiopterin. In the presence of partially purified human liver extracts one hydrogen from the solvent is introduced at position C(6) and the 4-pro-S hydrogen from NADPH is incorporated at each of the C(1') and C(2') position of BH4. Label from the solvent is also introduced into position C(3'). These results suggest that dihydrofolate reductase is not involved in the biosynthesis of tetrahydrobiopterin from dihydroneopterin triphosphate. They are consistent with the assumption of the occurrence of a 6-pyruvoyl-tetrahydropterin intermediate, which is proposed to be formed upon triphosphate elimination from dihydroneopterin triphosphate, and via an intramolecular redox reaction. Our results suggest that the reduction of 6-pyruvoyl-tetrahydropterin might be catalyzed by sepiapterin reductase.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

CURTIUS, Hans-Christoph, Dorothee HEINTEL, Sandro GHISLA, Thomas KUSTER, Walter LEIMBACHER, Alois NIEDERWIESER, 1985. Tetrahydrobiopterin biosynthesis : Studies with specifically labeled (2H)NAD(P)H and 2H2O and of the enzymes involved. In: European Journal of Biochemistry. 1985, 148(3), pp. 413-419. ISSN 0014-2956. eISSN 1432-1033

BibTex

@article{Curtius1985Tetra-7427,
  year={1985},
  title={Tetrahydrobiopterin biosynthesis : Studies with specifically labeled (2H)NAD(P)H and 2H2O and of the enzymes involved},
  number={3},
  volume={148},
  issn={0014-2956},
  journal={European Journal of Biochemistry},
  pages={413--419},
  author={Curtius, Hans-Christoph and Heintel, Dorothee and Ghisla, Sandro and Kuster, Thomas and Leimbacher, Walter and Niederwieser, Alois}
}

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