PMID: 2110003Apr 19, 1990Paper

Purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from Drosophila melanogaster

Biochimica Et Biophysica Acta
Y S ParkJ J Yim


The enzyme 6-pyruvoyl-tetrahydropterin synthase (PTP synthase), which catalyzes the conversion of 7,8-dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, has been purified approx. 230-fold to apparent homogeneity from head extracts of Drosophila melanogaster. A partially purified 6-pyruvoyl-tetrahydropterin reductase (PTP reductase) was also prepared and in its presence, along with Mg2+ and NADPH, the purified PTP synthase converted 7,8-dihydroneopterin triphosphate to metastable 6-lactoyltetrahydropterin, which was autoxidized to sepiapterin under aerobic conditions. Purified PTP synthase had a specific activity of 3792 units per mg protein and migrated as a single protein band on both nondenaturing polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The purified active enzyme consisted of at least two identical subunits which had a molecular mass of 37.5 kDa on SDS-PAGE and NH2-Asx-Pro- as N-terminal amino acids. The native enzyme in crude extract was shown to be more complex, existing as higher multimeric forms.


Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
Aug 10, 1966·Biochimica Et Biophysica Acta·M MatsubaraS Kaufman
Jan 1, 1984·Methods in Enzymology·C R MerrilM L Van Keuren
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Dec 28, 1964·Annals of the New York Academy of Sciences·B J DAVIS
Oct 23, 2009·Brain : a Journal of Neurology·Lindsay E RhodesKenneth H Fischbeck

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