Abstract
Tetrahydrobiopterin is a cofactor of the aromatic amino acid hydroxylases1. 6-Pyruvoyl tetrahydropterin(PTP) synthase is essential in the biosynthesis of tetrahydrobiopterin. This enzyme catalyzes the conversion of dihydroneopterin triphosphate to PTP in the presence of Mg2+2. The decrease of the amount of this enzymatic activity is the most frequent cause of atypical phenylketonuria3,4. PTP synthases were highly purified from human liver5, salmon liver6, and Drosophila head7. Recently, cDNA sequence of PTP synthase from rat liver was reported8. However, although PTP synthases were highly purified from several sources, the information on the enzymatic properties has been reported hardly anything.
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© 1993 Springer Science+Business Media New York
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Masada, M. (1993). Enzymatic Properties of 6-Pyruvoyl Tetrahydropterin Synthase Purified from Fat Bodies of Silkworm Larvae. In: Ayling, J.E., Nair, M.G., Baugh, C.M. (eds) Chemistry and Biology of Pteridines and Folates. Advances in Experimental Medicine and Biology, vol 338. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2960-6_38
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DOI: https://doi.org/10.1007/978-1-4615-2960-6_38
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