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- W2044329596 abstract "Abstract The enzyme, D-erythrodihydroneopterin triphosphate synthetase from rat brain was observed to have a significantly lower specific activity than that from liver due to their degree of dephosphorylation during preparation. The brain enzyme could be phosphorylated in vitro in presence of [32P]-ATP and protein kinase, resulting in an increased specific activity. Isolation of brain enzyme in presence of 0.8 M NaF allowed recovery of the enzyme phosphorylated at residue 67 (serine) as determined by a new assay for phosphate. This enzyme is present in synaptosomes and its state of phosphorylation may regulate the rate at which dihydrobiopterin, the precursor of the hydroxylase cofactor (tetrahydrobiopterin, BH4), is synthesized by synaptosomes." @default.
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- W2044329596 date "1978-07-01" @default.
- W2044329596 modified "2023-09-26" @default.
- W2044329596 title "Phosphorylation, a factor controlling the synthesis of L-erythrodihydrobiopterin (BH2)" @default.
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- W2044329596 doi "https://doi.org/10.1016/0006-291x(78)91031-8" @default.
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