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- W1427550133 abstract "This chapter discusses the assay, purification, and properties of phenylalanine hydroxylase from Pseudomonas. The hydroxylation of phenylalanine to tyrosine is catalyzed by an inducible enzyme from Pseudomonas. This conversion requires molecular oxygen and a tetrahydropteridine. The molecular oxygen is the source of the oxygen of the tyrosine hydroxyl. The purified enzyme is inactive unless preincubated with a metal ion in the absence of substrate. The enzyme can be assayed either by the fluorometric determination of the tyrosine produced or by the measurement of the tritium released upon the hydroxylation of p-tritiophenylalanine and iodination of the product. One unit of enzyme is the amount of enzyme that produces 1 millimicromole of tyrosine by the fluorometric assay or hydroxylates 1 millimicromole of phenylalanine by the isotope assay. The two methods give comparable values if a small correction is introduced to correct for slightly less than 100% iodination. The preparation, usually stored in small portions at -20°, is quite stable over a period of a few months. The requirements for activation by ferrous ion can be satisfied by Hg2, Cd2+, Cu2+, or Cu+ as well." @default.
- W1427550133 created "2016-06-24" @default.
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- W1427550133 date "1970-01-01" @default.
- W1427550133 modified "2023-09-26" @default.
- W1427550133 title "[74] Phenylalanine hydroxylase (Pseudomonas)" @default.
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- W1427550133 doi "https://doi.org/10.1016/0076-6879(71)17246-1" @default.
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