Abstract
Phenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyses the conversion of L-phenylalanine (L-Phe) to form L-tyrosine (L-Tyr) in the presence of the cofactor tetrahydrobiopterin (BH4) and dioxygen. It is well established that PAH is activated by its substrate L-Phe, and upon binding of L-Phe the enzyme exhibits a sigmoidal dependence of activity on substrate concentration, which reflects a slow transition (minutes) of the enzyme from a low activity to a high activity state (1), characteristic of a hysteretic enzyme (2).
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Stokka, A.J., Flatmark, T. (2002). 3-(2-Thienyl)-L-Alanine as a Competitive Substrate Analogue and Activator of Human Phenylalanine Hydroxylase. In: Milstien, S., Kapatos, G., Levine, R.A., Shane, B. (eds) Chemistry and Biology of Pteridines and Folates. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0945-5_18
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DOI: https://doi.org/10.1007/978-1-4615-0945-5_18
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