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Phenylalanine hydroxylase (PAH) ( EC 126.96.36.199 ) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine . PAH is one of three members of the biopterin -dependent aromatic amino acid hydroxylases , a class of monooxygenase that uses tetrahydrobiopterin (BH 4 , a pteridine cofactor) and a non-heme iron for catalysis. During the reaction, molecular oxygen is heterolytically cleaved with sequential incorporation of one oxygen atom into BH 4 and phenylalanine substrate. 
PAH deficiency can be detected by newborn screening in virtually 100% of cases based on the presence of hyperphenylalaninemia using tandem mass spectrometry on a blood spot obtained from a heel prick. The diagnosis of PAH deficiency is established in a proband with:
The PAH gene provides instructions for making an enzyme called phenylalanine hydroxylase. This enzyme is responsible for the first step in processing phenylalanine, which is a building block of proteins (an amino acid) obtained through the diet. Phenylalanine is found in all proteins and in some artificial sweeteners.
Phenylalanine is found naturally in the breast milk of mammals. It is used in the manufacture of food and drink products and sold as a nutritional supplement for its reputed analgesic and antidepressant effects. It is a direct precursor to the neuromodulator phenethylamine , a commonly used dietary supplement .