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14. 16. 1) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine. PheOH is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH4, 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 BH4 and phenylalanine substrate.
expasy. org/enzyme/. If you go there, click search by cofactor and then click on the 3 listings of iron and the one of heme. These enzymes allow necessary biochemical reactions and transformations to take place. Some of the more studied of these enzymes are cytochrome C, cytochrome C oxidase, catalase, aconitase, and aromatic amino acid hydroxylases. The iron related enzymes are quite sensitive to depletion with even minor iron deficiency.