Sandbox Reserved 768: Difference between revisions
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Each monomeric subunit is composed of three sites: the N-terminal, the catalytic site, and the C-terminal. <ref name= "flydal"/>. | Each monomeric subunit is composed of three sites: the N-terminal, the catalytic site, and the C-terminal. <ref name= "flydal"/>. | ||
PAH enzyme has been studied extensively because of its correlation with the genetic defective condition phenylketonuria (PKU). Errors in the function or stability of PAH lead to its malfunction which causes a buildup of phenylalanine resulting in numerous health detriments. | PAH enzyme has been studied extensively because of its correlation with the genetic defective condition phenylketonuria (PKU). Errors in the function or stability of PAH lead to its malfunction which causes a buildup of phenylalanine resulting in numerous health detriments. | ||
== Phenylalanine Hydroxylase Mechanism of Action == | |||
PAH, belonging to the oxidoreductase enzyme class, acts on paired donors with pteridine being a donor and first incorporates one atom of molecular oxygen into the aromatic ring of phenylalanine. Then, it reduces the second oxygen atom to water using the two electrons that are supplied by the BH4 cofactor. BH4 is also hydroxylated at each turnover to produce pterin-4a-carbinolamine (4a-OH-BH4), with consequent dissociation from the enzyme. 4a-OHBH4 is dehydrated and reduced back to BH4 by the action of the enzyme pterin carbinolamine dehydratase. <ref name= "flydal"/>. | |||
