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'''Phenylalanine Hydroxylase''' (also known as Phenylalanine-4-monooxygenase or simply PAH) is the enzyme that catalyzes the conversion of L-phenylalanine into L-tyrosine by hydroxylation (addition of an -OH group) of the aromatic side chain of phenyalanine. This reaction is the initial and rate-limiting step in the phenylalanine catabolism pathway.

<Structure load='2pah' size='500' frame='true' align='right' caption='Dimeric Unit of Phenylalanine Hydroxylase with the iron atom in the active sites in brown. ' scene='~~Insert optional~~ scene name ~~here~~' />The tyrosine product (a non-essential amino acid) can then serve as a precursor to the synthesis of important neurotransmitters.<ref name= "flydal"> Flydal, Marte, and Aurora Martinez. "Phenylalanine Hydroxylase: Function, Structure, and Regulation." International Union of Biochemistry and Molecular Biology Journal 65.4 (2013): 341-349. Web. </ref>.

<Structure load='2pah' size='500' frame='true' align='right' caption='Dimeric Unit of Phenylalanine Hydroxylase with the iron atom in the active sites in brown. ' scene='<scene name='56/564044/Dimeric_structure/1'>TextToBeDisplayed</scene>' />The tyrosine product (a non-essential amino acid) can then serve as a precursor to the synthesis of important neurotransmitters.<ref name= "flydal"> Flydal, Marte, and Aurora Martinez. "Phenylalanine Hydroxylase: Function, Structure, and Regulation." International Union of Biochemistry and Molecular Biology Journal 65.4 (2013): 341-349. Web. </ref>.

PAH uses tetrahydrobiopterin (BH4) as a cofactor and has a nonheme iron atom bound to its active site. PAH is classified as an oxidoreductase, specifically enzyme class EC 1.14 since its mechanism of action involves the oxidation/reduction of its substrate. <ref name= "pdb"> http://www.rcsb.org/pdb/explore/explore.do?structureId=1J8U </ref>.

Sandbox Reserved 768: Difference between revisions

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 '''Phenylalanine Hydroxylase''' (also known as Phenylalanine-4-monooxygenase or simply PAH) is the enzyme that catalyzes the conversion of L-phenylalanine into L-tyrosine by hydroxylation (addition of an -OH group) of the aromatic side chain of phenyalanine. This reaction is the initial and rate-limiting step in the phenylalanine catabolism pathway.
-<Structure load='2pah' size='500' frame='true' align='right' caption='Dimeric Unit of Phenylalanine Hydroxylase with the iron atom in the active sites in brown. ' scene='Insert optional scene name here' />The tyrosine product (a non-essential amino acid) can then serve as a precursor to the synthesis  of important neurotransmitters.<ref name= "flydal"> Flydal, Marte, and Aurora Martinez. "Phenylalanine Hydroxylase: Function, Structure, and Regulation." International Union of Biochemistry and Molecular Biology Journal 65.4 (2013): 341-349. Web. </ref>.
+<Structure load='2pah' size='500' frame='true' align='right' caption='Dimeric Unit of Phenylalanine Hydroxylase with the iron atom in the active sites in brown. ' scene='<scene name='56/564044/Dimeric_structure/1'>TextToBeDisplayed</scene>' />The tyrosine product (a non-essential amino acid) can then serve as a precursor to the synthesis  of important neurotransmitters.<ref name= "flydal"> Flydal, Marte, and Aurora Martinez. "Phenylalanine Hydroxylase: Function, Structure, and Regulation." International Union of Biochemistry and Molecular Biology Journal 65.4 (2013): 341-349. Web. </ref>.
 PAH uses tetrahydrobiopterin (BH4) as a cofactor and has a nonheme iron atom bound to its active site. PAH is classified as an oxidoreductase, specifically enzyme class EC 1.14 since its mechanism of action involves the oxidation/reduction of its substrate. <ref name= "pdb"> http://www.rcsb.org/pdb/explore/explore.do?structureId=1J8U </ref>.