Sandbox Reserved 480
From Proteopedia
| Line 4: | Line 4: | ||
== Phenylalanine Hydroxylase == | == Phenylalanine Hydroxylase == | ||
| - | [[Image:2pah_bio_r_500.jpg]] | ||
<Structure load='1tg2' size='400' frame='true' align='right' caption='Phenylalanine Hydroxylase' scene='Phenylalanine Hydroxylase' /> | <Structure load='1tg2' size='400' frame='true' align='right' caption='Phenylalanine Hydroxylase' scene='Phenylalanine Hydroxylase' /> | ||
| - | Phenylalanine Hydroxylase(<scene name='Sandbox_Reserved_480/Phenylalanine_hydroxylase/1'>PAH</scene>)is a type of enzyme involved in the catalization of phenylalanine into tyrosine. | + | Phenylalanine Hydroxylase(<scene name='Sandbox_Reserved_480/Phenylalanine_hydroxylase/1'>PAH</scene>)is a type of enzyme involved in the catalization of phenylalanine into tyrosine. It belongs to the family of aromatic amino acid hydroxylases. Some other enzymes in this family include tyrosine hydroxylase and tryptophan hydroxylase. These enzymes require oxygen and forms of pterin to convert their amino acid substrates into products. |
| - | + | ||
| - | + | ||
== Structure == | == Structure == | ||
| - | It has been observed as a <scene name='Sandbox_Reserved_480/Dimer/1'>dimer</scene> and tetrameric structure. This is the <scene name='Sandbox_Reserved_480/Active_site/3'>active</scene> site within the subunit. This includes the residues His, His, and | + | PheOH is a tetrameric enzyme, consisting of 2 asymmetric components. It contains an It has been observed as a <scene name='Sandbox_Reserved_480/Dimer/1'>dimer</scene> and tetrameric structure. This is the <scene name='Sandbox_Reserved_480/Active_site/3'>active</scene> site within the subunit. This includes the residues His, His, and |
This enzyme has two <scene name='Sandbox_Reserved_480/Ligands/1'>ligands</scene>, Fe (III) and . | This enzyme has two <scene name='Sandbox_Reserved_480/Ligands/1'>ligands</scene>, Fe (III) and . | ||
| - | == | + | == Phenylketonuria == |
| - | + | Phenylalanine hydroxylase is the rate limiting exzyme invovled in the metabolism of phenylalanine. With Fe (III), oxygen, and tetrahydrobiopterin, PheOH hydroxylates Phe into Tyr. Tyr goes on to make L-dopa and eventually dopamine. | |
| + | |||
== Mechanism == | == Mechanism == | ||
== References == | == References == | ||
Revision as of 04:53, 2 May 2012
| This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500. | |||||||
To get started:
More help: Help:Editing For more help, look at this link: http://www.proteopedia.org/wiki/index.php/Help:Getting_Started_in_Proteopedia
Phenylalanine Hydroxylase
Phenylalanine Hydroxylase()is a type of enzyme involved in the catalization of phenylalanine into tyrosine. It belongs to the family of aromatic amino acid hydroxylases. Some other enzymes in this family include tyrosine hydroxylase and tryptophan hydroxylase. These enzymes require oxygen and forms of pterin to convert their amino acid substrates into products. StructurePheOH is a tetrameric enzyme, consisting of 2 asymmetric components. It contains an It has been observed as a and tetrameric structure. This is the site within the subunit. This includes the residues His, His, and This enzyme has two , Fe (III) and . PhenylketonuriaPhenylalanine hydroxylase is the rate limiting exzyme invovled in the metabolism of phenylalanine. With Fe (III), oxygen, and tetrahydrobiopterin, PheOH hydroxylates Phe into Tyr. Tyr goes on to make L-dopa and eventually dopamine. MechanismReferences |
