Sandbox Reserved 480: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
<Structure load='2pah' size='400' frame='true' align='right' caption='Phenylalanine Hydroxylase' scene='Insert optional scene name here' /> | <Structure load='2pah' size='400' frame='true' align='right' caption='Phenylalanine Hydroxylase' scene='Insert optional scene name here' /> | ||
Phenylalanine Hydroxylase (<scene name='Sandbox_Reserved_480/Phenylalanine_hydroxylase/2'>PheOH</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 | Phenylalanine Hydroxylase (<scene name='Sandbox_Reserved_480/Phenylalanine_hydroxylase/2'>PheOH</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 tetrahydrobiopterin to convert their amino acid substrates into products. | ||
== Structure == | == Structure == | ||
The regulatory domain affects the function of the active site. When the regulatory domain is <scene name='Sandbox_Reserved_480/Phosphorylated_pheoh/2'>phosphorylated</scene>, the active site is closed off and prevented form interacting with the substrates. | |||
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 | 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 . | ||
Revision as of 17:55, 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: https://www.proteopedia.org/wiki/index.php/Help:Getting_Started_in_Proteopedia  Phenylalanine Hydroxylase
Phenylalanine Hydroxylase (PheOH) 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 tetrahydrobiopterin to convert their amino acid substrates into products. StructureThe regulatory domain affects the function of the active site. When the regulatory domain is phosphorylated, the active site is closed off and prevented form interacting with the substrates. PheOH is a tetrameric enzyme, consisting of 2 asymmetric components. It contains an It has been observed as a dimer and tetrameric structure. This is the active site within the subunit. This includes the residues His, His, and This enzyme has two ligands, 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 |
