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Sandbox Reserved 480

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{{Sandbox_Reserved_Robert_B_Rose_1}}
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<Structure load='1tg2' size='500' frame='true' align='right' caption='Phenylalanine Hydroxylase' scene='Phenylalanine Hydroxylase' />
 
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== Phenylalanine Hydroxylase ==
== Phenylalanine Hydroxylase ==
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<Structure load='1tg2' size='500' 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. 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
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 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 .
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== Introduction ==
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== Structure ==
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== Mechanism ==
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== Medical Implications ==
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== References ==

Revision as of 02:42, 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.
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Contents

Phenylalanine Hydroxylase

Phenylalanine Hydroxylase

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Phenylalanine Hydroxylase()is a type of enzyme involved in the catalization of phenylalanine into tyrosine. 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 .

Introduction

Structure

Mechanism

Medical Implications

References

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