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= Phenylalanine Hydroxylase =

'''Phenylalanine Hydroxylase'''(PheOH), otherwise known as phenylalaine-4-monooxygenase, is an enzyme produced by the ''PAH'' gene found on the twelfth chromosome in the human genome, but it is also found in some bacteria. This enzyme functions as a catalyst in the conversion of the amino acids phenylalanine to tyrosine by adding a hydroxyl group (-OH) to the benzene ring of the amino acid. This is why this protein is therefore classified as a hydroxylase. In most organisms, this hydroxylation process is the first step in phenylalanine degradation. A faulty ''PAH'' gene can cause an increase in phenylalanine level in the plasma, resulting in the genetic disorder Phenylketonuria (PKU).<ref> College, Davidson. The Structure-Function of Phenylalanine Hydroxylase [http://www.bio.davidson.edu/courses/molbio/molstudents/spring2005/castle/assign1home.html]</ref>

'''Phenylalanine Hydroxylase'''(PheOH), otherwise known as phenylalaine-4-monooxygenase, is an enzyme produced by the ''PAH'' gene found on the twelfth chromosome in the human genome, but it is also found in some bacteria. This enzyme functions as a catalyst in the conversion of the amino acids phenylalanine to tyrosine by adding a hydroxyl group (-OH) to the benzene ring of the amino acid. This is why this protein is therefore classified as a hydroxylase. In most organisms, this hydroxylation process is the first step in phenylalanine degradation. A faulty ''PAH'' gene can cause an increase in phenylalanine level in the plasma, resulting in the genetic disorder Phenylketonuria (PKU).<ref> College, Davidson. The Structure-Function of Phenylalanine Hydroxylase [http://www.bio.davidson.edu/courses/molbio/molstudents/spring2005/castle/assign1home.html]</ref> Other proteins in this classification include Tryptophan and Tyrosine Hydroxylase. These three amino acid hydroxylases share a highly conserved region of 27 amino acids from His263 to His289. <ref> Erlandsen H., DirSci; Marianne G. Patch, PhD; Alejandra Gamez, PhD; Mary Straub; and Raymond C. Stevens, PhD. Structural Studies on Phenylalanine Hydroxylase and Implications Toward Understanding and Treating Phenylketonuria [http://www.pkuworld.org/home/docs/literature/erlandsen_2003_p.pdf]</ref>

Sandbox Reserved 642: Difference between revisions

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 = Phenylalanine Hydroxylase =
 <Structure load='2PAH_tetramer3.pdb' size='500' frame='true' align='right' caption='This is a model of the pheylalanine hydroxylase dimer as found in humans. The green ball in within each subunit represents the iron ion in the catalytic domains.' scene='Insert optional scene name here' />
-'''Phenylalanine Hydroxylase'''(PheOH), otherwise known as phenylalaine-4-monooxygenase, is an enzyme produced by the ''PAH'' gene found on the twelfth chromosome in the human genome, but it is also found in some bacteria. This enzyme functions as a catalyst in the conversion of the amino acids phenylalanine to tyrosine by adding a hydroxyl group (-OH) to the benzene ring of the amino acid. This is why this protein is therefore classified as a hydroxylase. In most organisms, this hydroxylation process is the first step in phenylalanine degradation. A faulty ''PAH'' gene can cause an increase in phenylalanine level in the plasma, resulting in the genetic disorder Phenylketonuria (PKU).<ref> College, Davidson. The Structure-Function of Phenylalanine Hydroxylase [http://www.bio.davidson.edu/courses/molbio/molstudents/spring2005/castle/assign1home.html]</ref>
+'''Phenylalanine Hydroxylase'''(PheOH), otherwise known as phenylalaine-4-monooxygenase, is an enzyme produced by the ''PAH'' gene found on the twelfth chromosome in the human genome, but it is also found in some bacteria. This enzyme functions as a catalyst in the conversion of the amino acids phenylalanine to tyrosine by adding a hydroxyl group (-OH) to the benzene ring of the amino acid. This is why this protein is therefore classified as a hydroxylase. In most organisms, this hydroxylation process is the first step in phenylalanine degradation. A faulty ''PAH'' gene can cause an increase in phenylalanine level in the plasma, resulting in the genetic disorder Phenylketonuria (PKU).<ref> College, Davidson. The Structure-Function of Phenylalanine Hydroxylase [http://www.bio.davidson.edu/courses/molbio/molstudents/spring2005/castle/assign1home.html]</ref> Other proteins in this classification include Tryptophan and Tyrosine Hydroxylase. These three amino acid hydroxylases share a highly conserved region of 27 amino acids from His263 to His289. <ref> Erlandsen H., DirSci; Marianne G. Patch, PhD; Alejandra Gamez, PhD; Mary Straub; and Raymond C. Stevens, PhD. Structural Studies on Phenylalanine Hydroxylase and Implications Toward Understanding and Treating Phenylketonuria [http://www.pkuworld.org/home/docs/literature/erlandsen_2003_p.pdf]</ref>