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For more help, look at this link: http://proteopedia.org/w/Help:Getting_Started_in_Proteopedia 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 phenyalanine 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 phenyalanine degradation. A faulty PAH gene can cause an increase in phenylalanine level in the plasma, resulting in the genetic disorder Phenylketonuria (PKU).

PheOH can exist as a dimer or tetramer with identical subunits. Each subunit is organized to have a regulatory, catalytic and tetramerization domain. The center of each catalytic domain consists of an iron ion which is vital to the enzyme activity.