Sandbox Reserved 642
From Proteopedia
This Sandbox is Reserved from 30/08/2012, through 01/02/2013 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 636 through Sandbox Reserved 685. | ||||||
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More help: Help:Editing 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 hydroxylation. In most organisms, this reaction is the first step in phenyalanine degradation. 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.
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