Sandbox Reserved 642
From Proteopedia
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<Structure load='2PAH' size='500' frame='true' align='right' caption='This is a model of the pheylalanine hydroxylase dimer as found in humans. The red ball in within each subunit represents the iron ion in the catalytic domains. ' scene='Insert optional scene name here' /> | <Structure load='2PAH' size='500' frame='true' align='right' caption='This is a model of the pheylalanine hydroxylase dimer as found in humans. The red ball in within each subunit represents the iron ion in the catalytic domains. ' scene='Insert optional scene name here' /> | ||
| - | PheOH can exist as a dimer or tetramer with identical subunits. Each subunit is organized to have a regulatory, catalytic and tetramerization domain. The native form of human PheOH has an estimated secondary structure composed 48% alpha-helices, 28% extended structures, 12% beta-turns, and 12% non-structured conformations. The more structured elements are usually concentrated in the catalytic C-terminal domain of the protein, while the more flexible and unstructured elements are grouped in the regulatory N-terminal domain. The active site of PheOH can be found in the center of the catalytic domain and is characterized by a 13 Angrstrums deep and 10 Angstrums wide hydrophobic pocket. Lining the active site are 3 glutamates, 2 histadines and 1 tyrosine residues. The center of each catalytic domain consists of an iron ion which is vital to the enzyme activity and binds to histadine residues 285 and 290, 1 oxygen atom and glutamate 330. | + | PheOH can exist as a dimer or tetramer with identical subunits. Each subunit is organized to have a regulatory, catalytic and tetramerization domain. The native form of human PheOH has an estimated secondary structure composed 48% alpha-helices, 28% extended structures, 12% beta-turns, and 12% non-structured conformations. The more structured elements are usually concentrated in the catalytic C-terminal domain of the protein, while the more flexible and unstructured elements are grouped in the regulatory N-terminal domain. The active site of PheOH can be found in the center of the catalytic domain and is characterized by a 13 Angrstrums deep and 10 Angstrums wide hydrophobic pocket. Lining the active site are 3 glutamates, 2 histadines and 1 tyrosine residues. The center of each catalytic domain consists of an iron ion which is vital to the enzyme activity and binds to histadine residues 285 and 290, 1 oxygen atom and glutamate 330. The PheOH model protein was generated via xray crystallography. |
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www.pdb.org/pdb/education_discussion/molecule_of_the_month/download/PhenylalanineHydroxylase.pdf. | www.pdb.org/pdb/education_discussion/molecule_of_the_month/download/PhenylalanineHydroxylase.pdf. | ||
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| + | www.pkuworld.org/hom/docs/lierature/erlandsen_2003_p.pdf | ||
Revision as of 22:14, 4 November 2012
| 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 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 native form of human PheOH has an estimated secondary structure composed 48% alpha-helices, 28% extended structures, 12% beta-turns, and 12% non-structured conformations. The more structured elements are usually concentrated in the catalytic C-terminal domain of the protein, while the more flexible and unstructured elements are grouped in the regulatory N-terminal domain. The active site of PheOH can be found in the center of the catalytic domain and is characterized by a 13 Angrstrums deep and 10 Angstrums wide hydrophobic pocket. Lining the active site are 3 glutamates, 2 histadines and 1 tyrosine residues. The center of each catalytic domain consists of an iron ion which is vital to the enzyme activity and binds to histadine residues 285 and 290, 1 oxygen atom and glutamate 330. The PheOH model protein was generated via xray crystallography.
References Fusetti, F., Erlandsen,H., Flatmark, T., and Stevens, R.C., Structure of tetrameric human phenyalanine hydroxylase and its implications for phenylketonuria. (www.rcsb.org/pdb/explore/explore.do?structureID=2PAH) www.bio.davidson.edu/courses/molbio/molstudents/spring2005/castle/assign1home.html www.ncbi.nlm.nih.gov/pubmed/9490012 www.pdb.org/pdb/education_discussion/molecule_of_the_month/download/PhenylalanineHydroxylase.pdf. www.pkuworld.org/hom/docs/lierature/erlandsen_2003_p.pdf |
![[1]](http://www.bmb.leeds.ac.uk/illingworth/bioc1010/image017.gif){kind=link}