Phenylalanine Research Paper

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Seema Sabbagh
Dr. Kelts – CHM 405
Phenylalanine Hydroxylase Structure and Mutant Forms
Amino acids are the building blocks of all proteins, and can be divided into two groups, essential and non-essential amino acids. Essential amino acids cannot be synthesized by the body, and must be provided from one’s diet, while nonessential amino acids are made up in the body. Phenylalanine, a neutral and nonpolar amino acid, is one of the essential amino acids for the body. The L-isomer side chain is made up of an aromatic benzene ring that is hydrophobic, and therefore is marginally nonreactive. Because of this, the amino acid seldom participates in direct protein function; but is involved in stacking interactions between other aromatic side chains. Therefore, the main function of this amino acid is that it serves as the precursor to the amino acid, tyrosine. Tyrosine differs from phenylalanine as it contains a reactive hydroxyl group on the aromatic benzene ring, in the ortho- position. After the conversion to tyrosine, it is …show more content…
The blue region shows the N-terminal regulatory domain, the red region shows the catalytic domain, and the green region shows the tautermization domain. The iron ion is shown in light blue sphere in the middle of the catalytic domain.
The dimerization of the phenylalanine hydroxylase monomers occurs when two loops, residues 414-420, both related to one another through their symmetry, interact. Their interaction is strengthened by van der Waals forces, along with hydrogen-bonding. The recombinant dimeric form of PEH is constitutes the active state of the enzyme. Based on the crystal structure of this enzyme, it has been observed that the active site gives easy access for the substrate to bind. Although the 3D structure of the truncated form of dimeric human PAH, the crystal structure of the full-length tetrameric PAH has yet to be

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