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Tetrameric Structure of PheOH

Phenylalanine Hydroxylase

Phenylalanine Hydroxylase (PheOH) is a type of enzyme involved in the catalization of phenylalanine into tyrosine. It belongs to the family of aromatic amino acid hydroxylases. Some other enzymes in this family include tyrosine hydroxylase and tryptophan hydroxylase. These enzymes require oxygen and tetrahydrobiopterin to convert their amino acid substrates into products.

Structure

The regulatory domain affects the function of the active site. When the regulatory domain is , the active site is closed off and prevented form interacting with the substrates. In this scene the chain is colored from N-terminus to C-terminus blue to red and the active site and Fe (III) is colored black. In the PheOH, the active site is open to the subtrates and can convert them to products.

PheOH is a tetrameric enzyme, consisting of 2 asymmetric components. It contains an It has been observed as a and tetrameric structure. This is the site within the subunit. This includes the residues His, His, and This enzyme has two , Fe (III) and .

Phenylketonuria

Phenylalanine hydroxylase is the rate limiting exzyme invovled in the metabolism of phenylalanine. With Fe (III), oxygen, and tetrahydrobiopterin, PheOH hydroxylates Phe into Tyr. Tyr goes on to make L-dopa and eventually dopamine.

Mechanism

References