What is the structure of phenylalanine?
C9H11NO2
Phenylalanine/Formula
What is the role of phenylalanine hydroxylase?
Phenylalanine hydroxylase is responsible for the conversion of phenylalanine to another amino acid, tyrosine. The enzyme works with a molecule called tetrahydrobiopterin (BH4) to carry out this chemical reaction.
What is the mechanism of phenylalanine hydroxylase?
Phenylalanine hydroxylase (PheH) catalyzes the hydroxylation of phenylalanine to tyrosine (Scheme 1) in catabolism of phenylalanine in the liver, with tetrahydrobiopterin (BH4) supplying the two electrons needed for the reaction (1).
Does phenylalanine 4 hydroxylase require a cofactor?
The hydroxylation of phenylalanine requires free oxygen and a helper molecule (cofactor), tetrahydrobiopterin. These mutations disrupt the interaction of the enzyme with either the cofactor or the iron ion, reducing or stopping the enzyme activity.
What type of protein is phenylalanine hydroxylase?
PAH is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH4, a pteridine cofactor) and a non-heme iron for catalysis.
Is phenylalanine bad in drinks?
Phenylalanine can cause intellectual disabilities, brain damage, seizures and other problems in people with PKU . Phenylalanine occurs naturally in many protein-rich foods, such as milk, eggs and meat. Phenylalanine is also sold as a dietary supplement.
What is the function of phenylalanine hydroxylase ( PAH )?
Phenylalanine hydroxylase (PAH) is a key enzyme in the catabolism of phenylalanine, and mutations in this enzyme cause phenylketonuria (PKU), a genetic disorder that leads to brain damage and mental retardation if untreated.
What is the BH 4 bound state of PAH?
The BH 4 -bound state is physiologically relevant, keeping PAH stable and in a precatalytic state at low L-Phe concentration. Furthermore, a synthetic form of BH 4 (Kuvan) is the only drug-based therapy for a subset of phenylketonuria patients.
What kind of iron is used in phenylalanine hydroxylase?
Phenylalanine hydroxylase. PAH is one of three members of the biopterin -dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH 4, a pteridine cofactor) and a non-heme iron for catalysis. During the reaction, molecular oxygen is heterolytically cleaved with sequential incorporation…
Why is phenylalanine hydroxylase not a positive cooperativity?
In addition to reduced catalytic efficiency, the dimer does not display positive cooperativity toward L-Phe (which at high concentrations activates the enzyme), suggesting that L-Phe allosterically regulates PAH by influencing dimer-dimer interaction.
