Not available outside of the UK & Ireland.

Application

L-Phenylalanine dehydrogenase is a NAD+-dependent oxidoreductase that catalyzes the reversible, oxidative deamination of L-phenylalanine which results in its degradation. L-Phenylalanine dehydrogenase is used to study phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis.

Biochem/physiol Actions

Phenylalanine dehydrogenase (PheDH) is considered as an effective enzyme to estimate the quantity of phenylalanine to distinguish phenylketonuria (PKU) disease.

Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine €-dehydrogenase, and meso-a,€-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure.

Unit Definition

One unit will oxidize 1.0 µmole of L-phenylalanine per min at pH 10.5 at 30 °C in the presence of β-NAD.