L-Phenylalanine Dehydrogenase from Sporosarcina sp.

Research area: CELL SIGNALING

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

Phenylalanine dehydrogenase (PheDH) is considered an effective enzyme to estimate the quantity of phenylalanine to distinguish phenylketonuria (PKU) disease.Moreover, it is utilized for the production of optically pure l-phenylalanine, a key component of the artificial sweetener aspartame. 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.

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.