Phenylalanine dehydrogenase (PheDH)

Phenylalanine dehydrogenase (PheDH) is a microbial enzyme belonging to the oxidoreductase family that catalyzes the reversible oxidative deamination of L-phenylalanine into phenylpyruvate, utilizing NAD+ or NADP+ as a cofactor [1, 2]. Although not naturally occurring in humans, PheDH is widely produced by various bacterial species, including members of the genera Bacillus, Sporosarcina, and Rhodococcus [1]. In the medical field, the enzyme is primarily utilized as a critical diagnostic tool; it serves as the core component in biosensors and clinical assays designed to monitor phenylalanine levels in patients with Phenylketonuria (PKU) [3, 5]. Beyond its diagnostic utility, research has explored the potential of PheDH as an enzyme substitution therapy to lower toxic systemic phenylalanine levels, similar to the application of phenylalanine ammonia-lyase [4]. Additionally, PheDH is employed in industrial biocatalysis for the stereospecific synthesis of L-phenylalanine and other chiral amino acids [6]. Its high specificity for L-phenylalanine makes it an essential molecule for both metabolic monitoring and biotechnological production.

Other names

L-phenylalanine dehydrogenasePhenylalanine:NAD+ oxidoreductase (deaminating)PheD

Catalyzes the reversible NAD+-dependent oxidative deamination of L-phenylalanine to phenylpyruvate, ammonia, and NADH [1, 2].