This recombinant protein product features a stable and soluble fragment (residues 2-104) of human Pterin-4-alpha-carbinolamine dehydratase (PHS), also known as DCoH or PCD. It is designed for structural and biochemical studies, offering a functional unit that supports research into tetrahydrobiopterin biosynthesis and transcriptional coactivation mechanisms.

The full-length Pterin-4-alpha-carbinolamine dehydratase (encoded by the PCBD1 gene) plays a dual role in cellular processes. It is involved in tetrahydrobiopterin biosynthesis by preventing the formation of 7-pterins and accelerating quinonoid-BH2 production, which is critical for neurotransmitter and nitric oxide synthesis. Additionally, it acts as a coactivator for transcription factors HNF1A and HNF1B, enhancing their dimerization and transcriptional activity. The protein localizes to both the cytoplasm and nucleus, with nuclear recruitment mediated by interaction with HNF1B, underscoring its importance in gene regulation and metabolic pathways.