Phytanoyl-CoA dioxygenase domain-containing protein 1 (PHYHD1)

Phytanoyl-CoA dioxygenase domain-containing protein 1 (**PHYHD1**) is a human enzyme belonging to the 2-oxoglutarate (2OG)-dependent dioxygenase superfamily[1][2][4][5]. It catalyzes the conversion of 2-oxoglutarate to succinate and CO₂, utilizing Fe²⁺ as a cofactor and exhibiting typical biochemical properties of this enzyme class, including inhibition by succinate and fumarate, and activation by citrate[1][2][5]. Despite its structural homology to phytanoyl-CoA hydroxylase, PHYHD1 does not catalyze the hydroxylation of acyl-CoA derivatives and is unlikely to participate directly in phytanoyl-CoA metabolism[1][2][5]. Subcellular localization studies place PHYHD1 in both the nucleus and cytoplasm[2][5]. Recent research suggests it may serve as an oxygen sensor and participate in RNA binding, with its enzymatic activity regulated by interactions with mRNA[2][5]. Protein-protein interaction and gene expression studies implicate PHYHD1 in pathways linked to cell division, RNA and carbohydrate metabolism, and possibly in disease contexts such as Alzheimer’s disease, certain cancers, and immune cell function[2][5][6]. Additional context: - There are multiple isoforms of PHYHD1, some of which likely lack enzymatic activity[1]. - It is not currently considered a therapeutic target; there are no approved drugs or clinical candidates acting directly on this protein[1][2][5]. - The gene/protein is well annotated in major databases (HGNC: 23396; NCBI Gene: 254295; UniProt: Q5SRE7)[1][2][4]. - Most functional knowledge is based on biochemical, structural, and model organism studies, with emerging links to human disease requiring further validation.

Other names

PHYHD1Phytanoyl-CoA dioxygenase domain containing 1Protein PHYHD1MGC16638phytanoyl-CoA dioxygenase domain-containing protein 1