Pyridine nucleotide-disulphide oxidoreductase domain-containing protein 1 (PYROXD1)

Pyridine nucleotide-disulphide oxidoreductase domain-containing protein 1 (PYROXD1) is a nuclear-cytoplasmic flavoprotein oxidoreductase involved in the maintenance of cellular redox homeostasis, particularly by catalyzing pyridine nucleotide-dependent reduction of protein thiols and participating in response to oxidative stress[1][2]. It directly protects the catalytic subunit (RTCB) of the human tRNA ligase complex against oxidative inactivation through a mechanism involving NAD(P)H- and FAD-dependent redox cycling and regulated protein–protein interaction[2]. PYROXD1 is localized in the nucleus and striated muscle compartments and is essential for normal sarcomere structure and muscle fiber integrity. Loss-of-function mutations are associated with early-onset myopathies characterized by internalized myonuclei and disorganized myofibrils[1]. PYROXD1 is not currently recognized as a therapeutic drug target, and no direct interacting drugs or established therapeutic mechanisms are known.

Other names

Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1PYROXD1DKFZp762G094FLJ22028MFM8pyridine nucleotide-disulfide oxidoreductase domain 1