Target intelligence / Profile preview

Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 (PYROXD2)

Target
PYROXD2
Molecular classification
Enzyme, Oxidoreductase (specifically, predicted to be involved in redox reactions utilizing pyridine nucleotides and disulfide bonds)
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Overview

Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 (PYROXD2) is a protein-coding gene product localized primarily to the mitochondrial inner membrane and matrix. It is predicted to have oxidoreductase activity, acting on sulfur group donors and is imported into mitochondria via Tom40 and Tim23 import machinery. PYROXD2 is involved in regulating mitochondrial function—specifically, it interacts with complex IV subunit COX5B, and is required for normal mitochondrial membrane potential, redox balance, ATP production, mtDNA copy number, and the maturity of mitochondria. Knocking out PYROXD2 impairs these functions and results in increased mitochondrial ROS levels and immature mitochondria. Disease associations include dimethylglycine dehydrogenase deficiency, trimethylaminuria, and altered expression is observed in hepatocellular carcinoma. While its biochemical role as an oxidoreductase is established, PYROXD2 is not currently used as a therapeutic target or biomarker

Other names
PYROXD2Pyridine nucleotide-disulphide oxidoreductase domain 2Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2C10orf33FLJ23849FP3420YUEF
02

Mechanism of action

Not applicable, as there are no described drugs targeting PYROXD2

03

Biological functions

Mitochondrion organization and functionRegulation of mitochondrial membrane potential, reactive oxygen species (ROS) levels, complex IV activity (interacts with COX5B, a subunit of cytochrome c oxidase)Involved in regulation of cell proliferation and mitochondrial maturityPredicted oxidoreductase activity, likely involved in the redox homeostasis of the mitochondrial matrix
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Disease associations

Associated (not directly causal) with Dimethylglycine dehydrogenase deficiencyAssociated with TrimethylaminuriaAltered expression in hepatocellular carcinoma (HCC): significantly downregulated, suggesting possible involvement in tumor suppression or mitochondrial dysregulation in cancer
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Safety considerations

Not documented for therapeutic intervention, as the target is not presently a drug target; dysfunction may affect mitochondrial health and cellular redox balance, but no therapeutic safety profile is available

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