Recombinant Human Glutaredoxin 5 protein (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Glutaredoxin 5 also known as GRX5 is a mitochondrial protein with a molecular mass of approximately 17 kDa. It efficiently catalyzes the reduction of disulfide bonds in substrate proteins through a thiol-disulfide exchange mechanism. GRX5 is highly expressed in tissues with active metabolism such as heart liver and skeletal muscles. This protein belongs to the glutaredoxin family which are small redox enzymes that use glutathione as a cofactor.

Biological function summary

The function of GRX5 revolves around iron-sulfur (Fe-S) cluster assembly. It is part of a multiprotein complex involved in the maturation of Fe-S proteins within the mitochondria. These iron-sulfur clusters are essential for various cellular processes including enzymatic functions and electron transport. The loss of GRX5 activity disrupts Fe-S cluster assembly leading to compromised cellular function and increased oxidative stress.

Pathways

GRX5 plays a significant role in the biosynthesis of Fe-S clusters. It is closely connected to the ISC assembly machinery an important pathway for the formation of these clusters. In this context GRX5 interacts with proteins such as ISCU and NFU1 contributing to the proper maturation and stability of Fe-S proteins which are pivotal for mitochondrial electron transport chain function and DNA repair mechanisms.

GRX5 dysregulation is linked to autosomal recessive sideroblastic anemia and mitochondrial dysfunction. This disorder results from defective Fe-S cluster biosynthesis leading to impaired haem synthesis and mitochondrial iron accumulation. GRX5's interaction with frataxin another protein involved in Fe-S cluster assembly further elucidates its role in the pathophysiology of diseases like Friedreich's ataxia where deficient iron-sulfur cluster synthesis leads to neurodegeneration and systemic abnormalities.