GRX2

Glutaredoxin-2, mitochondrial

143 amino acids

Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX2 is more active as an oxidoreductase than GRX1.

Belongs to the glutaredoxin family.

15.861 kDa

METNFSFDSNLIVIIIITLFATRIIAKRFLSTPKMVSQETVAHVKDLIGQKEVFVAAKTYCPYCKATLSTLFQELNVPKSKALVLELDEMSNGSEIQDALEEISGQKTVPNVYINGKHIGGNSDLETLKKNGKLAEILKPVFQ

grx2

Glutaredoxin-2

110 amino acids

The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase. Thioltransferase catalyzes cellular thiol-disulfide transhydrogenation reactions. It transfers reducing equivalents to cytosolic protein and nonprotein disulfides (By similarity).

Belongs to the glutaredoxin family.

12.235 kDa

MTSIAKAFVEKAISNNPVTVFSKSFCPFCKAAKNTLTKYSAPYKAYELDKIENGSDIQAYLHEKTKQSTVPSIFFRNQFIGGNSDLNKLRSSGTLTKMIAELKENKSSIL