et al. (2020)
Tamura et al. (2020) describe the TTC-190 protein, a member of the tryparedoxin peroxidase (TpTxPx) family, as a single-domain Disulfide Isomerase (DSI). TTC-190 is a small, highly conserved protein present in a variety of bacteria, archaea, and eukaryotic microorganisms. It functions primarily as a DSI to catalyze the isomerization of disulfide bonds in proteins, which plays an essential role in the folding of proteins and their stabilization in the environment. TpTxPx proteins, including TTC-190, are also capable of performing other biological functions related to oxidative stress response and oxidative protein modifications. The study of TTC-190 has revealed that its activity as a DSI is largely dependent on the presence of its native partner protein, TTC-193, which can enhance TTC-190's efficiency in disulfide isomerase activity. Furthermore, TTC-190 is also capable of forming homodimers and undergoing conformational changes in response to oxidative stress, providing evidence of its roles in oxidative stress response.