Additional proteins belong to the thioredoxin superfamily because they possess a thioredoxin domain. This superfamily encompasses five major groups of proteins: thioredoxins, glutaredoxins (GRX), protein disulfide isomerases (PDI), glutathione peroxidases, and glutathione-S-transferases. Sign in to ...
The amino acid sequence placed the enzyme in the thioredoxin-like superfamily with Cys44 being the active site. The enzyme expressed in Escherichia coli as well as the native enzyme catalyzed not only the reduction of prostamide H2 to prostamide F2α, but also that of PGH2 to PGF2α. The...
These sequences had high homology to those of proteins belonging to the thioredoxin-like superfamily and had CXXC, which is basically the active site of the enzymes belonging to the thioredoxin-like superfamily. Fig. 3 shows SDS-PAGE (Fig. 3A) and Western blot (Fig. 3B) results for each ...
Human thioredoxin-like protein (txl) is a novel member of the expanding thioredoxin superfamily whose main characteristic is the presence, after the thioredoxin domain, of a C-terminal extension of 184 residues with no homology with any other protein in the databases. Txl is a cytosolic ...
Structural and Functional Characterization of a Thioredoxin-Like Protein (Mt0807) from Methanobacterium thermoautotrophicum † members of the thioredoxin superfamily indicate that Mt0807 actually has several key structural and active-site characteristics more common to a thioredoxin. ... GY Amegbey,H ...
Thioredoxin transmembrane related protein (TMX), a member of thioredoxin superfamily, is localized to the endoplasmic reticulum and possesses a thioredoxin-like domain that plays an important role as an oxidoreductase. The functions of TMX in CsTMX cDNA sequence contained a 414-nucleotide open-reading...
In turn, TRAF6 is a critical regulator of NF-κB and the MAPK route during the activation mediated by the superfamily of the TNF receptor and of the family of Toll/IL-1 receptors. TRAF6 is also recruited to the ASK1 signalosome by the presence of H2O2, suggesting that the ROS-dependent ...
Thioredoxins represent ubiquitous small proteins acting as redox regulators of diverse metabolic and developmental processes in almost all organisms. These proteins contain highly conserved cysteines in their redox-active sites, which enable the modifica
The dimerization interface identified in ERp29 has so far not been observed in the thioredoxin superfamily. For example, human thioredoxin requires an intermolecular disulfide bridge for dimer formation 45, 46, and the intermolecular contacts observed in the single crystal of calsequestrin involve more ...
Thioredoxin is the best characterized of these and belongs to a superfamily of proteins that contain an active site CX1X2C motif and share a similar fold, in those cases where structure is known (18). The redox potential of thioredoxin is low (−270 mV) (19) and, in vitro, thioredoxin...