Disease relevance of thioredoxin

• HGCP-Iv, produced in Escherichia coli as a fusion protein with thioredoxin, degrades the synthetic peptide benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin and is inhibited by E-64, a substrate and inhibitor commonly used for functional characterization of CPs [1].

High impact information on thioredoxin

• A novel thioredoxin-like protein encoded by the C. elegans dpy-11 gene is required for body and sensory organ morphogenesis [2].
• ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress [3].
• Glutathione was the only thiol tested that served as a substrate for the enzyme, which showed no activity with the thioredoxin system (thioredoxin, thioredoxin reductase, and NADPH) [4].
• Thioredoxin (TRX) is generally a 12-kDa protein-disulfide reductase [5].
• Lifespan decrease in a Caenorhabditis elegans mutant lacking TRX-1, a thioredoxin expressed in ASJ sensory neurons [6].

Biological context of thioredoxin

• By site-directed mutagenesis the second cysteine residue of the -CysGlyHisCys- motif in the thioredoxin domain of the enzyme protein was found to be the active site of the transamidation reaction and chemical modification of histidine in their motif blocked TGase activity [7].
• This suggests that SSP411 may play a role in sperm maturation, fertilization, and/or embryo development, as has been shown in thioredoxin family [8].

Anatomical context of thioredoxin

• In summary, we have identified a new rat spermatid protein gene, ssp411, and its orthologs in human and mouse and demonstrated that SSP411 might belong to a testis-specific thioredoxin family [8].

Associations of thioredoxin with chemical compounds

• Transglutaminases (TGases) are a family of enzymes that share catalytic function with thioredoxin and protein disulphide isomerases (PDI) and catalyze protein crosslink reaction by establishing epsilon-(gamma-glutamyl)lysine isopeptide bonds [9].

References