Thioredoxin is a small dithiol protein and specific reductant for major allergenic proteins present in foods from animal and plant products. It is a 12-kD oxidoreductase enzyme encoded by TXN and TXN2 genes that contains a dithiol-disulfide active site. It plays an essential role as an antioxidant in neutralizing food allergens and redox signalling. Allergens containing disulfide bonds are inactivated when reduced by thioredoxin.
Examples of Clinical Use:
Mechanism of action:
The primary function of Thioredoxin (Trx) is the reduction of oxidized cysteine residues and the cleavage of disulfide bonds. For Trx1, this process begins by attack of Cys32, one of the residues conserved in the thioredoxin CXXC motif, onto the oxidized group of the substrate. Almost immediately after this event Cys35, the other conserved Cys residue in Trx1, forms a disulfide bond with Cys32, thereby transferring 2 electrons to the substrate which is now in its reduced form. Oxidized Trx1 is then reduced by thioredoxin reductase, which in turn is reduced by NADPH as described above.
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