Thioredoxins are small proteins involved in thiol-redox processes. They contain two redox-active cysteine residues in their active sites, usually in a CXXC motif. The thioredoxins are kept in the reduced state by the flavoenzyme thioredoxin reductase, in a NADPH-dependent reaction. Thioredoxins act as electron donors to peroxidases and ribonucleotide reductase.

See also

• RuBisCO - enzyme activity regulated by thioredoxin

External links

• Pfam database - thioredoxin. http://pfam.wustl.edu/cgi-bin/getdesc?acc=PF00085