Disulphide oxidoreductase (DsbA) is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope. It is a member of the thioredoxin superfamily. DsbA introduces disulfide bonds directly into substrate proteins by donating the disulfide bond in its active site Cys30-Pro31-His32-Cys33 to a pair of cysteines in substrate proteins. DsbA is reoxidized by dsbB. It is required for pilus biogenesis.
SDS-PAGE - Disulphide oxidoreductase protein (ab51282)
ab51282 run on a 15% SDS-PAGE gel with molecular weight markers.
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