| Primary Identifier | IPR017758 | Type | Family |
| Short Name | CoA_disulphide_reductase |
| description | Coenzyme A disulphide reductase () has been characterised in Staphylococcus aureus, Pyrococcus horikoshii, and Borrelia burgdorferi (Lyme disease spirochete), and inferred in several other species on the basis of high levels of CoA and an absence of glutathione as a protective thiol. Coenzyme A disulphide reductase specifically catalyses the NAD(P)H-dependent reduction of coenzyme A disulphide using FAD and NAD(P)H [, , ]. In some species the enzymes show a distinct preference for NADH or NADPH, while others can use either substrate equally well. The reduction of disulphides occurs by a thiol-disulphide exchange reaction, but involves only a single catalytic cysteine residue that forms a stable mixed disulphide with CoA during catalysis. This enzyme contains 2 FAD binding domains and a single NAD(P)H binding domain []. |
