<p>Coenzyme A disulphide reductase (<db_xref db="EC" dbkey="1.8.1.14"/>) has been characterised in <taxon tax_id="1280">Staphylococcus aureus</taxon>, <taxon tax_id="53953">Pyrococcus horikoshii</taxon>, and <taxon tax_id="139">Borrelia burgdorferi</taxon> (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 [<cite idref="PUB00044719"/>]. </p> Coenzyme A disulphide reductase