CoA-persulphide: a possible in vivo inhibitor of mammalian short-chain acyl-CoA dehydrogenase

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Why is it important?

The short-chain acyl CoA dehydrogenase, involved either in beta oxidation or (in anaerobes) in production of butryate as an end-productof fermentation, is a flavoprotein, but typically is isolated not as a yellow protien but as a bright green protein. The significance of this colour was a puxxle for many years but we finally showed it is due to tightly bound CoA persulphide. This is in effect a very tightly bound competitive inhibitor that has to be kicked out by any incoming substrate molecule. The physiological significance of this potent inhibition remains to be explained.