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  • Title: Interaction of long-chain acyl-CoA analogs with pig kidney general acyl-CoA dehydrogenase.
    Author: Thorpe C, Ciardelli TL, Stewart CJ, Wieland T.
    Journal: Eur J Biochem; 1981 Aug; 118(2):279-82. PubMed ID: 7285923.
    Abstract:
    The interaction of two long-chain acyl-CoA analogs with pig kidney general acyl-CoA dehydrogenase (EC 1.3.99,3) was examined. The effect of S-heptadecyl-CoA and heptadecan-2-onyl-dethio-CoA on the flavo-protein was observed spectrophotometrically using the flavin as an active-site probe. The S-heptadecyl thioether analog bound strongly to the enzyme (Kd = 17 nM) and was a powerful competitive inhibitor (Ki less than 40 nM). In contrast to the thioether analog, the dethiocarba derivative, heptadecan-2-onyl-dethio-CoA, was a substrate inthe standard assay system being dehydrogenated at about 60% of the rate shown by palmitoyl-CoA. These results support the proposal that alpha-carbanion formation is an early event in the dehydrogenation of acyl-CoA substrates.
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