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  • Interaction of long-chain acyl-CoA analogs with pig kidney general acyl-CoA dehydrogenase.

Interaction of long-chain acyl-CoA analogs with pig kidney general acyl-CoA dehydrogenase.

European journal of biochemistry (1981-08-01)
C Thorpe, T L Ciardelli, C J Stewart, T Wieland
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
n-Heptadecanoyl coenzyme A lithium salt, ≥90%