Open AccessInteraction of Long‐Chain Acyl‐CoA Analogs with Pig Kidney General Acyl‐CoA Dehydrogenase
Author(s) -
THORPE Colin,
CIARDELLI Thomas L.,
STEWART Charles J.,
WIELAND Theodor
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb06397.x
Subject(s) - thioether , chemistry , dehydrogenation , acyl coa dehydrogenase , coenzyme a , stereochemistry , acyl coa , dehydrogenase , substrate (aquarium) , acylation , enzyme , biochemistry , carbanion , biology , catalysis , ecology , reductase
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 flavoprotein was observed spectrophotometrically using the flavin as an active‐site probe. The S ‐heptadecyl thioether analog bound strongly to the enzyme ( K d = 17 nM) and was a powerful competitive inhibitor ( K i < 40 nM). In contrast to the thioether analog, the dethiocarba derivative, heptadecan‐2‐onyl‐dethio‐CoA, was a substrate in the standard assay system being dehydrogenated at about 60% of the rate shown by palmitoyl‐CoA. These results support the proposal that α‐carbanion formation is an early event in the dehydrogenation of acyl‐CoA substrates.