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Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA

Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA

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WENZ, Alexandra, Sandro GHISLA, Colin THORPE, 1985. Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA. In: European Journal of Biochemistry. 147(3), pp. 553-560. ISSN 0014-2956. eISSN 1432-1033

@article{Wenz1985Studi-7298, title={Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA}, year={1985}, number={3}, volume={147}, issn={0014-2956}, journal={European Journal of Biochemistry}, pages={553--560}, author={Wenz, Alexandra and Ghisla, Sandro and Thorpe, Colin} }

application/pdf 2011-03-24T17:33:20Z Wenz, Alexandra First publ. in: European Journal of Biochemistry 147 (1985), 3, pp. 553-560 1985 Ghisla, Sandro 2011-03-24T17:33:20Z terms-of-use Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA 3,4-Pentadienoyl-CoA, an allenic substrate analog, is a potent inhibitor of the flavoprotein pig-kidney general acyl-CoA dehydrogenase. The analog reacts very rapidly (k = 2.4 x 103 min -1) with the native oxidized enzyme to form a covalent flavin adduct probably involving the isoalloxazine position N-5. This species is inactive, but activity may be regained by two pathways. The allenic thioester can be displaced (k = 0.3 min - 1) by a large excess of octanoyl-CoA substrate upon reversal of covalent adduct formation. Alternatively, the enzyme inactivator adduct slowly decomposes (t 111 = 75 min) to form the strongly thermodynamically favoured 2,4-diene and catalytically active, oxidized enzyme. During this latter process 15-20% of the activity is irreversibly lost probably due to covalent modification of the protein. These data suggest that 3,4-pentadienoyl-CoA should be considered a suicide substrate of the acyl-CoA dehydrogenase. The mechanism of the reactions, and in particular the 3,4->2,4 tautomerization, are consistent with a catalytic sequence initiated by abstraction of an a-hydrogen as a proton. Ghisla, Sandro eng Thorpe, Colin Wenz, Alexandra Thorpe, Colin

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