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- W1567205350 abstract "Abstract The coenzyme A thioesters of cinnamic acid, cyclohexene-1-carboxylic acid, and of three halocrotonic acids are reported as new substrates of bovine liver crotonase. From the kinetic parameters of the halocrotonyl derivatives, comparisons are made with the action of fumarase on analogous halofumarates. One of the five cysteinyl residues per subunit of crotonase is shown to be unessential for catalysis, although it is hyperreactive toward a variety of sulfhydryl reagents. If this reactive sulfhydryl group is first blocked by formation of its carboxyethyl-mixed disulfide, incubation with p-bromoacetamido-trans-cinnamoyl coenzyme A results in selective alkylation of 1 of the 4 remaining cysteinyl residues per subunit. Activity loss is linearly related with alkylation of the 2nd residue, which appears to be in the vicinity of the substrate binding site. It is proposed that this second sulfhydryl group is not essential for catalysis, and that the inactivation accompanying its modification results from simple steric blockage of the substrate binding site. The covalently bound substrate analog thus appears to behave as an efficient competitive inhibitor, whose Ki is effectively zero." @default.
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- W1567205350 date "1973-02-01" @default.
- W1567205350 modified "2023-10-01" @default.
- W1567205350 title "Bovine Liver Crotonase" @default.
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- W1567205350 doi "https://doi.org/10.1016/s0021-9258(19)44351-2" @default.
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