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1 tes for the binding of the reaction product, octenoyl-CoA.
2 urally different types of CoA-ligands (viz., octenoyl-CoA, acetoacetyl-CoA, and indoleacryloyl-CoA) t
3 endence of DeltaH degrees for the binding of octenoyl-CoA and 3'-dephosphooctenoyl-CoA revealed that
4 t decrease in hepatic acyl-CoA levels, while octenoyl-CoA and dicarboxylic acid levels increased.
5 and enzyme catalysis, utilizing octanoyl-CoA/octenoyl-CoA as a physiological substrate/product pair a
6                                    Moreover, octenoyl-CoA blocked the hydration of crotonyl-CoA sugge
7                     The reduction of trans-2-octenoyl-CoA catalyzed by InhA resulted in the syn addit
8 ies, we discerned that formation of the MCAD-octenoyl-CoA complex, at pH 7.6, accompanies abstraction
9 CoA complex is similar to that of the enzyme-octenoyl-CoA complex, their microscopic equilibria withi
10 termined for Glu376 in the human MCAD.4-thia-octenoyl-CoA complex.
11 '-dephosphorylated forms of octanoyl-CoA and octenoyl-CoA (cumulatively referred to as C8-CoA) as the
12  the deletion of the 3'-phosphate group from octenoyl-CoA increased the magnitude of the heat capacit
13 nd temperature on the thermodynamics of MCAD-octenoyl-CoA interaction.
14 ndent reductive half-reaction and the enzyme-octenoyl-CoA interaction.
15 -1) K(-1), suggesting that formation of MCAD-octenoyl-CoA is enthalpically driven.
16 incomplete B-oxidation, and the accumulation octenoyl-CoA levels that inhibited the activity of short
17 endence of the association constant of MCAD +octenoyl-CoA <==> MCAD-octenoyl-CoA yields a pKa for the
18 zed by the stoichiometry (n) of 0.89 mole of octenoyl-CoA/(mole of MCAD subunit), delta G = -8.75 kca
19 CoA-ligands, viz., octanoyl-CoA (substrate), octenoyl-CoA (product), and octynoyl-CoA (inactivator) w
20 protein catalyzed the isomerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific act
21 an PECI catalyzed the isomerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific act
22 ), attesting to the fact that the binding of octenoyl-CoA to MCAD is primarily dominated by the hydro
23  that the DeltaCp degrees for the binding of octenoyl-CoA to pig kidney MCAD (which is believed to be
24               We investigated the binding of octenoyl-CoA to pig kidney medium chain acyl-CoA dehydro
25 t on the above properties for the binding of octenoyl-CoA to the enzyme, it had pronounced effects (a
26 omerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific activity of 16 units/mg.
27 omerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific activity of 27 units/mg of
28 ion constant of MCAD +octenoyl-CoA <==> MCAD-octenoyl-CoA yields a pKa for the free enzyme of 6.2.