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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 and enzyme catalysis, utilizing octanoyl-CoA/octenoyl-CoA as a physiological substrate/product pair a
6 ies, we discerned that formation of the MCAD-octenoyl-CoA complex, at pH 7.6, accompanies abstraction
7 CoA complex is similar to that of the enzyme-octenoyl-CoA complex, their microscopic equilibria withi
9 '-dephosphorylated forms of octanoyl-CoA and octenoyl-CoA (cumulatively referred to as C8-CoA) as the
10 the deletion of the 3'-phosphate group from octenoyl-CoA increased the magnitude of the heat capacit
14 endence of the association constant of MCAD +octenoyl-CoA <==> MCAD-octenoyl-CoA yields a pKa for the
15 zed by the stoichiometry (n) of 0.89 mole of octenoyl-CoA/(mole of MCAD subunit), delta G = -8.75 kca
16 CoA-ligands, viz., octanoyl-CoA (substrate), octenoyl-CoA (product), and octynoyl-CoA (inactivator) w
17 protein catalyzed the isomerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific act
18 an PECI catalyzed the isomerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific act
19 ), attesting to the fact that the binding of octenoyl-CoA to MCAD is primarily dominated by the hydro
20 that the DeltaCp degrees for the binding of octenoyl-CoA to pig kidney MCAD (which is believed to be
22 t on the above properties for the binding of octenoyl-CoA to the enzyme, it had pronounced effects (a
23 omerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific activity of 16 units/mg.
24 omerization of 3-cis-octenoyl-CoA to 2-trans-octenoyl-CoA with a specific activity of 27 units/mg of
25 ion constant of MCAD +octenoyl-CoA <==> MCAD-octenoyl-CoA yields a pKa for the free enzyme of 6.2.
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