4.2.1.17	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O	-	
4.2.1.17	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O	reaction mechanism, overview	
4.2.1.17	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O	reaction mechansim of enoyl-CoA hydration, overview	
4.2.1.17	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O	the CoA moiety of the substrate adopts the typical horseshoe conformation in a binding pocket formed from two adjacent monomers, while the active site catalytic residues are provided by a single monomer. The active site of rat liver mitochondrial ECH contains an oxyanion hole formed from the backbone amides of Gly141 and Ala98, which serves to polarize the carbonyl group of the alpha,beta-unsaturated enoyl-CoA substrate and stabilize the enolate intermediate. Two active site glutamate residues (Glu144 and Glu164) are proposed to act as a general base(s) for the conjugate addition of water onto the substrate enone and to protonate the resultant enolate