This review reproduces the latest advances in the design of carnitine acyltransferase inhibitors, and provides only the background necessary for a fruitful discussion of the conformational behavior of the inhibitors mentioned below. Tetrahedral intermediate for Carnitine-CoA acyl transfer. Irreversible inhibitors eliminate enzymatic activity in such a way that the enzyme does not recover its original activity.
Reversible inhibitors allow the recovery of catalytic activity after elimination of the inhibitor.
Competitive inhibitors bind to the active site instead of the substrate, while noncompetitive inhibitors do not attach themselves to the active site, so the substrate can still bind to the enzyme. Competitive reversible inhibitors. Tipton and Chase justified the recognition of the S isomers by postulating a two-point recognition site that binds only to carboxylate and ammonium. Aminocarnitine Figure 2.2. Gandour et al.