The effects of substrates on the optical rotatory dipersion of carnitine acetyltransferase.
1. The optical rotatory dispersion of carnitine acetyltransferase is altered in the presence of l-carnitine or acetyl-l-carnitine. These changes, which include an increase in the reduced mean residue rotation at 233nm. ([M'](233)), suggest that substrate binding causes the enzyme to unfold. 2. CoA and acetyl-CoA have no immediate effect on [M'](233) and CoA has no effect on the change in this parameter induced by l-carnitine. 3. The change in [M'](233) was used as a measure of the degree of saturation of the enzyme with carnitine substrates. Dissociation constants for the enzyme complexes with l-carnitine, d-carnitine and acetyl-l-carnitine were determined in this way. 4. Prolonged incubation of carnitine acetyltransferase in the presence of CoA leads to a small increase in the value of [M'](233) accompanied by irreversible inhibition of the enzyme. 5. Optical-rotatory-dispersion studies of two specifically inhibited enzyme forms are reported.
D000217:Acyltransferases / Q000037:antagonists & inhibitors; D001665:Binding Sites; D002331:Carnitine; D003065:Coenzyme A / Q000494:pharmacology; D007700:Kinetics; D009905:Optical Rotatory Dispersion; D013237:Stereoisomerism
D000217:Acyltransferases; D002331:Carnitine; D003065:Coenzyme A