Purification and Characteristics of a Butyryl Coenzyme a Synthetase from Bovine Heart Mitochondria.

During the purification of acetyl coenzyme A synthetase from bovine heart mitochondria it was noted that cruder preparations catalyzed appreciable butyrate-dependent disappearance of coenzyme A; activity toward butyrate disappeared from the acetate enzyme during advanced stages of the fractionation procedure (1). The present report describes the purification of a butyryl-CoA synthetase from bovine heart mitochondria. It was found that this enzyme has a different spectrum of substrate specificity than that described either for the acetate enzyme isolated from this source or for the intermediate fatty acyl-CoA synthetases of liver and kidney mitochondria (2, 3). Other distinguishing features of the butyrate enzyme of heart muscle are described also.