Partial purification and characterization of two forms of malonyl-coenzyme A:acyl carrier protein transacylase from soybean leaf tissue.

Investigation of malonyl-CoA:acyl carrier protein transacylase from soybeans has shown that this fatty acid biosynthetic enzyme occurs in at least two isozymic forms. Both forms exist as soluble, low-molecular-mass polypeptides (approx 43 kDa) which catalyze one of the first committed steps in the synthesis of C16 and C18 fatty acids. We have partially purified the two forms of this enzyme from soybean leaf tissue 1200- and 3900-fold respectively. Isozyme 1 does not adhere to ion-exchange or blue dye affinity chromatographic supports and elutes from a polybuffer exchanger column at a pH of 7.3. Isozyme 2 requires salt to be eluted from ion-exchange and affinity matrices and elutes from a polybuffer exchanger column at a pH of 5.3. The two forms of malonyl-CoA:acyl carrier protein transacylase also differ in their sensitivity to catalytic inhibitors, heat treatment, and inhibition by acyl-CoA ester substrates. Both forms utilize malonyl-CoA as the preferred substrate, and polyacrylamide gel electrophoresis of reaction products indicated that malonyl-acyl carrier protein was the major product formed. Analysis of developing soybean seeds indicates that only one form (isozyme 1) is predominant, whereas leaf tissue possesses both isozymes.