Fatty acid biosynthesis and the role of the acyl carrier protein.

TLDR: The marked substrate specificity of ACP hydrolase enzyme for intact ACP suggests a possible role for this enzyme in the control of fatty acid synthesis, by regulating the amount of ACp available, this enzyme could regulate fatty-acid synthesis.

Abstract: Publisher Summary This chapter discusses fatty acid biosynthesis and the role of the acyl carrier protein. The first indication that fatty acid synthesis is different from the β-oxidation pathway was the observation that bicarbonate is required for fatty acid synthesis in extracts from avian liver. The bicarbonate is required for the synthesis of malonyl CoA, and it is malonyl CoA that directly contributes the two-carbon units for the long-chain fatty acid. Malonyl CoA supplies all but the two methyl terminal carbons of long-chain fatty acids as shown by the stoichiometry experiments. Purification of this synthetase 200-fold demonstrates that all of the enzymes of fatty-acid synthesis were purified together in a single multienzyme complex. The marked substrate specificity of ACP hydrolase enzyme for intact ACP suggests a possible role for this enzyme in the control of fatty acid synthesis. Thus, by regulating the amount of ACP available, this enzyme could regulate fatty-acid synthesis.