Figure 1.

A, Putative fatty acid-activating enzyme of Synechococcus was expressed in E. coli, purified, and analyzed by in vitro assays conducted in presence of radiolabeled palmitic acid, ATP, and either CoA or ACP as an acyl acceptor. Control measurements were performed either without protein (control I) or with protein denatured by boiling (control II). B, Substrate specificity of Aas of Synechococcus. Purified enzyme was tested in acyl-ACP activity assays using six different fatty acids. Each assay was performed in triplicate. The error bars represent the sd.