When considering the malonyl-CoA substrate has a Km of ~2.5 mM the inhibition constants for the malonyl-CoA substrate analogs are respectable, Table . Recognizing that the kcat/KM for malonyl-ACP is 10,000 fold larger than that of malonyl-CoA, suggests appending the malonyl-thioester isosteres to the ACP will also engender them with tighter binding on the same order of magnitude.