2.3.1.179	C163Q	site-directed mutagenesis, interaction with platensimycin compared to the interaction with the wild-type enzyme	676148	
2.3.1.179	C164A	site-directed mutagenesis, inactive mutant	674581	
2.3.1.179	C164A/H337A	site-directed mutagenesis, inactive mutant	674581	
2.3.1.179	C164A/K332A	site-directed mutagenesis, inactive mutant	674581	
2.3.1.179	C164Q	site-directed mutagenesis, a mutant in which the binding site is altered to resemble the substrate-bound state	735397	
2.3.1.179	E122K	the mutant is less inhibited by cerulenin and platensimycin compared to the wild type enzyme and is resistant towards inhibition by acylated sulfonamides	-, 755804	
2.3.1.179	E346A	site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme	674581	
2.3.1.179	E383A	crystal structure determination and comparison to the wild-type enzyme, the mutation E383A appears to play a key role in disfavouring the less desirable triclinic crystal form and in generating a new surface for a packing interaction that stabilizes the new crystal form	701462	
2.3.1.179	E396A	site-directed mutagenesis, the mutant shows no condensation activity but retains about 50% of wild-type transacylation activity with acyl-ACP and ACP, and 40% of wild-type decarboxylation activity	674581	
2.3.1.179	F107I	less efficient than wild type protein	719275