3.4.21.21	306X	mutation studies show that the interaction between protein cofactor tissue factor and methionine-306 in the serine protease domain of FVIIa triggers the activation process and suggested some ensuing steps on the pathway to the active conformation	710606	
3.4.21.21	A294V	mutant enzyme shows delayed activation by activated factor X as well as reduced activity towards peptidyl and macromolecular substrates without impairing the catalytic efficiency of the triad	654496	
3.4.21.21	C164V/V299C-FVIIa	introduction of a new disulfide bridge between Cys-159 and an introduced Cys at position 299	667588	
3.4.21.21	D102Q	inactive mutant enzyme	654583	
3.4.21.21	D186A	turnover-number for activation of factor X is 5.5fold lower than that of the wild-type factor VII, Km-value for activation of factor X is 1.2fold lower than that of the wild-type factor VII	654583	
3.4.21.21	D343H	mutant enzyme shows no activity with methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide, factor X and factor IX	654508	
3.4.21.21	D72N	the mutant shows 13% of wild type FVIIa signaling activity towards protease-activated receptor 2	717790	
3.4.21.21	DELTA360-329	lower affinity for soluble tissue factor as compared to wild-type factor VIIa, 7fold smaller tissue factor-mediated acceleration of amidolytic activity compared to wild type factor VIIa	656000	
3.4.21.21	E154A	slightly increased Km-value and decreased turnover number compared to the wild-type enzyme	95334	
3.4.21.21	E154R	site-directed mutagenesis, activity and active site structure in comparison to the wild-type	683477