. 2017 Nov 22;59(1):79–88. doi: 10.1194/jlr.M079806

TABLE 4.

Kinetic analysis of each recombinant TpFADS2 and GcFADS2 by mutating amino acids

					Mutants
	Fatty acid	TpFADS2	V295T	T299S	L303F	I306L	A315S	H360D	F368Y	S377M/L378M	H381N	L383I
V_max ^a	18:2 (LA)	0.40	0.34	0.63	0.48	0.29	0.41	0.34	0.61	1.19	0.44	0.51
V_max ^a	18:3 (ALA)	0.54	0.32	0.83	0.56	0.72	0.27	0.54	0.34	0.91	0.71	0.55
K_m^a	18:2 (LA)	187.66	1544.62	627.58	388.28	427.59	1584.02	299.32	2556.04	3547.49	268.73	394.04
K_m^a	18:3 (ALA)	250.52	1243.70	691.91	495.87	739.78	1464.57	458.76	4412.12	2244.97	521.88	458.13
					Mutants
	Fatty acid	GcFADS2	T302V	S306T	F310L	L313I	S322A	D367H	Y375F	M384S/M385L	N388H	I390L
V_max^a	18:2 (LA)	0.12	0.07	0.13	0.13	0.07	0.10	0.09	0.06	0.10	0.22	0.51
V_max^a	18:3 (ALA)	0.27	0.07	0.26	0.23	0.12	0.11	0.13	0.07	0.08	0.19	0.16
^a	18:2 (LA)	1268.06	36.98	1340.53	1399.73	1020.82	159.35	1282.81	106.54	321.97	2182.43	6375.00
^a	18:3 (ALA)	2315.63	23.87	2621.65	2812.50	1250.00	129.31	1519.23	89.41	123.64	1821.43	4403.13

V_max and K_m were calculated by the Michaelis-Menten equation. Bold text indicates sites identified to critically influence FADS2 catalytic activity.