Table 1. Catalytic and Substrate Binding Properties of Most Representative ART-Hydroxylating P450_BM3 Variants^a.

	amino acid substitutionsb							prod distribution (%)						.
variant	74	78	81	82	87	181	184	2	3	4	TTN	KD (μM)	prod formation ratec	coupling efficd (%)
FL#62	A	A	S	V	A	L	V	83	10	7	339 ± 12	29 ± 5	316 ± 20	41.9
IV-H4		S	V	A				100	0	0	362 ± 15	53 ± 11	100 ± 4	71.4
V-H2		S	I	A				96	0	4	434 ± 21	45 ± 10	41 ± 2	23.5
II-H10		N	F	T	F	F	T	0	100	0	270 ± 08	61 ± 2	32 ± 2	12.8
III-B1		F	F	A				19	81	0	403 ± 17	38 ± 2	72 ± 2	23.3
II-E2		N	F	A				22	30	48	393 ± 25	164 ± 18	148 ± 3	38.2
X-E12	V	N	F	A		A	T	4	2	94	113 ± 12	300 ± 24	72 ± 3	45.1
X-F11	T	N	F	A			S	0	8	92	376 ± 19	234 ± 29	56 ± 2	56.3

^aMean values and standard deviations are calculated from triplicate experiments.

^bMutations in FL#62 vs P450_BM3 are V78A, F81S, A82 V, F87A, P142S, T175I, A180T, A184V, A197V, F205C, S226R, H236Q, E252G, R255S, A290V, L353V.

^cMoles of product per mole of P450 per minute. Rates are measured over initial 30 s.

^dRatio between product formation rate and NADPH oxidation rate in the presence of artemisinin.