TABLE 2

Kinetic parameters of MBA and KET for the isoform markers in DLM, recombinant CYP3A12, and CYP2B11

I	E	S	P	K_i (S.D.)^a	K_I (S.D.)^b	k_inact (S.D.)^c	IC₅₀ (S.D.)^d
KET	DLM	PHE	ACE				N.E.
	DLM	DIC	4′-OH				N.E.
	DLM	BUF	1′-OH				2.5
	2B11	DZ	NDZ	31.5 (10.1)			N.E.
	3A12	DZ	TMZ	0.33 (0.06)			0.1
	DLM	DZ	NDZ	14.4 (2.9)			N.E.
	DLM	DZ	TMZ	0.13 (0.02)			0.12
MBA	DLM	PHE	ACE				N.E.
	DLM	DIC	4′-OH				N.E.
	DLM	BUF	1′-OH				N.E.
	2B11	DZ	NDZ		0.35 (0.3)	1.5 (0.4)	0.15
	3A12	DZ	TMZ	5.6 (0.3)			N.E.
	DLM	DZ	NDZ		0.46 (0.39)	0.56 (0.29)	0.1
	DLM	DZ	TMZ	8.4 (1.2)			N.E.

I, inhibitor; E, enzyme source; S, substrate used; P, product formed; N.E., no inhibitory effect.
↵ a K_i, micromolar (S.D.), dissociation constant for reversible inhibition; ^bK_I, micromolar (S.D.), dissociation constant for mechanism-based inhibition; ^ck_inact, minutes (S.D.), inactivation velocity constant for mechanism-based inhibition; ^d IC₅₀, micromolar, a concentration at 50% maximum inhibition of the reaction.