Table 1.

Temperature dependence of enzyme kinetic parameters for the regioselective hydroxylation of mefenamic acid by P450 BM3 M11 and recombinant human CYP1A2 (i.e., for the formation of the products 3′‐hydroxymethylmefenamic acid, 4′‐hydroxymefenamic acid and 5‐hydroxymefenamic acid).

3′‐Hydroxymethylmefenamic acid				4′‐Hydroxymefenamic acid			5‐Hydroxymefenamic acid
T [K]	K M [μm]	V max [a]	V max/ K M [b]	K M [μm]	V max [a]	V max/ K M [b]	K M [μm]	V max [a]	V max/ K M [b]
P450 BM3 M11
277.0	72±16	135±10	1875	76±17	230±19	3026	77±22	24±3	312
283.4	140±18	212±9	1514	151±15	343±12	2271	124±19	34±2	274
290.2	161±14	561±44	3484	170±17	859±82	5053	148±15	85±8	574
292.7	145±45	498±33	3434	159±52	736±52	4628	188±37	72±4	383
298.6	85±20	463±33	5447	88±23	608±50	6909	86±25	64±7	744
304.4	266±56	607±53	2281	354±34	787±41	2223	409±165	81±7	198
313.3	556±200	358±28	644	603±150	431±37	714	384±202	42±5	109
317.6	388±184	194±19	500	538±34	208±14	387	762±118	21±2	27.6
CYP1A2
279.4	N.A.	N.A.	N.A.	204±118	0.56±0.13	2.75	6±2	0.50±0.02	83.3
287.7	N.A.	N.A.	N.A.	210±92	0.99±0.17	4.71	47±21	0.78±0.09	16.6
299.4	N.A.	N.A.	N.A.	144±68	0.91±0.18	6.88	42±7	0.67±0.03	16.0
309.8	N.A.	N.A.	N.A.	182±33	1.0±0.09	5.49	47±4	0.68±0.02	14.5

[a] Unit: (nmol product) min⁻¹ (nmol enzyme)⁻¹. [b] Unit: μL min⁻¹ (nmol enzyme)⁻¹. N.A.: not applicable.