Reaction | K_{S1}^{5-b} | K_{S2}^{5-b} | V_{max}^{5-b} | Factor^{5-b} | Equation^{5-b} |
---|---|---|---|---|---|
μM | nmol/min/nmol | ||||
Quinidine 3-hydroxylation | 1.3 ± 0.2 | 63.3 ± 9.6 | 5.8 ± 0.3 | 0.6 ± 0.4 | 1 |
(V _{maxQ}) | (α) | ||||
Diclofenac 5-hydroxylation | 1.4 ± 0.2 | 54.2 ± 4.5 | 10.5 ± 1.5 | 5.9 ± 0.8 | 2 |
(V _{maxD}) | (β) |
↵5-a The kinetic model is shown in Fig. 2 and equations are described under Experimental Procedures.
↵5-b V_{maxQ} andV_{maxD} are the maximum velocities for the formation of 3-hydroxyquinidine and 5-hydroxydiclofenac, respectively;K_{S1} is the dissociation constant for E⇌ ES_{1} and K_{S2} for E⇌ ES_{2}; α and β are the factors by whichV_{max} values increase (or decrease) when the second substrate is included in the interaction with the enzyme. Data are presented as mean ± S.E.