Table 2.
Inhibitor | |||||||
---|---|---|---|---|---|---|---|
1c |
1j |
||||||
Conc. | Vmax (mM/min) | KM (mM) | Ki (M) | Conc. | Vmax (mM/min) | KM (mM) | Ki (M) |
2.5 μM | 4.0 × 10−2 | 6.56 | 3.02 × 10−6 | 5.0 μM | 2.7 × 10−2 | 5.47 | 5.85 × 10−6 |
5.0 μM | 4.0 × 10−2 | 10.72 | 2.51 × 10−6 | 10.0 μM | 2.7 × 10−2 | 9.48 | 4.51 × 10−6 |
10.0 μM | 4.0 × 10−2 | 19.93 | 2.19 × 10−6 | 20.0 μM | 2.7 × 10−2 | 21.26 | 3.22 × 10−6 |
Data are mean values of 1/V (inverse of the increase in absorbance at a wavelength of 475 nm per min (ΔA475/min)), of three independent experiments conducted using different L-tyrosine concentrations. The Lineweaver-Burk plot equation is: 1/V = 1/Vmax + KM/Vmax × 1/[S] and the modified Michaelis-Menten equation is 1/Vmax = (1 + [I]/Ki) × 1/KM, where V is the reaction rate, Vmax is the maximum reaction rate, KM is the Michaelis-Menten constant, [S] is substrate concentration, [I] is inhibitor concentration, and Ki is the inhibition constant.