michaelis constant

Michaelis & amp？ Menteng? 19 13 deduces the mathematical expression of the above rectangular hyperbola, that is, Michaelis equation:? ν=? Vmax[ sec]/(Km+[sec]), where Vmax is the maximum reaction speed and km is Michaelis constant.

Traditionally, Michaelis equation dynamics describes the behavior of collective molecules with molecular number 10 15, and Michaelis equation is also effective at the single molecular level.

⑶ The significance of km and Vmax:?

① When ν=Vmax/2, Km=[S]. Therefore, when the enzymatic reaction rate reaches half the maximum, Km is equal to the substrate concentration. ?

② when k- 1 >; & gt when k+2, Km=k- 1/k+ 1=Ks. Therefore, Km can reflect the affinity between enzyme and substrate, that is, the smaller the Km value, the greater the affinity between enzyme and substrate; On the contrary, the smaller. ?

③Km can be used to judge the reaction sequence: when [s]; When 100Km, ν=Vmax, the reaction is zero order, that is, the reaction speed is independent of the substrate concentration; When 0.01km <