Cabanes J, Chazarra S, Garcia-Carmona F
Departamento de Bioquimíca y Biología Molecular A, Facultad de Veterinaria, Universidad de Murcia, Spain.
J Pharm Pharmacol. 1994 Dec;46(12):982-5. doi: 10.1111/j.2042-7158.1994.tb03253.x.
It was found that kojic acid, which is used in cosmetics for its excellent whitening effect, inhibits catecholase activity of tyrosinase in a non-classical manner. A decrease in the initial velocity to a steady-state inhibited velocity can be observed over a few minutes. This time-dependence, which is unaltered by prior incubation of the enzyme with the inhibitor, is consistent with a first-order transition. The kinetic data obtained correspond to those for a postulated mechanism that involves the rapid formation of an enzyme inhibitor complex that subsequently undergoes a relatively slow reversible reaction. Kinetic parameters characterizing this type of inhibition were evaluated by means of nonlinear regression of product accumulation curves.
据发现，用于化妆品中因其出色美白效果的曲酸，以非经典方式抑制酪氨酸酶的儿茶酚酶活性。在几分钟内可以观察到初始速度降至稳态抑制速度。这种时间依赖性不受酶与抑制剂预先孵育的影响，与一级转变一致。所获得的动力学数据与一种假设机制的数据相符，该机制涉及快速形成酶抑制剂复合物，随后该复合物经历相对缓慢的可逆反应。通过产物积累曲线的非线性回归评估表征这种抑制类型的动力学参数。
