Matsuura K, Nakayama T, Nakagawa M, Hara A, Sawada H
Department of Biochemistry, Gifu Pharmaceutical University, Japan.
Biochem J. 1988 May 15;252(1):17-22. doi: 10.1042/bj2520017.
The kinetic mechanism of guinea-pig lung carbonyl reductase was studied at pH 7 in the forward reaction with five carbonyl substrates and NAD(P)H and in the reverse reaction with propan-2-ol and NAD(P)+. In each case the enzyme mechanism was sequential, and product-inhibition studies were consistent with a di-iso ordered bi bi mechanism, in which NAD(P)H binds to the enzyme first and NAD(P)+ leaves last and the binding of cofactor induces isomerization. The kinetic and binding studies of the cofactors and several inhibitors such as pyrazole, benzoic acid, Cibacron Blue and benzamide indicate that the cofactor and Cibacron Blue bind to the free enzyme whereas the other inhibitors bind to the binary and/or ternary complexes.
在pH 7条件下，研究了豚鼠肺羰基还原酶在正向反应中与五种羰基底物及NAD(P)H的反应动力学机制，以及在逆向反应中与丙醇和NAD(P)+的反应动力学机制。在每种情况下，酶的作用机制都是有序的，产物抑制研究结果与双随机有序双底物双产物机制一致，即NAD(P)H首先与酶结合，NAD(P)+最后离开，辅因子的结合会诱导异构化。对辅因子和几种抑制剂（如吡唑、苯甲酸、汽巴克隆蓝和苯甲酰胺）的动力学和结合研究表明，辅因子和汽巴克隆蓝与游离酶结合，而其他抑制剂则与二元和/或三元复合物结合。
