人红细胞NADH：（受体）氧化还原酶。动力学性质及铁氰化物对底物的竞争性抑制作用

Human erythrocyte NADH: (acceptor) oxidoreductase. Kinetic properties and competitive substrate inhibition by ferricyanide.

作者信息

Wang C S

出版信息

Biochim Biophys Acta. 1980 Nov 6;616(1):22-9. doi: 10.1016/0005-2744(80)90259-4.

Abstract

The kinetic mechanism of human erythrocyte membrane NADH: (acceptor) oxidoreductase (EC 1.6.99.3) was studied by product and substrate inhibition kinetics. With ferricyanide as the substrate, the enzyme reaction follows an ordered bi-bi reaction mechanism. The Michaelis-Menten constants for NADH and ferricyanide are 0.014 and 0.049 mM, respectively. The competitive substrate inhibition effect of ferricyanide was due to its direct binding to the enzyme and forming an inactive binary complex. The dissociation constant of the complex was determined to be 0.37 mM.

摘要

通过产物抑制和底物抑制动力学研究了人红细胞膜NADH：（受体）氧化还原酶（EC 1.6.99.3）的动力学机制。以铁氰化物作为底物时，酶反应遵循有序的双底物双产物反应机制。NADH和铁氰化物的米氏常数分别为0.014和0.049 mM。铁氰化物的竞争性底物抑制作用是由于其直接与酶结合并形成无活性的二元复合物。该复合物的解离常数测定为0.37 mM。