Abstract
This chapter presents a kinetic investigation study of liver microsomal mixed function amine oxidase. The liver microsomal FAD-containing monooxygenase (MFMO) (E.C.1.14.13.8) has been shown to have a wide substrate specificity, which includes secondary and tertiary amines, mercaptans, and thioureylenes, many of which are drugs and carcinogens. This chapter discusses a mechanism for this enzyme based upon both steady-state and rapid kinetic studies. In studies described in the chapter, MFMO was isolated from fresh hog livers. Both steady-state and rapid kinetic studies were carried out on a computerized stopped-flow apparatus. Results show that substrate greatly increases the rate of both NADPH and O 2 consumption by MFMO in normal assays. A large increase in reduction rate is observed upon addition of substrate or substrate analogs. However, substrate has no effect on the reduction rate of the flavin in MFMO. This fact coupled with the absence of any kind of perturbation of the oxidized enzyme spectrum by substrate led to the conclusion that substrate binds after FAD reduction.
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