ABSTRACT
This chapter describes the early history of enzyme kinetics. Enzyme kinetics is the study of the chemical reactions that are catalyzed by enzyme. The goal of enzyme kinetics is to describe the catalytic mechanism of enzyme on the basis of kinetic data. By learning the history, you may understand the basis of enzyme kinetics. 2.1 Road to the Steady State KineticsBiochemistry books describe the Michaelis-Menten mechanism of the enzyme-catalyzed reaction. However, there were many works before the establishment of the mechanism [1, 2]. 2.1.1 Sucrose HydrolysisThe inversion of sucrose to glucose and fructose was easily monitored by a polarimeter. Sucrose is dextrorotatory (specific rotation: [a ] D25 = 66.5°). Glucose is dextrorotatory (α-d-glucose; [a ] D25 = 112.2°), and fructose (β-d-fructose, [a ] D25 = –132°) is levorotatory, and the whole products become levorotatory after mutarotation of each product. Thus, sucrose is inverted to the levorotatory products.
