第8章生化 (刘建华).ppt

In the random sequential mechanism, the order of addition of substrates and release of products is random. Sequential random reactions are illustrated by the formation of phosphocreatine and ADP from ATP and creatine, a reaction catalyzed by creatine kinase (肌氨酸激酶). Double-Displacement (Ping-Pong) Reactions. In double-displacement, or Ping-Pong, reactions, one or more products are released before all substrates bind the enzyme. The defining feature of double-displacement reactions is the existence of a substituted enzyme intermediate, in which the enzyme is temporarily modified. Reactions that shuttle amino groups between amino acids and α-keto acids are classic examples of double-displacement mechanisms. The enzyme aspartate aminotransferase catalyzes the transfer of an amino group from aspartate to α-ketoglutarate. After aspartate binds to the enzyme, the enzyme removes aspartate‘s amino group to form the substituted enzyme intermediate. The first product, oxaloacetate （草酰乙酸）, subsequently departs. The second substrate, α-ketoglutarate, binds to the enzyme, accepts the amino group from the modified enzyme, and is then released as the final product, glutamate. In the Cleland notation, the substrates appear to bounce on and off the enzyme analogously to a Ping-Pong ball bouncing on a table. 8.4.4. Allosteric Enzymes Do Not Obey Michaelis-Menten Kinetics The Michaelis-Menten model has greatly assisted the development of enzyme chemistry. Its virtues are simplicity and broad applicability. However, the Michaelis-Menten model cannot account for the kinetic properties of many enzymes. An important group of enzymes that do not obey Michaelis-Menten kinetics comprises the allosteric enzymes. These enzymes consist of multiple subunits and multiple active sites. Allosteric enzymes often display sigmoidal plots (Figure 8.14) of the reaction velocity V0 versus substrate concentration [S], rather than the hyperbolic plots predicted by the Michaelis-Men