Enzyme reaction kinetics Eadie-Hofstee plot

Enzyme kinetics. Data for reactions that follow the Michaelis-Menten equation are sometimes analyzed by a plot of v,/tA]o versus l/[A]o. This treatment is known as an Eadie-Hofstee plot. Following the style of Fig. 4-7b, sketch this function and label its features. 

Enzyme kinetics Michaelis constant, symbol iCm maximum velocity of an enzyme catalysed reaction, Vm DC inhibitor constant, symbol X Michaelis-Menten equation and graph in the absence and the presence of inhibitors. Lineweaver-Burke and Eadie-Hofstee plots. 

The following kinetic data were reported for an enzyme catalyzed reaction of the type E-l-S<->ES E-l-P. Since these data pertain to initial reaction rates, the reverse reaction may be neglected. Use an Eadie-Hofstee plot to determine the... 

Evaluate the inhibited enzyme kinetic rate law parameters Kf, and K. Data from a substrate (S) inhibited reaction is shown below, in the fonn of Eadie-Hofstee plot. 

There are well-established methods for obtaining the type of inhibition and the value of the inhibition constants from initial-rate kinetics, often from linearized plots such as lineweaver-Burk, Eadie-Hofstee, or Hanes. As these procedures are covered very well by a range of basic textbooks on biochemistry and kinetics (see the list of Suggested Further Reading ) we will not repeat these procedures here. Instead, we will discuss the situation in which an enzyme reaction is followed over more than just the initial range of conversion. Towards this end, the rate equation,... 

Figure 7.4 Methods of plotting data for enzyme-catalyzed reactions (a) Lineweaver-Burk plot (b) Eadie or Hofstee plot (c) Hanes plot. (Adapted from K. Plowman, Enzyme Kinetics. Copyright 1972. Used with permission of McGraw-Hill Book Company.)...

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