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** Enzyme kinetics and Eadie-Hofstee plots **

** Enzyme reaction kinetics Eadie-Hofstee plot **

Eadie-Hofstee Plot Another rearrangement of the Michaelis-Menten equation gives [Pg.37]

Eadie-Hofstee plot 112,114 Editing mechanisms 384-399 cost of editing 395 - 399 editing in protein synthesis 385-389 [Pg.322]

The Eadie-Hofstee plot of Mo against Mo/S has an intercept of Vmax on the Mo axis, while on the other axis the intercept is Vmax/Km (Fig. 5.13). [Pg.288]

For the Eadie-Hofstee plot, both coordinates contain rates that are subjected to the greatest error, as indicated in Figure E.2.3. [Pg.111]

Figure 7.7 Eadie-Hofstee plot for the hydrolysis of triethyl orthoformate in 1, pH 11,100 mM K2CO3,50 C, using NPr4 as a competitive inhibitor. |

Figure 9-4 The Eadie-Hofstee plot of v / [S] against v. The slope is -1/K, the intercept on the vertical axis is Vlnax/Km and that on the horizontal axis is Vmax. |

In addition to the Lineweaver-Burk plot (see p.92), the Eadie-Hofstee plot is also commonly used. In this case, the velocity v is plotted against v /[A]. In this type of plot, Vmax corresponds to the intersection of the approximation lines with the v axis, while Km is derived from the gradient of the lines. Competitive and non-competitive inhibitors are also easily distinguishable in the Eadie-Hofstee plot. As mentioned earlier, competitive inhibitors only influence Km, and not Vmax- The lines obtained in the absence and presence of an inhibitor therefore intersect on the ordinate. Non-competitive inhibitors produce lines that have the same slope (l

The Scatchard plot is bound free (/i/ L, y-axis) vs. bound (B, x-axis) (the Eadie-Hofstee plot is bound vs. bound/free). If this equation is applicable (i.e., the binding represents a simple bimolecular [Pg.171]

Figure 9-10 Effect of a competitive inhibitor on the Eadie-Hofstee plot (top) and on a double reciprocal plot (bottom). The apparent Km (Eq. 9-59) is increased by increasing [ I ], but E.naxis unchanged. |

The plot of r versus r/Cs will result in a straight line with a slope of -Km and an intercept of rmax, as shown in Figure 2.7. This plot is known as the Eadie-Hofstee plot (Eadie, 1942 Hofstee, 1952). [Pg.23]

Figure 3.6 Evaluation of kinetic parameters in Michaelis-Menten equation (a) Lineweaver-Burk plot, (b) C /r versus plot, and (c) 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. [Pg.99]

The deviation of the reaction rate 31, from the rectangular hyperbola which would be shown by a true Michaelis-Menten reaction law, is best illustrated by considering the data as represented by an Eadie-Hofstee plot. The original equation for the Michaelis-Menten or Monod kinetics [Pg.359]

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. [Pg.29]

While the point for [S] = 0 and v = 0 cannot be plotted, the ratio v / [S] approaches Vma JKm as v approaches zero. Notice the distribution of the points in Fig. 9-4. Substrate concentrations were chosen such that the increase in velocity from point to point is more or less constant, a desirable experimental situation. The points on the Eadie-Hofstee plot are also nearly evenly distributed, but those of the Lineweaver-Burk plot are compressed at one end. (However, if the substrate concentrations for successive points are selected in the ratios 1,1 / 3,1/ 5,1/ 7, and 1/9, the spacing will be uniform on the Lineweaver-Burk plot.) A second advantage of the Eadie-Hofstee plot is that the entire range of possible substrate concentration from near zero to infinity can be fitted onto a single plot. [Pg.460]

Pirrang, Liu, and Morehead [22] have elegandy demonstrated the application of saturation kinetics (Michaehs-Menten) to the rhodium(II)-mediated insertion reactions of a-diazo /9-keto esters and a-diazo /9-diketones. Their method used the Eadie-Hofstee plot of reaction velocity (v) versus v/[S] to give and K, the equilibrium constants for the catalytic process. However, they were unable to measure the Michaelis constant (fC ) for the insertion reactions of a-diazo esters because they proved to be too rapid. [Pg.366]

Purification. One main peak was observed with detection at 405 nm, when purified lignin peroxidase was analyzed by Mono Q chromatography. The retention time of the main peak was 11.8 min and its area was 98.9% of the total peak area. Possibly the enzyme solution contains, however, two isoenzymes which have very similar properties. The Kj of the purified lignin peroxidase for veratryl alcohol was 139 on the basis of Eadie-Hofstee plot. [Pg.233]

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** Enzyme kinetics and Eadie-Hofstee plots **

** Enzyme reaction kinetics Eadie-Hofstee plot **

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