清华本科课件《生物化学》Summary of Chapter 1-6 182402108.pptVIP

Determine KM and Vmax by Double-reciprocal Plots Double-reciprocal plot of enzyme kinetics is generated by plotting 1/V0 as a function 1/[S]. The slope is the KM/Vmax, the intercept on the vertical axis is 1/Vmax, and the intercept on the horizontal axis is -1/KM. Lineweaver-Burk equation ***** Subunit interactions in an allosteric enzyme, and interactions with inhibitors and activators. In many allosteric enzymes the substrate binding site and the modulator binding site(s) are on different subunits, the catalytic (C) and regulatory (R) subunits, respectively. Binding of the positive (stimulatory) modulator (M) to its specific site on the regulatory subunit is communicated to the catalytic subunit through a conformational change. This change renders the catalytic subunit active and capable of binding the substrate (S) with higher affinity. On dissociation of the modulator from the regulatory subunit, the enzyme reverts to its inactive or less active form. Some enzyme modification reactions Activation of zymogens by proteolytic cleavage Many proteolytic enzymes are synthesized as inactive precursors called zymogens, which are activated by cleavage of small peptide fragments. * * * * * FIGURE 2-16 The titration curve of acetic acid. After addition of each increment of NaOH to the acetic acid solution, the pH of the mixture is measured. This value is plotted against the amount of NaOH added, expressed as a fraction of the total NaOH required to convert all the acetic acid (CH3COOH) to its deprotonated form, acetate (CH3COO–). The points so obtained yield the titration curve. Shown in the boxes are the predominant ionic forms at the points designated. At the midpoint of the titration, the concentrations of the proton donor and proton acceptor are equal, and the pH is numerically equal to the pKa. The shaded zone is the useful region of buffering power, generally between 10% and 90% titration of the weak acid. * FIGURE 2-17 Comparison of the titration c