生物化学教学课件：Enzyme.pptVIP

酶的催化作用 H:\生物化学 2015\酶的作用.f4v Where from？ Living cells What could do? catalysis What is the molecular basis? Proteins 自由的双分子间 同一的分子内 分子内成合适角度 The specificity of serine proteases is determined by the structural features of a substrate binding pocket Electron charge Lys/Arg Jencks: “If complementarity between the active site and the transition state contributes significantly to enzymatic catalysis, it should be possible to synthesize an enzyme by constructing such an active site. One way to do this is to prepare an antibody to a haptenic group which resembles the transition state of a given reaction. The combining site of such antibodies should be complementary to the transition state and should cause an acceleration by forcing bound substrates to resemble the transition state.” Reversible Inhibitions Clavulanic acid（克拉维酸）灭活β-lactamase的机理 Artificial inhibition Inhibition Irreversible Reversible Group-specific 化学基团 Affinity 亲和接触 活性位点 Suicide 亲和接触 活性位点外 Artificial inhibition Inhibition Irreversible Reversible Competitive Uncompetitive Mixed Group-specific Affinity Suicide reversible inhibitors： attach to enzymes with non-covalent interactions such as?hydrogen bonds,?hydrophobic interactions?and?ionic bonds. can be easily removed by dilution or dialysis. Competitive inhibitors alters the Km but not the Vmax of enzymes Inhibitor only binds to the ES complex anti-competitive Uncompetitive inhibitors alter both the Km and the Vmax of an enzyme Goto 78 Mixed inhibition Mixed inhibitors alter both the Km and the Vmax of an enzyme Goto 76 §5.1 Introduction §5.2 How Do Enzymes Play Specificity §5.3 How Do Enzymes Accelerate Reaction §5.4 Enzyme examples §5.5 Enzyme Kinetics §5.6 Enzyme Regulation §5 Enzyme Steady state Pre-steady state One substrate kinetics Two substrates kinetics Steady state kinetics Pre-steady state kinetics One substrate kinetics: Michaelis-Menten equation 合理简 化 Kcat代表“暗箱”的表观速率常数，是各正向速率常数的函数.如果“暗箱”中只有一个限速步骤，则kcat 近