生物化学 Chap 6 enzymes幻灯片.pptVIP

An enzyme works by stabilizing the transition state of a chemical reaction and decreasing ΔG?. it does not alter energy levels of the substrate and products. Thus an enzyme increases the rate at which the reaction occurs but has no effect on the overall change in energy of the reaction. Emil Fischer 1894 the shape of substrate and the active site of the enzyme are thought to fit together like a key into a lock. The two shapes are considered as rigid and fixed, and perfectly complement each other when brought together in the right alignment. Lock-and-key model (锁钥学说) Daniel E. Koshland 1958 the binding of substrate induces a conformational change in the active site of the enzyme so that the active site assumes a shape that is complementary to the substrate. Induced-fit model (诱导锲合学说) Section 5 enzyme kinetics When [S]Km, at very low [S], v=Vmax[S]/Km When [S]Km, at very high [S], v= Vmax At low substrate concentrations, V is directly proportional to [S]; High substrate concentrations, V tends to become independent of [S] (maximum rate, Vmax). Significance of Km (equilibrium constant) When v=Vmax/2, Km=[S]. Km is equivalent to the substrate concentration at which the velocity is equal to half of Vmax(mol/L) A high Km indicates weak substrate binding; a low Km indicates strong substrate binding. Km is one of the characteristic constant of enzymes; closely related with enzyme properties; irrelevant to enzyme concentrations. (5) Enzyme inhibitors Inhibitors act directly on an enzyme to lower its catalytic rate without causing the enzyme to be denatured. Enzyme inhibition may be of two main types: irreversible or reversible. Irreversible inhibition (不可逆抑制) Inhibitors bind irreversibly to an enzyme and form a covalent bond to an amino acid residue at or near the active site Enzyme is permanently inactivated. Iodoacetamide (碘乙酰胺) modifies Cys residues and hence may be used as a diagnostic tool in determining whether one or more Cys residues