BIOCH200 Lecture Notes - Lecture 18: Hydrolysis, Covalent Bond, Protein Kinase
30 Oct 2016
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Biochem 200 - lecture #18 - enzymes pt. Regulating enzyme activity: reaction velocity vs. Vo = initial velocity (measure the rate of product formation) Vmax = maximum velocity (occurs when all active sites are occupied) Vo = 50% vmax when [substrate] = km. Measure of affinity of enzyme for subsrate. Enzyme active site is saturated; active site is fully occupied. If it was allosteric, curve would be sigmoidal. Mechanisms that alter activity of existing enzyme: competitive inhibition. Substances that bind reversibly to the active site. Resembles the substrate or the transition site but do not react. Physically blocks active site and prevents substrate binding. Competitive inhibitors decrease the apparent affinity ( km) for enzyme. Deals with the t and r state. Reflects different state (geometries) for the active site. Compounds besides the substrate may affect the equilibrium between t and. Sigmoidal relationship between reaction velocity and substrate concentration. Nb: km only applies for non-allosteric enzymes (like kd) is for ligand.
