Biochemistry 2280A Lecture 7: Enzyme Catalysis Part II Sept 26

• School: Western University
• Department: Biochemistry
• Course: Biochemistry 2280A
• Professor: Derek Mc Lachlin

Document Summary

Hydrolysis reaction: the conformation of the enzyme forces a sugar into a strained chair conformation, resembles transition state more closely transition state is typically high energy and short time but not covalent. Enzyme kinetics: set up multiple tubes with different concentrations of substrate and add enzyme, eventually plateaus. Vmax: maximum speed that this reaction can occur with infinitely high substrate concentration. The km is the substrate concentration at which the rate of reaction is of the max. Michaelis menten: we use a double reciproca pot, equation is the inverse of michaelis menten, 1/v = (1/[s])(km/vmax) + 1/vmax, plot of 1/v and 1/[s, gives a straight line, km/vmax is just the slope now! Enzyme inhibition: therapeutic drugs natural inhibitors of metabolism, herbicides and pesticides, two general types, reversible: E. g. poisonous gas forms a covalent bond to disable enzyme permanently. Can be explained by michaelis menten kinetics: major category of reversible inhibitors: competitive, inhibitors binds in active site.