BCHM 310 Lecture 28: BCHEM 315 10:2
22 Dec 2018
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S es formation of es complex, desolvation of e + s. Es ep true transition state, rx passing thru transition state (=/=) will either go back to es or move fwd to ep. Ep p dissociation of ep complex to p and e. Enzyme provides an enviro that decr the e of transition state. Helps us understand mechanism of catalysis ex. can compare kinetics of variations of s w one enzyme: assesses effectiveness of inhibitor. E + s es ep e + p. Keq= [p]/[s] this is unchanged by presence of enzyme, enzyme just speeds up rate of reaching equil only. Measure kinetics via measuring change in p vs time. V1, v2 and v3 are initial velocities det from slop at t=0 for [s]1, [s]2, [s]3. Slope decr w time as s is depleted: measure initial velocities, assume [p]=0 and thus no reverse reaction. Resembles a binding cure (o vs [l])
