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ch369_f09_enzymes_3_notes

ch369_f09_enzymes_3_notes - S tudy group tim s locations e...

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Extra office hours for the T.A.’s on Monday, Oct 5. Ken, 3- 4 pm in cubicle A, 1st floor of Welch. Cassidy, 11 - noon in 3.422F of MBB.
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Plan for today is to finish chapter 7. Enzyme kinetics & enzyme inhibition.
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Last time - Michaelis-Menten enzyme kinetics: [S] = initial substrate concentration, typically in units of moles/liter. v o = initial reaction velocity (such as moles of product produced / sec) The shape of the curve is described by the Michaelis- Menten eqn:
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K M is the substrate concentration when the initial reaction velocity is one-half of its Three numbers that can describe an enzyme’s catalytic abilities are: K M and V max and k cat initial reaction velocity V 0 [S]
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K M is a measure of how tightly an enzyme binds substrate. High K M means weak substrate binding ; Lower K M means tighter substrate binding.
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Another quantity used to characterize enzymes is k cat . k cat = V max / [E] total k cat is called “catalytic constant” or “turnover number”. k cat = number of catalytic cycles by each active site per second. Enzyme k cat Staph. nuclease 95 sec -1 Chymotrypsin 190 sec -1 Trios phosphate isomerase 4300 sec -1 Carbonic anhydrase 1,000,000 sec -1
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Finding V max and K M : May use a “ Lineweaver-Burk plot
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Not all enzymes follow Michaelis-Menten kinetics. For example, some reactions have multiple steps and several transition states (these are not taken into account in the M-M model, which assumes one transition state).
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ch369_f09_enzymes_3_notes - S tudy group tim s locations e...

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