Enzyme Kinetics Bwahahahaha!

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Presentation transcript:

Enzyme Kinetics Bwahahahaha!

Ribozymes

Saturation kinetics

Assumptions in the Henri-Michaelis-Menton Equation formation of an enzyme-substrate complex ES complex is in rapid equilibrium with free enzyme Breakdown of ES to form products is assumed to be slower than 1) formation of ES and 2) breakdown of ES to re-form E and S

Michaelis-Menton Equation is a Combination of 0-order and 1st-order kinetics When S is low, the equation for rate is 1st order in S When S is high, the equation for rate is 0-order in S The Michaelis-Menten equation describes a rectangular hyperbolic dependence of v on S!

Be able to derive it!

Assumptions in the Henri-Michaelis-Menton Equation formation of an enzyme-substrate complex ES complex is in rapid equilibrium with free enzyme Breakdown of ES to form products is assumed to be slower than 1) formation of ES and 2) breakdown of ES to re-form E and S Under ‘steady-state’ conditions d[ES]/dt = 0

The Michaelis constant Km is a constant Km ≠KD Km is derived from rate constants Km is, under true Michaelis-Menten conditions (k2 is small), an estimate of the dissociation constant of E from S Small Km means tight binding; high Km means weak binding

What is Vmax? Vmax is a constant Vmax is the theoretical maximal rate of the reaction - but it is NEVER achieved in reality To reach Vmax would require that ALL enzyme molecules are tightly bound with substrate Vmax is asymptotically approached as substrate is increased If k2 is rate limiting, v = k2[ES]. At saturation, [ES] = [E]total and Vmax = k2[E]total

http://www.wellesley.edu/Biology/Concepts/Html/vmaxfrommme.html

kcat, the turnover number, is the number of substrate molecules converted to product per enzyme molecule per unit of time, when E is saturated with substrate. If the M-M model fits, k2 = kcat = Vmax/Et Values of kcat range from less than 1/sec to many millions per sec

Catalytic efficiency An estimate of "how perfect" the enzyme is kcat/Km is an apparent second-order rate constant It measures how the enzyme performs when S is low The upper limit for kcat/Km is the diffusion limit - the rate at which E and S diffuse together