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Lecture

Enzyme kinetics, Michaelis and Menton, Briggs and Haldane, ..
Enzyme kinetics, Michaelis and Menton, Briggs and Haldane, comparing enzymes

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School
Colorado State University
Department
Life Science
Course
LIFE 210
Professor
Paul Laybourn
Semester
Fall

Description
7 September Enzymes affect the kinetics of a reaction Can use enzyme kinetics to Compare chemical reactions Compare enzymes as catalysts Specificity and efficiency Study enzyme mechanisms Chemical Kinetics Experiments Δ[P] Rate or velocity: v = t ← S k−1 1 P; at 0 only 1 is significant0 v 1 k [S] → Compare rates or velocities (v0) as it varies with [S] “Simple” case E + S ↔ES ↔ EP ↔ E + P E + S associate E catalyzes conversion of S to P E + P dissociate Michaelis and Menton Used initial velocities0(v ), plot vs. [S] Simplifies reaction to ← k−1 1 k2 E + S → ES → E + P Gives hyperbolic curve Michaelis – Menton equation Vmax[S] V0= K +MS] KM– Michaelis Constant – [S] at ½ Vmax Briggs and Haldane Applied M&M Kinetics in terms and conditions useful for enzyme comparison [ES] in “steady state” Not changing K2rate limiting (k2< < k-1 [S] very high Enzyme is saturated ≈ [ES] [Et [Et known V0= k 2ES] So v0= k 2E] t Produces Terms Useful for Comparing Enzymes ← k k k 2 E + S −1→1 ES → E + P Turnover Number V0= Vmax = k [E2 t Vmax rxns K2= [E ] = kcatn (measures efficiency) t s
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