michaelismenten

michaelismenten - ;[S] ) to the mechanism ( v max ; K m )....

Info iconThis preview shows page 1. Sign up to view the full content.

View Full Document Right Arrow Icon
MICHAELIS-MENTEN ENZYME KINETICS MODEL MICHAELIS-MENTEN ENZYME KINETICS MODEL E S ES EP E P + + k 1 k 2 k 3 k 4 k 5 k 6 Make assumptions to simplify: v max = k 3 [E] tot Experimental: Measure velocity of reaction at time = 0, v o , when substrate concentration known [S] o . 1. Assume the first step is fast and reactions are in equilibrium. 2. Assume the second step is irreversible and slow, therefore the rate determining step. Start with a mechanism: k 3 K s E S ES E P + + Now derive the Michaelis-Menten equation. This relates experiment (v
Background image of page 1
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: ;[S] ) to the mechanism ( v max ; K m ). 1. Initial velocity of the reaction. 2. Total concentration of enzyme. 3. ES complex dissociation equilibrium constant. [S] o K s = [E] [ES] [E] [E] tot = + [ES] v o = k 3 [ES] (When [S]>>[E]) [E] tot = [ES] v o = v max K s K m when K m = [S] o v o = v max 1 / 2 = [S] o + K m [S] o v o v max MICHAELIS-MENTEN EQUATION MICHAELIS-MENTEN EQUATION 3. Assume the third step is fast....
View Full Document

This note was uploaded on 11/27/2011 for the course CHM 365 taught by Professor Thomaszamis during the Spring '06 term at FSU.

Ask a homework question - tutors are online