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BIOC Lecture 5s

Enzyme Kinetic

DefinitionTerm
What do enzymes stabilize, lower transition state, activation energy
oxidoreductase function redox reaction
transferase function group transfer
hydrolase function hydrolysis
lyase function removal of group to form double bond
isomerase function intramolecular transfer
ligase function ligation via ATP hydrolysis
small organic molecules often derived form vitamins or metals cofactors
tightly binding coenzymes prosthetics
enzyme with its cofactor holoenzyme
enzyme without its cofactor apoenzyme
slope of product concentration over time velocity
reaction order with rate constant s^-1 first order
reaction order with rate constant (Ms)^-1 second order
approached as substrate increases in reaction equilibrium
Michaelis Menton requirement rate of formation of ES equals rate of loss of ES
Michaelis Menton equation (using Vmax equation) (k2 Et S)/(S + Km)
Michaelis Menton constant (Km) (k-1 + k2)/(k1)
rate of a reaction (general) k(reactant)
Velocity when all enzymes are bound to substrate Vmax
Equation for Vmax k2(Et)
equation for Vo at low [S] (Vmax [S])/(Km)
Vo at high [S] Vmax
When k-1 is much larger than k2 (k2 is negligible) Km=Kd
slope of reciprocal of MM equation Km/Vmax
x-intercept of reciprocal of MM equation -1/Km
y-intercept of reciprocal of MM equation 1/Vmax
Michaelis Menton plot Velocity over substrate concentration
Created by: oclar11
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