Enzyme Kinetics

Christopher Boga
Mind Map by Christopher Boga, updated more than 1 year ago
Christopher Boga
Created by Christopher Boga about 4 years ago


Enzyme kinetics maps

Resource summary

Enzyme Kinetics
1 Michaelis Constant (Km)
1.1 [Substrate] when rxn rate = 1/2 Vmax
1.1.1 Indicates [Substrate] needed to speed up rxn High [substrate] means low affinity for substrate Km inversely proportional to enzyme-substrate affinity
2 Vmax
2.1 Maximum rxn rate
3 Saturation Kinetics
3.1 [Substrate] increase, rate of rxn increases until Vmax is achieved
4 Cofactor
4.1 Non-protein component required by some enzymes to reach optimal activity
4.1.1 Can be coenzymes or metal ions Coenzymes Organic molecules Water-soluble vitamins Cosubstrates Reversibly bind to an enzyme, transfer a chemical group to another substrate Reverts to original form via other enzymatic rxn Example: ATP Prosthetic groups Binds covalently to enzyme during rxn Emerges from rxn unchanged Example: Heme Heme binds to Catalase in peroxisomes to degrade H2O2 Metal Ions
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