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
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Enzyme kinetics maps

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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
1.1.1.1 High [substrate] means low affinity for substrate
1.1.1.1.1 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
4.1.1.1 Coenzymes
4.1.1.1.1 Organic molecules
4.1.1.1.1.1 Water-soluble vitamins
4.1.1.1.1.2 Cosubstrates
4.1.1.1.1.2.1 Reversibly bind to an enzyme, transfer a chemical group to another substrate
4.1.1.1.1.2.1.1 Reverts to original form via other enzymatic rxn
4.1.1.1.1.2.1.1.1 Example: ATP
4.1.1.1.1.3 Prosthetic groups
4.1.1.1.1.3.1 Binds covalently to enzyme during rxn
4.1.1.1.1.3.1.1 Emerges from rxn unchanged
4.1.1.1.1.3.1.1.1 Example: Heme
4.1.1.1.1.3.1.1.1.1 Heme binds to Catalase in peroxisomes to degrade H2O2
4.1.1.2 Metal Ions
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