4934094
Description
Mind Map by Christopher Boga, updated more than 1 year ago
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Created by Christopher Boga
over 8 years ago
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Enzyme Kinetics
- Michaelis Constant (Km)
- [Substrate] when rxn rate = 1/2 Vmax
- Indicates [Substrate] needed to speed up rxn
- High [substrate] means low affinity for substrate
- Km inversely proportional to enzyme-substrate affinity
- Km inversely proportional to enzyme-substrate affinity
- High [substrate] means low affinity for substrate
- Indicates [Substrate] needed to speed up rxn
- [Substrate] when rxn rate = 1/2 Vmax
- Vmax
- Maximum rxn rate
- Maximum rxn rate
- Saturation Kinetics
- [Substrate] increase, rate of rxn increases until Vmax is achieved
- [Substrate] increase, rate of rxn increases until Vmax is achieved
- Cofactor
- Non-protein component required by some enzymes to reach optimal activity
- 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
- Example: ATP
- Reverts to original form via other enzymatic rxn
- Reversibly bind to an enzyme, transfer a chemical group to another substrate
- Prosthetic groups
- Binds covalently to enzyme during rxn
- Emerges from rxn unchanged
- Example: Heme
- Heme binds to Catalase in peroxisomes to degrade H2O2
- Heme binds to Catalase in peroxisomes to degrade H2O2
- Example: Heme
- Emerges from rxn unchanged
- Binds covalently to enzyme during rxn
- Water-soluble vitamins
- Organic molecules
- Metal Ions
- Coenzymes
- Can be coenzymes or metal ions
- Non-protein component required by some enzymes to reach optimal activity
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