Enzyme Kinetics

Description

Enzyme kinetics maps
Christopher Boga
Mind Map by Christopher Boga, updated more than 1 year ago
Christopher Boga
Created by Christopher Boga about 8 years ago
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Resource summary

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