Enzymes Notes

Proteins that catalyze chemical rxns

Enzymes only catalyze rxns – lower activation energy. They only affect kinetics, not thermodynamics.
Same ∆G between reactants and products.

Lowering Ea leads in faster rxn because there will be more particles with sufficient energy (and
geometry) to collide and form products.

Lower Ea = more fraction of molecules with enough KE to react.

Enzymes bind specifically to reactants and lower Ea and don’t affect eqb position.

How enzymes work:

 Bind to substrate – they have a high affinity for reactants

 Increase in [reactants] because they are in close proximity to each other.
 Bonding causes stress on key bonds, therefore increase in probability of bonds breaking and
reaction
 Products usually have lower affinity than reactants for enzyme

Reactants bind to active site

AA that form active site are brought together during folding. Therefore, when enzyme gets
denatured/unfolded, these regions are not together and therefore no active site

Enzyme and substrate bind together to form Enzyme-substrate complex. Then, reaction happens and
Enzyme product complex forms. Then, enzyme releases products

Fastest step = smallest hill

Rate limiting = largest hill (big Ea)

Note: even with enzyme, there was no change in energy levels of products and reactants

Enzyme Regulation

Co factors that bind to enzymes (usually in active site) and therefore increase the affinity of substrate to
enzyme (can be ions or other organic molecules)
Competitive inhibition: Inhibitor competes for active site. Once its bounded, the substrate can’t bind due
to change in conformation in active site.

From Biocore: Competitive inhibitors “compete” with the substrate for the active site. Once the
competitive inhibitor binds there, the substrate can’t bind and therefore the reaction does not
occur. Here is a diagram from the Enzymes PowerPoint (slide 19) to help visualize.

Often times, competitive inhibitors are part of a feedback system (allosteric regulation) where when too
much product is formed, the inhibitor (often one of the products) binds to the enzyme at the active site
to prevent more product from being produced.

Non competitive inhibitors: Bind to anywhere but active site – change conformation of enzyme so no
affinity for substrate

From Biocore: Non-competitive inhibitors bind to the enzyme (anywhere other than the active
site) and alter the conformation of the enzyme such that it looses affinity for the substrate and
does not bind with the substrate.

Non-competitive inhibitors can also work in an allosteric regulation system or can be heavy metals (Pb)
that inhibit enzyme activity.
Hydrolysis of ATP provides energy for certain rxns as breaking high bonds between phosphates releases a
lot of energy

Couple strong exergonic rxn (ATP hydrolysis) with endergonic rxn (slow).

[ ligand ]
Saturation function: saturation=
Kd + [ ligand ]
For enzymes, ligand = substrate