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Enzymes
Biological catalysts used to speed up chemical reactions
(process is called catalysis)
Section 1.7
Role of Proteins
• Ex. Lactose needs to be broken up to create glucose + galactose
ome Activation Energy (Ea)
needed to break the
ond (usually heat)
However Ea required
would kill your cells.
•Enzymes are protein catalysts that work on specific
substrates
•They speed up a reaction (without being consumed) by
lowering Ea
How do Enzymes Lower Ea?
1. Use amino acid R groups to weaken the
bonds in the substrate
2. Put the substrate(s) in the correct
orientation
3. Transfer electrons to or from the substrate
to destabilize it (oxidative enzymes)
4. Add or remove H+
from the substrate
(hydrolytic enzymes)
Enzyme/substrate
•An enzyme has a special active site that will only fit a specific
substrate (or reactant)
•The active site will change shape (called the induced fit
model) and the reaction can proceed
•1000’s of substrates/second
•This process is repeated, know as the catalytic cycle
•Some enzymes require additional
molecules or ions to catalyze a reaction:
•Organic molecules that help enzymes are
called coenzymes (coenzyme-A, NAD+
, FAD)
•Ions that help are called cofactors
Rate of enzyme activity
Enzyme action is modified by:
1. Heat (excessive kinetic energy can denature)
2. pH (alters ionization of peptides)
3. Enzyme concentration
Regulating Enzymes
Competitive Inhibition:
A inhibitor competes for an enzyme’s active site and slows down its
action.
Non-competitive inhibition:
1. Allosteric Regulation (inhibition): A non-competitive
inhibitor binds to a regulatory site called the allosteric site
and changes the shape of the active site so it no longer
accepts substrates.
2. Feedback Inhibition: A group of enzymes in sequence
change a substrate until enough of the finished product
reacts with a regulatory site on the original enzyme,
stopping the sequence.
*Feedback regulation
is an important
concept in biology
Allosteric Regulation (activation): molecules
called activators can also bind to the allosteric
site and increase the enzyme’s activity
HWK
Pg. 57, Q. 1-13

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Enzymes Speed Up Reactions

  • 1. Enzymes Biological catalysts used to speed up chemical reactions (process is called catalysis) Section 1.7
  • 3. • Ex. Lactose needs to be broken up to create glucose + galactose ome Activation Energy (Ea) needed to break the ond (usually heat) However Ea required would kill your cells.
  • 4. •Enzymes are protein catalysts that work on specific substrates •They speed up a reaction (without being consumed) by lowering Ea
  • 5. How do Enzymes Lower Ea? 1. Use amino acid R groups to weaken the bonds in the substrate 2. Put the substrate(s) in the correct orientation 3. Transfer electrons to or from the substrate to destabilize it (oxidative enzymes) 4. Add or remove H+ from the substrate (hydrolytic enzymes)
  • 6. Enzyme/substrate •An enzyme has a special active site that will only fit a specific substrate (or reactant) •The active site will change shape (called the induced fit model) and the reaction can proceed •1000’s of substrates/second
  • 7. •This process is repeated, know as the catalytic cycle
  • 8. •Some enzymes require additional molecules or ions to catalyze a reaction: •Organic molecules that help enzymes are called coenzymes (coenzyme-A, NAD+ , FAD) •Ions that help are called cofactors
  • 9.
  • 10. Rate of enzyme activity Enzyme action is modified by: 1. Heat (excessive kinetic energy can denature) 2. pH (alters ionization of peptides)
  • 12. Regulating Enzymes Competitive Inhibition: A inhibitor competes for an enzyme’s active site and slows down its action.
  • 13. Non-competitive inhibition: 1. Allosteric Regulation (inhibition): A non-competitive inhibitor binds to a regulatory site called the allosteric site and changes the shape of the active site so it no longer accepts substrates.
  • 14. 2. Feedback Inhibition: A group of enzymes in sequence change a substrate until enough of the finished product reacts with a regulatory site on the original enzyme, stopping the sequence. *Feedback regulation is an important concept in biology
  • 15. Allosteric Regulation (activation): molecules called activators can also bind to the allosteric site and increase the enzyme’s activity