Enzymes:
Outcome: I can describe how the
structure of an enzyme correlates to its
function(s)
Drill:
What background knowledge do you
have on enzymes?
Enzyme Structure and Function
• Enzymes are protein catalysts
• They speed up the rate at which reactions occur
• Lower the activation energy by creating a
microenvironment that is energetically more favorable
for a reaction
Features of Enzymatic Reactions
1. Enzymes do not make anything happen that could
not happen on its own
– they just make it happen much faster.
2. Reactions do not destroy or use up enzyme
molecules.
3. Each type of enzyme recognizes and binds to only
certain substrates.
- ‘substrate specificity”
Enzyme-catalyzed Reactions
• Reactants in an enzyme-catalyzed reaction known as
substrates. They bind to the enzyme
Enzyme-catalyzed Reactions
• Substrates bind to the enzyme's active site
– interactions between the enzyme and the substrate
stabilize the transition state
– decrease the activation energy.
Active Site
• Pocket or crevice
• Site where substrates are bound
• Site of reaction catalysis
• Only substrates of specific size, shape, solubility,
and charge can bind
• Basis of enzyme specificity
Do Enzymes Act Alone?
• Some enzymes require cofactors to function normally.
-these are either metal ions or small organic molecules
called coenzymes.
•The cofactors usually are in the active site and are
involved in transition state stabilization.
Regulation of Enzyme Action
Enzyme activity can be regulated by molecules which
are not part of the enzyme
• Competitive inhibition: molecule similar in size and
shape to substrate binds to active site.
– “competes” with substrate for active site
Allosteric Regulation
•Allosteric regulation either increases or
decreases enzyme activity depending on the way
in which enzyme shape changes
Allosteric Activation
allosteric
activator enzyme active site
active site cannot
vacant bind substrate
allosteric
binding
site
active site
altered,
can bind
substrate
Allosteric Inhibition
allosteric inhibitor
allosteric
binding
site vacant;
active site
can bind
substrate
active site altered,
can’t bind substrate
Regulation of Enzyme Action
• Allosteric inhibition: regulatory molecule binds at
site other than active site (allosteric = different
structure)
– binding changes shape of active site
Feedback Inhibition
• Feedback inhibition of enzyme activity occurs in
pathways which require multiple enzyme-catalyzed
steps
• The end product of the pathway inhibits the first
enzyme in the pathway
– when there is an abundance of product the
pathway is shut down
enzyme 2 enzyme 3 enzyme 4 enzyme 5
enzyme A cellular change, caused by a
1 specific activity, shuts down the
activity that brought it about
END
SUBSTRATE PRODUCT
(tryptophan)
Enzymes:
Exit Ticket:
What is the difference
between competitive
inhibition and allosteric
inhibition?
