Enzymes

General Biology I
ENZYMES
BIOLOGICAL CATALYSTS
Unlocking: Energy of Activation
• The energy used to

break the bonds in the
reactants so they can be
reformed in the products
is called the energy of
activation.
Unlocking: Energy of Activation
• Mix two moles of hydrogen gas H2 with one mole of

oxygen gas-nothing happens.
• If you add a spark to the container, the following reaction
occurs. KABOOM!
2H2 + O2 → 2 H2O G= -58 kcal/mole
• In order for water to be produced H2 must become 2H and the O2

must become 2O as this frees up the electrons tied up in covalent
bonds, to form chemical bonds forming water, H2O.
Enzymes
• A catalyst is a chemical agent that speeds up a reaction

without being consumed by the reaction
• Enzymes are biological catalysts that increase the reaction

rate of biochemical reactions by lowering the activation
energy without being consumed in the reaction
Fig. 8-14
A B
C D
Transition state
A B EA
C D
Reactants
A B
∆G < O
C D
Products
Progress of the reaction

Fig. 8-15
Course of
reaction
without EA
enzyme without
enzyme EA with
enzyme
is lower
Reactants
Course of
∆G is unaffected
reaction
by enzyme
with enzyme
Products
Progress of the reaction

Characteristics of Enzymes
A. Made of proteins (or RNA).

B. They are very specific and only work with a certain set of reactants or
substrates that fit on their active site.
C. Enzymes can be used over and over again.
D. When an enzyme binds with the substrate, the substrate interacts with
the enzyme causing it to change shape. This change in shape facilitates
the chemical reaction to occur. This is called the induced fit.
E. Enzymes increase the reaction rate by lowering the energy of activation.
They do NOT change Gibbs free energy or G.
Characteristics of Enzymes: Substrate Specificity
• The reactant that an enzyme acts on is called the enzyme’s

substrate
• The enzyme binds to its substrate, forming an enzyme-
substrate complex
• The active site is the region on the enzyme where the
substrate binds
• Induced fit of a substrate brings chemical groups of the
active site into positions that enhance their ability to
catalyze the reaction
Fig. 8-16
Substrate
Active site
Enzyme Enzyme-substrate
complex
(a) (b)
Catalysis in the Active Site
• In an enzymatic reaction, the substrate binds to the active

site of the enzyme
• The active site can lower an EA barrier by

✓Orienting substrates correctly
✓Straining substrate bonds
✓Providing a favorable microenvironment
✓Covalently bonding to the substrate
Factors Affecting of Enzyme
Activity
Initial Velocity
• The reaction rate of an enzymatic reaction is always

fastest at the beginning of the reaction when there is the
greatest concentration of substrate. Why?
Factors Affecting Enzyme Activity
• An enzyme’s activity can be affected by

✓General environmental factors, such as temperature
and pH
✓Chemicals that specifically influence the enzyme
(regulatory molecules: cofactors and inhibitors)
Factors Affecting Enzyme Activity: Temperature
• Each enzyme has an optimal temperature in which it can

function
Factors Affecting Enzyme Activity: pH
• Each enzyme has an optimal pH in which it can function

Factors Affecting Enzyme Activity: Regulatory
molecule
• Cofactors are nonprotein enzyme helpers
• Cofactors may be inorganic (such as a metal in ionic
form) or organic
• An organic cofactor is called a coenzyme
• Coenzymes include vitamins
Factors Affecting Enzyme Activity: Regulatory
molecule
• Inhibitors- Some chemicals inhibit the action of an
enzyme.
• Competitive inhibitors bind to the active site of an
enzyme, competing with the substrate
• Noncompetitive inhibitors bind to another part of an
enzyme, causing the enzyme to change shape and making
the active site less effective
• Examples of inhibitors include toxins, poisons, pesticides,
and antibiotics
Fig. 8-19
Substrate
Active site
Competitive
inhibitor
Enzyme
Noncompetitive inhibitor
(a) Normal binding (b) Competitive inhibition (c) Noncompetitive inhibition
Regulation of Enzyme Activity
Regulation of enzyme activity
• Regulation of an enzyme helps control metabolism

• Chemical chaos would result if a cell’s metabolic pathways
were not tightly regulated
• A cell does this by switching on or off the genes that
encode specific enzymes or by regulating the activity of
enzymes
Regulation of enzyme activity
A. Allosteric Regulation
1) Allosteric inhibition
2) Allosteric activation
• Cooperativity
B. Feedback Inhibition
Allosteric Regulation
• Allosteric regulation, is any form of regulation where the

regulatory molecule (an activator or inhibitor) binds to an
enzyme someplace other than the active site and affects
the enzyme function at another site. The place where the
regulator binds is called the allosteric site.
• Allosteric regulation may either inhibit or stimulate an
enzyme’s activity
• Allosteric enzymes typically have multiple active sites
located on different protein subunits
• Most allosterically regulated enzymes are made

from polypeptide subunits
• Each enzyme has active and inactive forms
• The binding of an activator stabilizes the active form
of the enzyme
• The binding of an inhibitor stabilizes the inactive
form of the enzyme
Allosteric enzyme Active site
with four subunits (one of four)
Regulatory
site (one
Activator
of four)
Active form Stabilized active form
Oscillation
Non- Inhibitor
functional Inactive form Stabilized inactive
active form
site
(a) Allosteric activators and inhibitors
• Cooperativity is a form of allosteric regulation that

can amplify enzyme activity
• In cooperativity, binding by a substrate to one active
site stabilizes favorable conformational changes at
all other subunits (or all other active sites)
• the substrate itself can serve as an allosteric
activator: when it binds to one active site, the
activity of the other active sites goes up
Substrate
Inactive form Stabilized active

form
(b) Cooperativity: another type of allosteric activation
Feedback Inhibition
• In feedback inhibition, the end product of a

metabolic pathway shuts down the pathway
• Why would a molecule turn off its own pathway?

Feedback inhibition prevents a cell from wasting
chemical resources by synthesizing more product
than is needed

Enzymes

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General Biology I

• The energy used to

• Mix two moles of hydrogen gas H2 with one mole of

• In order for water to be produced H2 must become 2H and the O2

• A catalyst is a chemical agent that speeds up a reaction

• Enzymes are biological catalysts that increase the reaction

Progress of the reaction

Progress of the reaction

A. Made of proteins (or RNA).

• The reactant that an enzyme acts on is called the enzyme’s

• In an enzymatic reaction, the substrate binds to the active

• The active site can lower an EA barrier by

• The reaction rate of an enzymatic reaction is always

• An enzyme’s activity can be affected by

• Each enzyme has an optimal temperature in which it can

• Each enzyme has an optimal pH in which it can function

• Regulation of an enzyme helps control metabolism

• Allosteric regulation, is any form of regulation where the

• Most allosterically regulated enzymes are made

• Cooperativity is a form of allosteric regulation that

Inactive form Stabilized active

• In feedback inhibition, the end product of a

• Why would a molecule turn off its own pathway?

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