UNIT 1: BIOCHEMISTRY

1.7 Enzymes

Homework Questions?
10.

Nucleotides

Amino Acids

Enzymes

Biological catalysts usually having names ending in

(-ase)

Involved in, but not changed by, a chemical

reaction.

Proteins with a tertiary or quaternary structure

Commercial uses include: cheese, corn & bleach

Many enzymes function by lowering the activation

energy (Ea) of reactions. Temperatures within living things are
relatively low. By lowering the activation energy required
cells are able to carry out reactions by the use of enzymes

Enzyme Action

The functioning of enzymes is determined by its shape

The arrangement of molecules on the enzyme produces an
area known as the active site within which the specific
substrate(s) will "fit (i.e-substrate specific)
e.g- The enzyme peptidase (which breaks peptide bonds
in proteins) will not do the same to starches (which are
broken down by human-produced amylase in the mouth).
Substrates bind to active sites on enzymes, forming the
enzyme-substrate complex

Induced-Fit Model
Notice how
enzyme alters its
shape to better
fit substrate!

Example: Sucrase

Special Considerations
Some enzymes require cofactors in order to function:
1) Cofactors: non-proteins essential for enzyme activity.
Ions such as K+ and Ca+2 are cofactors.
2) Coenzymes: organic cofactors

Factors Affecting
Rate of Enzyme Activity
1) Temperature
Increases in temperature will speed up the
rate of non-enzyme mediated reactions, and so
temperature increase speeds up enzyme
mediated reactions, but only to a point. When
heated too much, enzymes (since they are proteins
dependent on their shape) become denatured.
When the temperature drops, the enzyme regains
its shape

2) pH
Enzymes are also adapted to operate at a
specific pH or pH range. Any change in pH level
will denature or change the shape of the enzyme.

Notice the
optimal pH is
different for
different
enzymes!

2) The concentration of substrate and product

also control the rate of reaction, providing a
biofeedback mechanism.
3) Inhibitors can lower the rate at which an
enzyme catalyzes a reaction. There are both
competitive and non-competitive inhibitors.

Competitive Inhibition
Notice how
the inhibitors
have the
same shape
as the
substrate!
They
compete with
the substrate
for access to
the active
site.

Non-Competitive Inhibition
The inhibitory chemical, which does not have
to resemble the substrate, binds to the enzyme
other than at the active site. When the chemical
either permanently binds to or massively
denatures the enzyme so that the tertiary structure
cannot be restored, the process is irreversible.
Many drugs and pesticides act in this way!

The Biochemical Pathway

Enzymatic pathways form as a result of the common

occurrence of a series of dependent chemical reactions
The end product depends on the successful completion of
five reactions, each mediated by a specific enzyme.
The enzymes in a series can be located adjacent to each
other (in an organelle or in the membrane of an
organelle), thus speeding the reaction process.
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Feedback Inhibition

Used to regulate multi-step metabolic pathways

The product of a pathway usually acts as an
allosteric inhibitor of the first enzyme of the
pathway
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Allosteric Regulation
Allows an enzyme to
be temporarily
inactivated.
Binding of an
allosteric
effector changes the
shape
of the enzyme,
inactivating
it while the effector
is still
bound.

Long Weekend Homework

1)

Complete Jmol activity- if not already done

2)

Read pg 50-56 (make notes)

3)

Complete pg 57 #2,6,8,10,12

4)

Edmodo Challenge: Choose one career profile to read

(Cheese Plant Manager or Marvellous Mutant) and
comment on your reactions to the reading in a 2-4 sentence
post