Enzymes

Cell Biology
Lecture#7
 Metabolism
Metabolism is the whole range of
biochemical processes that occur within
the cell.

Metabolism consists of:

Breaking down molecules to get energy
(catabolism)
Using the energy to buildup new
molecules (anabolism).
 Enzymes
Definition
Organic (catalysts) in cells that speed
up chemical reactions without getting
changed or consumed themselves.

Enzymes are typically proteins, but

certain types of RNA can also serve as
catalysts. These RNA molecules are
called ribozymes
 Enzyme / Substrate Relationship
Substrate:
It is the reactant upon which an enzyme
reacts.

Enzymes are substrate specific.

Only the active site of the enzyme

actually binds the substrate.
 The Active Site
The reactants and products in enzyme reactions bind to
the enzyme at specific active sites

The 3-dimensional structures of the reactants and

products must be complementary to the 3-dimensional
structure of the active site (like hand and glove, or foot
and shoe)

Most enzyme-substrate interactions are the result of

weak bonds.

The active site may cause the enzyme to hold onto the
substrate in a very specific way.

The active site may provide a micro-environment (e.g.

low pH) which enhances a reaction.
Induced-Fit Model of enzyme catalysis

In this model, the enzyme changes shape on

substrate binding. The active site forms a shape
complementary to the substrate only after the
substrate has been bound
Enzymes orients substrates and
bring them in proximity
 Factors that affect enzyme activity
1- Temperature:

Higher temperature generally causes more

collisions among the molecules and therefore
increases the rate of a reaction. More collisions
increase the likelihood that substrate will collide with
the active site of the enzyme, thus increasing the rate
of an enzyme-catalyzed reaction.

Above a certain temperature, activity begins to

decline because the enzyme begins to denature.

The rate of the reaction therefore increases with

temperature but then decreases
 Factors that affect enzyme activity
2- pH:
Each enzyme has optimal pH that maintains its normal
configuration

A change in pH alters ionization of side chains,

eventually resulting in denaturation
 Factors that affect enzyme activity
3- Enzyme Concentration
If there is insufficient enzyme present,
the reaction will not proceed as fast
as it otherwise would because there
is not enough enzyme for all of the
reactant molecules.

As the amount of enzyme is increased, the rate of

reaction increases. If there are more enzyme
molecules than are needed, adding additional enzyme
will not increase the rate. Reaction rate therefore
increases as enzyme concentration increases but
then it levels off.
 4- Substrate Concentration:
At lower concentrations, the active
sites on most of the enzyme
molecules are not filled because
there is not much substrate. Higher
concentrations cause more
collisions between the molecules.
With more molecules and collisions,
enzymes are more likely to
encounter molecules of reactant.

The maximum velocity of a reaction is reached when

the active sites are almost continuously filled.
Increased substrate concentration after this point will
not increase the rate. Reaction rate therefore
increases as substrate concentration is increased but
it levels off.
 Cofactors
Non-protein molecules that help enzymes
function.

Bind to active site to enhance enzymatic

reactions.

Cofactors may be inorganic metals such as

zinc, iron, or copper.

Coenzymes are organic cofactors (e.g. vitamins)

 Classification of Enzyme
Exoenzymes: extracellular; break down large food
molecules or harmful agents
e.g. Cellulase, amylase, penicillinase

Endoenzymes: intracellular enzymes; varied functions

e.g. Metabolic enzymes

Constitutive enzymes: always present and in relatively

constant amounts

Induced enzymes: produced only when the substrate is

present
 Enzyme's name is often derived from its substrate
or the chemical reaction it catalyzes, with the word
ending in -ase

According to the function they can be classified as:

1-Oxidoreductases: catalyze oxidation/reduction

reactions
2- Transferases: transfer a functional group (e.g.
phosphate group)
3- Hydrolases: catalyze the hydrolysis of various bonds
4- Lyases: cleave various bonds by means other than
hydrolysis and oxidation
5- Isomerases: catalyze isomerization changes within a
single molecule
6- Ligases: join two molecules with covalent bonds
 Enzyme inhibition
A molecule with very similar 3-D shape to
the substrate may bind to active site, block
substrate. This is called a competitive
inhibitor.

Competitive inhibition always depends on

relative concentrations of substrate and
inhibitor. More inhibitor, more inhibition.
Less inhibitor, less inhibition.
 Something that changes protein structure
(e.g. by binding to the enzyme at some
site outside the active site called the
allosteric site) can block enzyme activity.
This is called noncompetitive inhibition.
 Allosteric Regulation
Allosterically regulated enzymes have a
quaternary protein structure (has 2 or more
subunits).

Each subunit of the enzyme has an active site

and an allosteric site.

Allosteric activators stabilizes the active site and

allosteric inhibitors deactivates the active site.

Cooperativity is the binding of one substrate (or

inhibitor) to one active site (or allosteric site) cause
the other subunits to assume the same state
Allosteric Regulation
 Feedback inhibition
Many enzymatic pathways
are regulated by feedback
inhibition.
As an enzyme's product
accumulates, it turns off the
enzyme.
The end product of the
pathway binds to an
allosteric site on the first
enzyme in the pathway and
shuts down the entire
sequence.
Summary