Enzymes

Enzymes are biological catalyst. Catalyst speed up reactions. Almost all of the
chemical reactions in living systems take place with the help of enzymes. In
fact, some biochemical processes would not take place at all without enzymes.

Enzymes speed up the rate of chemical

reactions by lowering the activation
energy (the amount of energy needed to
start the reaction).

Increase rate - Decrease energy.

Enzymes consist of one or two

components. Enzymes consist of one
component: it is a protein that catalyzes
a chemical reaction.
Enzymes (haloenzymes) consist of two
main components: a protein component and a non-protein component
called a cofactor. The cofactor can
be a metal ion or an organic
molecule.

If it is metal ion, we call cofactor:

Metal cofactor - these are the
inorganic substances hold loosely
with the protein part.
If it is organic molecule, we call
cofactor:
a) Co enzyme - these are the organic substances which are hold loosely with
the apoenzyme or
b) Prosthetic group - these are the organic substances held tightly with the
protein part.

The protein component provides the structural framework for the enzyme,
while the cofactor assists in the enzyme's catalytic activity. These
components work together to enable the enzyme to carry out its specific
biochemical function.

The SUBSTRATE is the REACTANT in the

chemical reaction that is catalyzed by the enzyme,
the substance that is CHANGED.

The ACTIVE SITE is the region on the enzyme

where the substrate attaches; the shape of the
active site determines which substrates the enzyme
can bind.

The PRODUCT is what you end up with after the chemical reaction has
occurred.
Biochemical function of enzymes:
1. Enzymes are highly specific: they catalyze only one chemical reaction,
having a specific substrate. This specificity results from an enzyme’s
specific 3-dimensional shape.
2. The part of the enzyme that binds to the substrate is called the active site.
The active site has a 3- dimensional shape that precisely matches the 3-
dimensional shape of the molecule to be reacted, called the substrate.
3. When the substrate and enzyme bind temporarily, an enzyme-substrate
complex is formed.
4. The activation energy needed for the reaction to occur is reduced.
5. After the reaction is complete, the substrate has formed a new product or
products and the enzyme is released to be reused.

1. Lock and Key model – the substrate molecule has a specific 3-

dimensional shape that allows it to fit into the specific 3-dimensional shape of
an enzyme’s active site. Both enzyme and substrate already exist in these
specific 3-dimensional shapes.

2. Induced Fit model – Some enzymes are flexible structures. An enzyme

might wrap its active site around the substrate as the substrate approaches.
An interaction between the enzyme and substrate induces or changes the
shape of the molecules to produce a suitable fit.
Several factors affect the rate at which enzymatic reactions proceed -
temperature, pH, enzyme concentration, substrate concentration, and the
presence of any inhibitors or activators.

a) The concentration of enzyme: Assuming a sufficient concentration of

substrate is available, increasing enzyme concentration will increase the
enzyme reaction rate.

b) The concentration of substrate: At a constant enzyme concentration

and at lower concentrations of substrates, the substrate concentration is
the limiting factor. As the substrate concentration increases, the enzyme
reaction rate increases. However, at very high substrate concentrations,
the enzymes become saturated with substrate and a higher concentration
of substrate does not increase the reaction rate.

c) The temperature: Each enzyme has an optimum temperature at which it

works best. A higher temperature generally results in an increase in
enzyme activity. As the temperature increases, molecular motion
increases resulting in more molecular collisions. If, however, the
temperature rises above a certain point, the heat will denature the
enzyme, causing it to lose its three-dimensional functional shape by
denaturing its hydrogen bonds. Cold temperature, on the other hand,
slows down enzyme activity by decreasing molecular motion.

d) The pH: Each enzyme has an optimal pH that helps maintain its three-
dimensional shape. Changes in pH may denature enzymes by altering the
enzyme's charge. This alters the ionic bonds of the enzyme that
contribute to its functional shape.
e) The presence of activators or inhibitors:

Activators: molecules that increase the activity of an enzyme.

Inhibitors: molecules that decrease the activity of an enzyme.

Competitive inhibition:
An inhibitor may bind to an enzyme and block binding of the substrate, for
example, by attaching to the active site. This is called competitive inhibition,
because the inhibitor “competes” with the substrate for the enzyme. That is,
only the inhibitor or the substrate can be bound at a given moment.

Noncompetitive inhibition:
In noncompetitive inhibition, the inhibitor doesn't block the substrate from
binding to the active site. Instead, it attaches at another site and blocks the
enzyme from doing its job. This inhibition is said to be "noncompetitive"
because the inhibitor and substrate can both be bound at the same time.

Uncompetitive inhibition:
Uncompetitive inhibitor binds to the enzyme-substrate complex only but not to
the free enzyme. Besides this property, enzyme-substrate-inhibitor complex
does not form product because of the conformation change of enzyme.

Enzyme regulation refers to the multiple mechanisms available to control the

activity of enzymes.

Feedback inhibition:
Key metabolic enzymes are often inhibited by the end product of the pathway
they control (feedback inhibition). In the process of feedback inhibition, the
end product of a metabolic pathway acts on the key enzyme regulating entry
to that pathway, keeping more of the end product from being produced.
Allosteric regulation:
Allosteric regulation, broadly speaking, is just any form of regulation where the
regulatory molecule (an activator or inhibitor) binds to an enzyme someplace
other than the active site. The place where the regulator binds is called
the allosteric site. Pretty much all cases of noncompetitive inhibition (along
with some unique cases of competitive inhibition) are forms of allosteric
regulation.