What are enzymes?
 It is a protein or RNA produced by living cells, which is highly specific
and highly catalytic to its substrates.
 A very important type of macromolecular biological catalysts.
 Enzymes act as catalyst in cellular reactions.
 Enzymes catalyze reactions by weakening chemical bonds, which
lowers activation energy.
 The energy required for a chemical reaction to occur is known as
the activation energy.
How do enzymes work?
 Each enzyme has a unique 3-D shape, including a surface groove
called an active cites.
 The enzyme works by binding a specific chemical reactant
(substrate) to its active site, causing the substrate to become
unstable and react.
 The resulting product(s) is then released from the active site.
An enzyme acts on a specific substrate to form an enzyme–
substrate complex because of the fit between their structures. As a result,
something happens to the substrate molecule. For example, it might be split
in two at a particular location. Then the enzyme–substrate complex comes
apart, yielding the enzyme and products. The enzyme is not changed in the
reaction and is now free to react again. Note that the arrows in the formula
for enzyme reaction point both ways. This means that the reaction is
reversible.
Active Site
 The area of an enzyme where the substrate binds.
 Structure has a unique geometric shape that is designed to fit the
molecular shape of the substrate.
 It contain residues that bind the substrate and also participate in
catalysis
Classification of Enzymes
1. OXIDOREDUCTASES- catalyze the transfer of reducing equivalents
from one redox system to another.
- REDOX REACTION/REDOX SYSTEM (PHOTOSYNTHESIS)
H2O2 + H2O2  2H2O + O2
A red + B ox  A ox + B red
 D-glucose-6-phosphate ---- D-fructose-6-phosphate

2. TRANSFERASES- catalyze the transfer of other groups from one molecule All trans-retinene ---- 11-cis-retinene
to another.
- Oxidoreductases and transferases generally require coenzyme A-B-C  A-C-B
- ATP-ADP CYCLE

ATP + D-hexose --- ADP = D-hexose-6-phosphate 6. LIGASES OR SYNTHETASES- are energy-dependent and are therefore
always coupled to the hydrolysis of nucleoside triphosphates.
A – B + C --- A + B - C
-KREB CYCLE

3. HYDROLASES- are also involved in group transfer, but the acceptor is

always a water molecule ATP + acetate + CoA --- AMP + pyrophosphate + acetyl – CoA

- HYDROLYSIS (GLYCOLYSIS) A + B + ATP --- A – B + ADP + Pi

L-arginine + H2O ---- L-ornithine + urea

A – B + H2O ---- A – H + B - OH Formats in writing an enzymatic reaction.

( enzyme )
Reactant+ Reactant -----------> Product
4. LYASES OR DESMOLASES- often also referred to as “synthases”;
- catalyze reactions involving either the cleavage or formation of chemical ( enzyme )
bonds, with double bonds either arising or disappearing. Reactant -----------> Product + Product
- KREB CYCLE
*One or more of the reactants in an enzymatic reaction is the substrate, the
reactant(s) that specifically interacts with the enzyme.
L-malate ---- Fumarate = H2O

A-B  A+B

(reverse reaction: synthase)

5. ISOMERASES- move groups within a molecule, without changing the

gross composition of the substrate.
-KREB CYCLE
How do you stop an enzyme? • Cofactor is more general term. Includes inorganic and organic
molecules.
DENATURED IT!
• Coenzyme is a type of cofactor, but specifically organic molecules.
 Alteration of a protein shape through some form of external stress Ex. Vit B12
 Example, by applying heat or changing pH.
 Denatured protein can’t carry out its cellular function .

C. Inhibitors
Factors That Influence Enzyme Activity
Two Types of Enzyme Inhibitors
A. Temperature and pH 1. COMPETITIVE INHIBITOR
 Temperatures far above the normal range denature
enzymes. (This is why very high fevers are so dangerous. - Chemicals that resemble an enzyme’s normal substrate and
They can cook the body’s proteins.) compete with it for the active site.
 Most enzymes work best near neutral pH (6 to 8).
- Reversible depending on concentration of inhibitor and substrate.

2. NON-COMPETITIVE INHIBITOR
B. Cofactors & Coenzymes
-Do not enter active site, but bind to another part of the enzyme, causing
• Non-protein substances (zinc, iron, copper, vitamins) are sometimes the enzyme & active site to change shape.
need for proper enzymatic activity.
- Usually reversible, depending on concentration of inhibitor &
substrate.
 (catecholase)
Catechol + oxygen ----------------- polyphenol
colorless substrate brown product

Enzyme Inhibitors

Blocking an enzyme's activity can kill a pathogen or correct a metabolic  Lemon juice and other acids are used to preserve color in fruit,
imbalance. particularly apples, by lowering the pH and removing the copper
(cofactor) necessary for the enzyme to function.
 Many medications are enzyme inhibitors.
 Enzyme inhibitors are also used as herbicides and pesticides.
Reaction:

EXAMPLE:
 Another example of competitive inhibition is protease inhibitors.
 They are a class of anti-retroviral drugs used to treat HIV.
 The structure of the drug ritonavir (say ri-TAHN-a-veer) resembles
the substrate of HIV protease, an enzyme required for HIV to be
made.
Meet the Enzyme: Catecholase
 Catecholase is present in most fruits and vegetables.
 It is the enzyme that facilitates the browning of cut or bruised fruits
and vegetables by catalyzing the following reaction:
catecholase
catechol + O2 ---------- polyphenol
colorless substrate brown product
Meet the Enzyme: Bromelain
 Pineapple contains enzyme bromelain, which can digest protein.
 Jell-O® is made of gelatin, a processed version of a structural protein
called collagen found in many animals, including humans.
 Collagen = big, fibrous molecule makes skin, bones, and tendons
both strong and elastic.
 Gelatin you eat in Jell-O ® comes from the collagen in cow or pig
bones, hooves, and connective tissues. (Yummie!)