PRELAB

4
ENZYMES
Instructor: TONG THI HANG
Tuesday morning class
Date: 10/1/2022

Student: Trần Xuân Quỳnh

-BTBTIU21097
 1. What is a catalyst and a catalysis reaction?

- Catalysts have no effect on the equilibrium constant and thus on the equilibrium composition. Catalysts
are substances that speed up a reaction, but which are not consumed by it and do not appear in the net
reaction equation. Also — and this is very important — catalysts affect the forward and reverse rates
equally; this means that catalysts have no effect on the equilibrium constant and thus on the composition
of the equilibrium state. Thus, a catalyst (in this case, sulfuric acid) can be used to speed up a reversible
reaction such as ester formation or its reverse, ester hydrolysis:

-The catalyst has no effect on the equilibrium constant or the direction of the reaction. The direction can
be controlled by adding or removing water (Le Chatelier principle).

-Catalysts function by allowing the reaction to take place through an alternative mechanism that requires
a smaller activation energy. This change is brought about by a specific interaction between the catalyst
and the reaction components. Catalysts provide alternative reaction pathways

-Catalysts are conventionally divided into two categories: 

o Homogeneous
o Heterogeneous. 
o Enzymes, natural biological catalysts, are often included in the former group, but because they share
some properties of but exhibit some very special properties of their own, we will treat them here as a
third category.

-A Catalysis reaction: When heated by itself, a sugar cube (sucrose) melts at 185°C but does not burn.
But if the cube is rubbed in cigarette ashes, it burns before melting owing to the catalytic action of trace
metal compounds in the ashes

2. Compare the basic difference between chemical catalysts and biological catalysts.
 Catalyst Enzyme
Function Catalysts are substances that increase Enzymes are proteins that increase rate of
or decrease the rate of a chemical chemical reactions converting substrate into
reaction but remain unchanged. product.
Molecula Low molecular weight compounds. High molecular weight globular proteins.
r weight
Types There are two types of catalysts – There are two types of enzymes - activation
positive and negative catalysts. enzymes and inhibitory enzymes.
Nature Catalysts are simple inorganic Enzymes are complex proteins.
molecules.
Alternate Inorganic catalyst. Organic catalyst or bio catalyst.
terms

Reaction Typically, slower Several times faster

rates
Specificit They are not specific and therefore Enzymes are highly specific producing large
y end up producing residues with errors number of good residues
Condition High temp, pressure Mild conditions, physiological pH and
s temperature
C-C and absent present
C-H
bonds
Example vanadium oxide amylase, lipase
Activatio Lowers it Lowers it
n Energy
3. What are enzymes? Describe their basic four properties?

Enzymes are biocatalysts of protein in nature, which accelerate the rate of biochemical reactions but do
not affect the nature of final product. Like catalyst the enzymes regulate the speed and specificity of
reaction without being used up but unlike catalysts enzymes are produced by the living cells only. Like
catalysts enzymes also influence the rate of biochemical reaction so that they can take place at a
relatively low temperature. Thus, the enzymes are known to lower the activation energy. In many cases
enzymes initiate the biological reaction.
 Catalytic Property
 Specificity
 Reversibility
 Sensitiveness to heat and temperature and pH
Catalytic Property:
Enzymes have extra-ordinary catalytic power. They are active in very small quantities. A small amount
of enzyme is enough to convert a large quantity of substrate. The enzymes remain unchanged after the
reaction. The turnover number of enzymes ranges from 0.5 to 600000. Turn over number is the number
of substrate molecules converted by one molecule of enzymes per second when its active site is
saturated with substrate.
Specificity:
Enzymes are very specific in their action. Enzymes act on substrates only. Enzymes are also specific to a
particular type of reaction. In some rare cases, the specificity may not be too strong. Enzymes show
different types of specificity as follows:
1. Bond Specificity: It is also called as relative specificity. Here the enzymes are specific for a
bond. eg; peptidase is specific or peptide bond, lipase is specific for ester bond in a lipid.
2. Group Specificity: It is also called structural specificity. Here the enzymes are specific for a
group. e.g., pepsin hydrolyze the peptide bonds in with the amino group belongs to aromatic amino
acids.
3. Substrate Specificity: It is also called absolute specificity. Here the enzyme acts only on a
particular substrate. e.g., arginase acts only on arginine; carbonic anhydrase acts only on carbonic
acid.
4. Optical Specificity: It is also called stereo-specificity. This is the highest specificity shown by an
enzyme. Here the enzymes are specific not only to the substrate but also to its optical configuration.
e.g., L amino acid oxidase acts only L-amino acids, not on D-amino acids. Similarly, the alpha-
amylase act only on alpha-14 glycosidic linkage of starch and glycogen. It is not able to hydrolyze
the beta-14 glycosidic linkage of cellulose.
5. Co-factor Specificity: This shows that enzymes are not only specific to the substrate but also
specific to its co-factors.
6. Geometric Specificity: Here the specificity is very less. Some enzymes will work with a small
range of similar substrates having similar structural geometry. e.g., alcohol dehydrogenase can
oxidize methanol and n-propanol to aldehydes.
Reversibility:
Most of the enzyme catalyzed reactions are reversible. The reversibility of the reaction depends upon the
requirements of the cell. In some cases, there are separate enzymes for forward and reverse reaction.
Some enzyme-catalyzed reactions are not reversible.
Sensitivity To Heat, Temperature And pH:
Enzymes are very sensitive to heat and temperature. They are thermolabile. The maximum activity of
Associate in Nursing protein is at traditional temperature. The correct temperature for the utmost activity
is termed optimum temperature. Enzymes will be inactive at very low temperatures; this is the reason for
preserving food and vegetables in the refrigerator. The enzymatic activity increases with the increase in
temperature up to a certain level. At higher temperature (60-70 degree Celsius), the enzyme is destroyed
or denatured. Do you know an enzyme active at very high temperature? It is Taq-Polymerase used in
PCR reactions. The optimum temperature for it is 75 to 80 degrees Celsius.
The optimum pH of most endo-enzyme is pH 7.0 (neutral pH). However, digestive enzymes can
function at different pH. For example, salivary amylase act best at pH 6.8, pepsin act best at pH2 etc.
Any fluctuation in pH scale from the optimum causes ionization of R-groups of amino acids that
decrease the protein activity. Sometime a change in pH causes the reverse reaction, e.g., at pH 7.0
phosphorylase break down starch into glucose 1- phosphate while at pH5 the reverse reaction occurs.
4. How many types of enzymes are there? List them and give at least 1 example
Types Biochemical Property

 Oxidoreductase The enzyme Oxidoreductase catalyzes the oxidation reaction where the electrons
s tend to travel from one form of a molecule to the other.

The Transferases enzymes help in the transportation of the functional group among
 Transferases
acceptors and donor molecules.

Hydrolases are hydrolytic enzymes, which catalyze the hydrolysis reaction by

 Hydrolases
adding water to cleave the bond and hydrolyze it.

Adds water, carbon dioxide or ammonia across double bonds or eliminate these to
 Lyases
create double bonds.

The Isomerases enzymes catalyze the structural shifts present in a molecule, thus
 Isomerases
causing the change in the shape of the molecule.

 Ligases The Ligases enzymes are known to charge the catalysis of a ligation process.
Oxidoreductases: pyruvate dehydrogenase, catalysing the oxidation of pyruvate to acetyl coenzyme A.
Transferases: An example is a transaminase, which transfers an amino group from one molecule to
another.
Hydrolases: For example, the enzyme pepsin hydrolyses peptide bonds in proteins
Lyases: e.g., aldolase (an enzyme in glycolysis) catalyses the splitting of fructose-1, 6-bisphosphate to
glyceraldehyde-3-phosphate and dihydroxyacetone phosphate.
Isomerases: Example: phosphoglucomutase catalyses the conversion of glucose-1-phosphate to
glucose-6-phosphate in glycogenolysis
Ligases: For example, DNA ligase catalyses the joining of two fragments of DNA by forming a
phosphodiester bond.

5. Define the term “optimal temperature” of an enzyme.

 Optimum temperature is the temperature at which enzymes work best. The rate of reaction is greatest at the
optimum temperature
6. What makes biological catalysts specific? Define the “active site” of the enzyme
and the “substrate”?
Biological catalysts work on a very different principle. Rather than being metals with fast-and-loose
electrons, biological catalysts are large complex molecules called enzymes, which contain specific
pockets for the reactants to fit into. Once they are trapped inside the enzyme aids the reaction, either
by forming temporary bonds with the reactants to help them fit together, or by simply holding them
close enough to each other to react and form the product.

-Substrate is enzymes bind with chemical reactants. There may be one or more substrates for each type
of enzyme, depending on the chemical reaction. In some reactions, a single-reactant substrate is broken
down into multiple products. In others, two substrates may come together to create one larger molecule.
Two reactants might also enter a reaction, both become modified, and leave the reaction as two
products.

-The enzyme’s active site binds to the substrate. Since enzymes are proteins, this site is composed of a
unique combination of amino acid residues (side chains or R groups). Each amino acid residue can be
large or small; weakly acidic or basic; hydrophilic or hydrophobic; and positively charged, negatively
charged, or neutral. The positions, sequences, structures, and properties of these residues create a very
specific chemical environment within the active site. A specific chemical substrate matches this site like
a jigsaw puzzle piece and makes the enzyme specific to its substrate.