General Biology 1

Metabolism
and
Enzymes

Presented by: Joan A. Riparip

Learning Objectives
• At the end of the lesson, you should be able to:

• Explain Metabolism
• Describe Anabolism and Catabolism
• Describe the components of an enzyme
• Determine how factors such as pH,
temperature, and substrate affect enzyme
activity
 Metabolism

Fig. 1 The ideal metabolism of an average adult human body

 Metabolism
• A series of chemical reactions in the body that
converts food into energy. In the process of food
conversion, some forms of energy are released as by-
products.

• Metabolism is important in maintaining the living state

of the cells and, thus, of the organism.

• It helps us maintain the characteristics of life- growth,

reproduction, repair of damaged parts, and ability to
respond to the environment.
 Catabolism
• This process involves the breakdown of molecules to
release energy.

• Breakdown of polysaccharides into monosaccharides to generate

energy
• Breakdown of nucleic acid into nucleotides for transmitting
genetic information
• Breakdown of proteins into amino acids, either to make new ones
or to produce glucose in the blood
• Breakdown of food in the stomach for the nutrients to be
absorbed in to the blood vessels
 Anabolism
•

• Our bodies use simple chemicals and molecules to synthesize

(or build) a vast array of products and substances, such as
biomolecules, so that they can serve important functions.

• Building proteins fro amino acids

• Cell reproduction, where cells multiply to increase tissue size
• Mineralization of bones from inorganic substances
• Production of hormones necessary for certain organs to perform
their functions
Answer this!

1. What are the signs of overeating?

What are the bad effects of eating

too much?
 Enzymes
Enzymes are basically proteins
that are produced by living
organisms to bring about certain
metabolic and biochemical
reactions in the body.

They are biological catalysts that

speed up reactions inside the body
 Enzymes
Not all enzymes are proteins. Some
enzymes are also made of RNA molecules.
Example of these are the ribozymes, which
synthesize the proteins in the ribosomes
of cells.
Ribozymes undergo catabolism to help
build protein chains during protein
synthesis. This is why they are also called
catalytic RNA
 Enzymes
Enzymes usually end in ase

* Lipase (breaks lipids)

* Protease (breaks proteins)
* Maltase (breaks maltose into 2 glucose)

Enzymes are not changed when they

perform their function. (it can be reused!)
 Substrate
Substance the enzyme acts upon

Enzyme Substrate
Lipase Lipid
Protease Protein
Maltase Maltose
 Enzyme Structure
• All amino acids contain a carbon
atom in the middle of the
molecule, the alpha-carbon
• This atom is surrounded by three Work Planning
chemical groups.
• One is an amine group -NH2
• The second one is a carboxyl
group -COOH
• The third group is denoted by R.
This is the variable radical group
and is different for every amino
acid. This R group makes the
amino acid unique.
Enzyme Structure
• Enzymes are actually made up
of 1000s of amino acids that
are linked in a specific way to
form different enzymes.

• The enzyme chains fold over to

form unique shapes and it is
these shapes that provide the
enzyme with its characteristic
chemical potential
Components of an
Enzyme
1. Apoenzyme/Apoprotein

• Apoenzymes are those enzymes which require an organic or inorganic

cofactor to perform their specific functions but do not have one
bound.

• In other words, Apoenzymes are enzymes that lack their necessary

cofactor(s) for performing their specific function. Apoenzyme is an
inactive form of some enzyme.

• Apoenzyme is also called a proenzyme or zymogen.

2. Cofactors

• Cofactors are either one or more inorganic (e.g. metal ions and
iron-sulfur clusters) or a complex organic or metalloorganic (e.g.
flavin and heme), non-protein chemical compounds that assist in
the biochemical transformation of an Apoenzyme.

• Cofactors also known as that assist

apoenzyme during the catalysis of reactions.

• Some sources also limit the use of the term to

inorganic ions.
 Types of Cofactors
• Metal ion activators are not permanently bound to the
apoenzyme. They supply positive charges to the enzyme
through covalent bonding.

• Example of these metals include magnesium (Mg+2), zinc

(Zn+2), manganese (Mn+2), sodium (Na+1), Iron (Fe+2) and
potassium (K+1) and copper (Cu+2).

• These metals are actually the dietary minerals that are part
of your daily nutritional requirements. Without these, some
of the required catalytic reactions may not proceed.
 Types of Cofactors

• Coenzymes are organic molecules that usually come

from the vitamins that you take in every day. Like the
metal ion activators, they temporarily bind to
apoenzymes.

• Prosthetic cofactors can be either metal ions or

organic molecules. The only difference is that they
bind to apoenzymes permanently
 VITAMIN FUNCTION (S)
B1 Thiamine Part of coenzyme cocarboxylase; has several functions, including
the metabolism of pyruvate
B2 Riboflavin Coenzyme in flavoproteins; helps transfer electrons
B6 Pyridoxine Coenzyme in amino acid metabolism
B12 Helps in the transfer of methyl groups (methyl cyanocobalamide);
cyanocobalamin active in amino acid metabolism
Niacin (nicotinic Part of the nicotinic acid dinucleotide (NAD) molecule; helps
acid) transfer electrons
Pantothenic acid Part of coenzyme A; metabolizes pyruvate and lipids
Biotin Helps in carbon dioxide fixation reactions and fatty acid synthesis
Folic Acid Coenzyme involved in the synthesis of purines and pyrimidines
Vitamin E Coenzyme involved in cellular and molecular synthesis
Vitamin K Coenzyme used in electron transport (napthoquinones and
quinones)
Table. 1. List of selected vitamins as enzyme cofactors and their function
2. Holoenzyme
• The Holoenzyme is the combination Apoenzyme & Cofactor that
activated complex of an enzyme for a specific catalytic action.

• Holoenzymes are the active form of an apoenzyme.

• Here co-factor may be inorganic ions or organic or

metallorganic (coenzyme).

Example of Holoenzyme
• DNA polymerase,
• RNA polymerase etc.
 Enzymes increase the reaction rate by
lowering the energy of activation. They do
How do NOT change Gibbs free energy or .

enzymes
work?
Enzymes work by
lowering the energy of
activation
Enzymes help reduce the activation energy of the complex
molecules in the reaction.

• The following steps simplify how an enzyme works to speed

up a reaction:

the substrate molecules can

bind to. Thus, an enzyme-
substrate complex is
formed.
Enzymes help reduce the activation energy of the complex
molecules in the reaction.

• The following steps simplify how an enzyme works to speed

up a reaction:

2
This enzyme-substrate
molecule now reacts with the
second substrate to form the
product and the enzyme is
liberated as the second
product.
Enzymes help reduce the activation energy of the complex
molecules in the reaction.

• The following steps simplify how an enzyme works to speed

up a reaction:
 Enzymes with highest
Enzymes are highly specificity and accuracy
specific for the are involved in copying
type of the and expression of
genome.
reaction they
catalyze and for These enzymes have a
proof reading function
their substrate. e.g. DNA Polymerase
 Lock and Key Hypothesis
This is the most accepted of the theories of
enzyme action.
This theory states that the substrate fits exactly
into the active site of the enzyme to form an
enzyme-substrate complex.

This model also describes why enzymes are so

specific in their action because they are specific to
the substrate molecules.
 Induced Fit Hypothesis

The induced fit is a theory that explains the binding

of a substrate into an active site of an enzyme that
does not have a correct conformation with that of
the active site.

According to this theory, confirmation of the active

site modifies into a correct shape when the
substrate binds.
 How do
enzymes
work?
Enzymes work by
lowering the energy of
activation

https://www.differencebetween.com/difference-between-induced-fit-and-lock-and-key/
Enzyme Example Ribonuclease
Ribonuclease
decomposes RNA, and the
nucleotides can be
recycled.

The purple part is the

enzyme; the green part is
the substrate (RNA).
Factors Affecting
Enzymatic Speed
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.

• For humans, the optimal temperature for

human cells is around 37.5oC When this
temperature is elevated, the enzyme
structure starts to undergo denaturation or
breaking down.
2. Substrate Concentration
• Because the enzyme requires the presence of a
substrate to act as a catalyst, the substrate
concentration is directly related to enzyme
activity.
• Low substrate concentrations compared to
enzymes mean that only so many enzymes can
bind to the substrate and push the reaction
forward; thus, the reaction will slow down in low
substrate concentration.

• Provide a greater substrate concentration and,

as long as there are enzymes present, the
reaction will proceed at an optimal rate.
2. Substrate Concentration

• However, at high substrate levels, the reaction rate will begin to plateau and remain
constant.
• This reaction occurs because of enzyme saturation; at this point, all enzymes are
bound to substrate, and increasing substrate levels will affect the reaction rate
3. Optimal pH

• Enzymes are protein substances that contain acidic carboxylic groups

(COOH ) and basic amino groups (NH2). So, the enzymes are affected by
changing the pH value.

• Each enzyme has a pH value that it works at with maximum efficiency called
the optimal pH. If the pH is lower or higher than the optimal pH, the enzyme
activity decreases until it stops working.
3. Optimal pH

• For example, pepsin works at a

low pH, i.e, it is highly acidic,
while trypsin works at a high pH,
i.e, it is basic. Most enzymes
work at neutral pH 7.4.
3. Optimal pH

Table 2. Examples of enzymes in humans, their function, pH range, and optimal pH

4. Enzyme Cofactors
• Some enzymes need the addition of inorganic ions or
coenzymes to help speed up the rate of reaction. These are
small organic molecules in trace amounts that can promote
enzymatic activities. They help bind the substrate to the active
site or participate in the reaction at the active site.

• Vitamins either become part of the molecular

structure or become coenzymes themselves, such that if
vitamins are insufficient or deficient, certain vitamin disorder
occur. Riboflavin deficiency, for instance, results in cracks at
the corners of the mouth.
5. Enzyme Inhibitors

• There are instances when enzyme activity should be limited.

The molecule that binds to the enzyme to decrease its activity
is called enzyme inhibitor.

• The end product itself may be used as the inhibitor. Enzyme

inhibition is important in controlling enzymatic reactions
because once the body had completed the necessary chemical
processes, enzymatic reactions have to stop. This is also
beneficial in conserving raw materials and energy of the body.