Chapter 5

ENZYMES
5.1 BIOLOGICAL CATALYSTS

1)Describe a catalyst as a substance that increases

the rate of a chemical reaction and is not
changed by the reaction

A catalyst is a substance that facilitates a chemical reaction by lowering the activation

energy required for the reaction to proceed, thus increasing its rate, without being
consumed or altered in the process. In other words, it speeds up the reaction without
being permanently changed itself. Catalysts provide an alternative reaction pathway that
requires less energy, allowing reactant molecules to more easily overcome the energy
barrier and transform into products. Once the reaction is complete, the catalyst remains
unchanged and available to catalyze further reactions. This property makes catalysts
highly efficient and economical in various industrial and biological processes, as they can
be reused multiple times.

2 Describe enzymes as proteins that are involved

in all metabolic reactions, where they function as
biological catalysts

Enzymes are specialized proteins that play a fundamental role in virtually all metabolic
reactions within living organisms. As biological catalysts, enzymes facilitate these
reactions by speeding up the rate at which they occur without being consumed in the
process.

Enzymes achieve this catalytic function through their unique three-dimensional

structures, which include active sites specifically designed to bind with particular
substrate molecules. This binding process forms an enzyme-substrate complex, allowing
the enzyme to lower the activation energy required for the reaction to proceed, thus
increasing the reaction rate.

Moreover, enzymes are highly specific in their actions, meaning that each enzyme
typically catalyzes only one type of reaction or a specific set of closely related reactions.
This specificity ensures that metabolic processes occur in a highly regulated and
controlled manner within cells.
Overall, enzymes are indispensable to life as they regulate and facilitate a vast array of
biochemical reactions essential for processes such as digestion, energy production,
cellular signaling, and the synthesis of biomolecules.

3 Describe why enzymes are important in all living organisms in terms of a reaction rate
necessary to sustain life

Enzymes are crucial to all living organisms because they enable the necessary biochemical
reactions to occur at rates compatible with life. Here's why enzymes are essential for
sustaining life:

1. **Reaction Rate Regulation**: Enzymes significantly increase the rate of chemical

reactions without being consumed in the process. This acceleration is crucial because
many biochemical reactions required for life processes occur too slowly to sustain life
without enzymatic assistance. Enzymes lower the activation energy barrier, making
reactions occur more rapidly.

2. **Metabolic Pathways**: Living organisms rely on complex networks of metabolic

pathways to maintain homeostasis, produce energy, synthesize biomolecules, and
eliminate waste. Enzymes act as catalysts at each step of these pathways, ensuring that
the necessary reactions proceed efficiently and in the correct sequence.

3. **Energy Production**: Enzymes are essential for energy metabolism. For example,
enzymes like ATP synthase are involved in the synthesis of adenosine triphosphate (ATP),
the primary energy currency of cells. Enzymes involved in processes such as glycolysis, the
citric acid cycle, and oxidative phosphorylation facilitate the breakdown of nutrients to
generate ATP.

4. **Digestion and Nutrient Absorption**: Enzymes play a critical role in the digestion of
food and the absorption of nutrients. Enzymes such as amylase, lipase, and protease
catalyze the breakdown of carbohydrates, fats, and proteins, respectively, into smaller
molecules that can be absorbed and utilized by cells.

5. **Cellular Signaling**: Enzymes participate in various signaling pathways within cells.

Kinases, for example, are enzymes that add phosphate groups to proteins, thereby
regulating their activity and participating in cell signaling cascades that control processes
such as growth, differentiation, and apoptosis.
6. **Detoxification**: Enzymes are involved in detoxifying harmful substances that
organisms encounter in their environment. Enzymes like cytochrome P450s catalyze the
oxidation of toxins, drugs, and foreign compounds, making them more water-soluble and
easier to excrete from the body.

Overall, enzymes are indispensable for life as they enable organisms to carry out the
myriad biochemical processes necessary for growth, development, reproduction, and
survival. Without enzymes, these processes would occur too slowly or not at all, leading to
the inability of organisms to sustain life.

Describe enzyme action with reference to the shape of the active site of an enzyme being
complementary to its substrate and the formation of products

Enzyme action relies heavily on the specificity and complementary shape of the enzyme's
active site to its substrate. The active site is a region on the surface of the enzyme where
the substrate molecule binds, forming the enzyme-substrate complex. This active site has
a specific three-dimensional shape that is complementary to the shape of the substrate
molecule.

When the substrate molecule approaches the enzyme, it fits into the active site like a key
into a lock, forming a temporary enzyme-substrate complex. This binding occurs due to
various types of interactions, including hydrogen bonds, hydrophobic interactions, and
electrostatic attractions, between specific functional groups on the enzyme and substrate.

Once the substrate is bound to the active site, the enzyme undergoes conformational
changes, which may involve slight alterations in its shape, to further enhance the fit
between the enzyme and substrate. These changes often result in the activation of the
substrate, making it more reactive or facilitating the catalytic reaction.

The enzyme facilitates the conversion of the substrate into one or more products by
lowering the activation energy required for the reaction to occur. This lowering of
activation energy enables the chemical bonds in the substrate molecule to be broken or
rearranged more readily, leading to the formation of products.

After the reaction is complete, the products are released from the active site, and the
enzyme returns to its original conformation, ready to catalyze another round of reactions
with additional substrate molecules. It's essential to note that enzymes themselves remain
unchanged at the end of the reaction and can be reused multiple times.

Overall, the complementary shape of the active site to its substrate ensures the specificity
of enzyme-substrate interactions, while the catalytic action of the enzyme facilitates the
conversion of substrate molecules into products by lowering the activation energy barrier
for the reaction.

Investigate and describe the effect of changes in temperature and pH on enzyme activity
with reference to optimum temperature and denaturation

Certainly! Let's delve into how temperature and pH affect enzyme activity:

**Temperature:**
Enzymes have an optimal temperature at which they function most effectively. This
temperature varies depending on the specific enzyme and its natural environment.
Typically, enzymes from human bodies have an optimal temperature around 37°C (98.6°F),
which is the normal body temperature. However, enzymes from organisms living in
extreme conditions, such as in hot springs or cold ocean depths, may have different
optimal temperatures.

As the temperature increases from the optimal point, enzyme activity generally increases
due to the higher kinetic energy of molecules, which leads to more collisions between
enzymes and substrates. This results in faster reaction rates. However, beyond a certain
point, usually around 40-50°C (104-122°F) for most enzymes, the enzyme starts to
denature.

**Denaturation** occurs when the protein structure of the enzyme unfolds or changes
shape, disrupting the active site and making it unable to bind with the substrate
effectively. Denaturation is irreversible and leads to a permanent loss of enzyme activity.
At extremely high temperatures, the enzyme becomes completely denatured, rendering it
inactive.

Conversely, at lower temperatures, enzyme activity decreases due to reduced kinetic

energy, which slows down molecular motion and the frequency of enzyme-substrate
collisions. Extremely low temperatures can also cause enzymes to become inactive,
although they typically don't denature at these temperatures.
**pH:**
Enzymes also have an optimal pH at which they function best. This optimal pH varies
depending on the enzyme's specific structure and the environment in which it operates.
Enzymes can be classified into three broad categories based on their optimal pH:

1. **Acidic enzymes:** Optimal pH below 7 (acidic conditions).

2. **Neutral enzymes:** Optimal pH around 7 (neutral conditions).
3. **Basic enzymes:** Optimal pH above 7 (basic or alkaline conditions).

Deviation from the optimal pH can affect enzyme activity by altering the ionization state
of amino acid side chains involved in the enzyme's active site or by changing the overall
protein structure.

Extreme pH levels can denature enzymes by disrupting hydrogen bonds and electrostatic
interactions that stabilize the enzyme's tertiary structure. This denaturation leads to a
loss of enzyme activity. Some enzymes are more sensitive to changes in pH than others,
and their activity may decrease gradually or abruptly outside their optimal pH range.

In summary, both temperature and pH can significantly affect enzyme activity. Enzymes
have optimal ranges for both factors, and deviations from these ranges can lead to
denaturation and a loss of enzyme function. Understanding these factors is crucial for
various applications, such as biotechnology and medicine, where enzymes are used
extensively.

Explain enzyme action with reference to: active site, enzyme-substrate complex, substrate
and product
**6. Enzyme Action:**
Enzyme action involves the interaction between an enzyme and its substrate to catalyze a
chemical reaction. The key elements in this process include:

- **Active site:** This is a region on the surface of the enzyme where the substrate
molecule binds. The active site has a specific three-dimensional shape that is
complementary to the shape of the substrate.

- **Enzyme-substrate complex:** When the substrate molecule binds to the active site, it
forms a temporary structure called the enzyme-substrate complex. This complex brings
the substrate molecules into close proximity, which facilitates the chemical reaction.
- **Substrate:** The substrate is the molecule upon which the enzyme acts. It binds to the
active site of the enzyme and undergoes a chemical reaction, resulting in the formation of
products.

- **Product:** The product is the molecule that is formed as a result of the

enzyme-catalyzed reaction. After the reaction is complete, the products are released from
the active site, and the enzyme is free to catalyze another reaction.

Explain the specificity of enzymes in terms of the complementary shape and fit of the
active site with the substrate
**7. Specificity of Enzymes:**
Enzymes exhibit specificity in their interactions with substrates, primarily due to the
complementary shape and fit of the active site with the substrate. This specificity arises
from the precise arrangement of amino acid residues within the active site, which creates
a unique three-dimensional structure.

When a substrate molecule approaches the enzyme, it fits into the active site like a key
into a lock, due to the complementary shapes of the two molecules. This ensures that only
specific substrates can bind to the active site, while other molecules cannot. The
specificity of enzymes allows them to catalyze specific reactions in complex biological
systems with high efficiency.
Explain the effect of changes in temperature on enzyme activity in terms of kinetic energy,
shape and fit, frequency of effective collisions and denaturation
**8. Effect of Temperature on Enzyme Activity:**
Changes in temperature can significantly affect enzyme activity due to their impact on
various factors:

- **Kinetic energy:** Increasing temperature provides more kinetic energy to molecules,

leading to higher rates of collisions between enzymes and substrates, and thus increasing
enzyme activity.

- **Shape and fit:** However, excessive heat can disrupt the weak bonds and interactions
that maintain the enzyme's three-dimensional structure, causing it to change shape and
lose its ability to bind substrates effectively.
- **Frequency of effective collisions:** Initially, rising temperature increases the
frequency of effective collisions between enzymes and substrates, enhancing enzyme
activity. But beyond a certain point, denaturation occurs, reducing enzyme activity.

- **Denaturation:** Denaturation is the irreversible loss of the enzyme's native structure,

wPhich renders it inactive. It occurs at high temperatures when the enzyme's structure is
disrupted due to excessive kinetic energy.

Explain the effect of changes in pH on enzyme activity in terms of shape and fit and
denaturation
**9. Effect of pH on Enzyme Activity:**
Changes in pH can also influence enzyme activity, primarily through their effects on
enzyme structure and stability:

- **Shape and fit:** pH changes alter the ionization states of amino acid residues within
the enzyme's active site, affecting its three-dimensional structure and the fit between the
enzyme and substrate.

- **Denaturation:** Extreme pH levels can disrupt the hydrogen bonds and electrostatic
interactions that maintain the enzyme's structure, leading to denaturation and loss of
activity. Enzymes typically have an optimal pH at which they function most effectively, and
deviations from this pH can decrease enzyme activity.