1.

Characterize enzymes, coenzymes, and isoenzymes

Enzymes:

Enzymes are biological catalysts that accelerate chemical reactions in living organisms
without being consumed in the process. They are typically proteins. Enzymes lower the
activation energy required for a reaction to occur, making biochemical processes more
efficient.

Coenzymes:

Coenzymes are organic molecules that assist enzymes in catalyzing reactions. They
often function as carriers of specific functional groups or electrons during enzymatic
reactions such NAD+ (nicotinamide adenine dinucleotide) and FAD (flavin adenine
dinucleotide), which participate in redox reactions.

Isoenzymes:

Isoenzymes are different forms of an enzyme that catalyze the same reaction but may
have distinct properties. They are usually found in different tissues or under different
conditions. Isoenzymes can be used for diagnostic purposes, as changes in their levels
may indicate specific conditions or diseases.

2. State and discuss the different models that would explain the action of enzymes
on substrates.

Models Explaining Enzyme Action:

Lock and Key Model: Describes the specificity of enzymes by likening the enzyme to a
lock and the substrate to a key. The enzyme's active site has a specific shape that fits
only with a particular substrate.

Induced Fit Model: Suggests that the active site of an enzyme is flexible and can adjust
its shape to accommodate the substrate. The binding of the substrate induces a
conformational change in the enzyme.

3. State the function of the following enzymes:

Trypsin:
Function: Trypsin is a digestive enzyme that breaks down proteins in the small
intestine.
Substrate: Acts on peptide bonds, cleaving proteins into smaller peptides.
 Pepsinogen:
Function: Pepsinogen is the precursor to pepsin, an enzyme that digests proteins
in the stomach.
Activation: Converted to pepsin by the acidic environment of the stomach.

Lipase:
Function: Lipase is involved in the digestion of fats (lipids) by breaking them
down into fatty acids and glycerol.
Location: Produced by the pancreas and released into the small intestine.

Peptidase:
Function: Peptidases are enzymes that break down peptides (short chains of
amino acids) into individual amino acids.
Location: Found in the small intestine, facilitating the final stages of protein
digestion.

4. State the clinical significance of the five diagnostic serum enzymes.

● Alanine Aminotransferase (ALT) and Aspartate Aminotransferase (AST):

Elevated levels may indicate liver damage, such as in hepatitis or cirrhosis.

● Creatine Kinase (CK): Elevated levels may suggest muscle damage or

disorders, such as myocardial infarction (heart attack) or muscular dystrophy.

● Lactate Dehydrogenase (LDH): Elevated LDH levels may be indicative of tissue

damage, especially in the heart, liver, or muscles.

● Alkaline Phosphatase (ALP): Elevated ALP levels may be associated with liver
or bone disorders.

● Amylase and Lipase: Elevated levels may indicate pancreatitis, as these

enzymes are involved in the digestion of carbohydrates (amylase) and fats
(lipase).

1. What is enzyme kinetics? Zero –order kinetics? First –order kinetics?

Enzyme kinetics is the study of the rates at which enzymes catalyze chemical reactions.
It involves the measurement and analysis of the rates of enzyme-catalyzed reactions
and the factors that influence these rates.

​ Zero-order kinetics: In zero-order kinetics, the rate of the reaction is independent

of the concentration of the substrate. The reaction rate is constant over time until
the enzyme becomes saturated with substrate.
 ​ First-order kinetics: In first-order kinetics, the rate of the reaction is directly
proportional to the concentration of the substrate. As the substrate concentration
increases, the reaction rate also increases linearly.
​
2. What is meant by saturated level substrate?

Saturated level of substrate: When the concentration of substrate is high enough that all
available enzyme active sites are occupied, the enzyme is said to be saturated. At
saturation, further increases in substrate concentration do not lead to an increase in the
reaction rate because all enzyme active sites are already in use.

3. What is the effects of the following to enzymatic activity:

● Heavy metals: Heavy metals can act as inhibitors of enzymes by binding to the
enzyme and disrupting its structure or interfering with its function. Some heavy
metals can also act as cofactors or activators for certain enzymes.
● Inhibitors: Inhibitors are molecules that decrease the activity of enzymes. They
can be competitive (competing with the substrate for the active site) or
non-competitive (binding to a different site on the enzyme).
● Activators: Activators are molecules that increase the activity of enzymes. They
may bind to the enzyme and induce a conformational change that enhances the
enzyme's catalytic activity.

4. What is meant by maximum velocity?

Maximum velocity (Vmax): Vmax is the maximum rate of an enzymatic reaction, and it
occurs when the enzyme is saturated with substrate. At Vmax, all available enzyme
active sites are occupied, and the rate of the reaction cannot increase further with an
increase in substrate concentration.

5. What are the different models that explain the mode of action of enzymes

● Lock and Key Model: This model suggests that the enzyme's active site has a
specific shape that fits the substrate exactly, like a key fitting into a lock.
● Induced Fit Model: This model proposes that the active site of the enzyme
undergoes conformational changes upon binding to the substrate. The binding
induces a change in the enzyme's shape to better accommodate the substrate.
● Enzyme-Substrate Complex Model: This model emphasizes the formation of a
temporary complex between the enzyme and the substrate during the catalytic
process.