Chapter 5

Metabolism and Enzymes

Metabolism

• all chemical reactions that occur in a living organism

• involve
– conversion of food into energy in the form of ATP
– formation carbohydrate, protein, lipid and nucleic acid
• 2 types:
– catabolism
– anabolism
 Catabolism
Process of breaking down
complex substances into simple
substance
PQ P + Q
The reaction release energy when
chemical bond is broken down
E.g. :
1. Breakdown of glucose during
cellular respiration to produce
energy
2. Breakdown of one lipid
molecule into fatty acid and
glycerol
Anabolism
Process of synthesising complex
molecules from simple molecules.
P + Q PQ
The reaction uses or absorbed
energy to form chemical bond
E.g. :
1. Formation of glucose during
photosynthesis
2. Synthesising of lipid from fatty
acid and glycerol
Enzyme

• an organic catalyst that is mostly made up of proteins

• speed up biochemical reactions in the cell
• produced by living cell organisms
• Starts with a substrate molecule; ends with a product(s)
• Substrates => substances needed for an enzyme reaction
– bind with enzyme at specific site (known as active site) =>
enzyme - substrate complesx is formed.
 Naming the enzyme
• adding '-ase' to the name of the substrate it catalyses.
• few enzyme do not follow this naming system : trypsin, pepsin, renin,
erepsin
Substrate Catabolism Reaction /Hydrolysis
Lactose Lactose + water lactase glucose + galactose
Sucrose Sucrose + water sucrase glucose + fructose
Maltose Maltose + water maltase glucose + glucose
Cellulose Cellulose + water cellulase glucose + glucose

Lipid Lipid + water lipase glycerol + fatty acid

Starch Starch + water amylase maltose
(amylose)
Characteristics of Enzymes
Occurs rapidly

Required in small quantity and are reusable/used repeatedly

Enzyme activity can be slowed down /stopped by inhibitors (heavy metal)

Structure does not change and not destroyed at the end of reaction

Highly specific

Reactions catalysed by enzymes are reversible

Speed up bichemical reaction

Some enzymes need cofactors (Vit. B / Mg2+)to work more efficiently

Intracellular and Extracellular Enzymes

• Intracellular enzymes
– enzymes that are synthesised in a cell for its own use
– E.g. : hexokinase enzyme that is used in the glycolysis process
durin gcellular respiration
• Extracellular enzymes
– enzymes that are secreted outside the cell
– E.g.: trypsin is produced by pancreatic cells and secreted into
duodenum to break down polypeptide.
 1. Ribosome :
synthesise
5. Proteins are
protein
modified to form
enzymes then
2.Protein enter the secreted in secretory
lumen of RER and 6 vesicles ( formed
are transported from the tip of the
2 1 Golgi apparatus)
through it

3. Membrane bud 6. Secretory vesicles

off => transport => moves towards
vesicles is formed plasma membrane
=> fuse with it =>
4. Transport vesicles secrete extracellular
5
(contsin protein) enzyme
moves trowards
Golgi apparatus and 3
fuses with it
4
 Mechanism of enzyme action
§ Enzymes (tertiary protein structure) have active site; active site has
distinctive shape that complements its substrate
§ Shape of substrate must fit the enzyme => for reaction to take place
§ Substrate molecule = key; enzyme = lock => ‘lock and key’
hypothesis
§ Substrate molecules fit into the enzyme at the active site => enzyme-
substrate complex formed (temporary)
§ Reaction occurs; products produced.
§ Now, the products produced have different shape from substrate =>
leaves the active site
§ Active site (enzyme) is now free to receive another substrate
molecule
• Activation Energy
– Energy required to break
molecular bond in
substrates before a reaction
can occur
– Enzymes => lower the
activation energy => rate of
biochemical reaction in the
cell is accelerated.
Factors affecting enzyme activity

Ø4 factors that affect enzyme activity

a. temperature
b. pH
c. substrate concentration
d. enzyme concentration
• Temperature
1 – Low temperature, low rate of reaction
catalysed by enzyme
– Temperature increases => kinetic
energy of the substrate molecules
and enzymes increases; frequency
of effective collision between
substrate molecules and enzyme
molecules increases => rate of
reaction increases
– every 10oC rise, rate of reaction
doubled => only up to optimum
temperature
• Temperature
2 – Optimal temperature => enzyme
reaction is at maximum
– Optimum temperature in human = 37oC
3 – temperature higher than optimum
temperature => bonds that hold enzyme
molecules together begin to break;
altering the 3D shape of enzymes and
will destroy the active sites
§ substrate cannot fit into the active
site; enzyme lose their activities =>
denatured (irreversible)
• pH
q enzyme are sensitive to the changes of pH
q slightly change in pH => large effect on rate of
reaction
q alter the charges on the active sites of the
enzyme and substrate surfaces => ability to
bind each other reduced
q each enzyme only function optimally at a
particular pH
q Optimum pH => pH at which the rate of reaction is at
the maximum
q Most enzyme works best at pH range from 6 to 8
q pH value that the enzyme works best
q Pepsin : pH 2 ; Trypsin : pH 8.5; Salivary amylase : 6.8
• pH change => charge (H+) of
the active site of enzyme and
substrate surface change =>
enzyme-substrate complex
cannot formed
• at optimum pH => charge on
the active site restored =>
enzyme can function
• extreme change in pH value
=> structure of chemical bond
broken and active site
changed => denaturation
occurs
• Substrate concentration
v concentration high => substrate molecules that available to bind the
active sites of enzyme increases => more products produced
v more substrate molecules => chances of collision between substrate
and enzyme increases => reaction occurs faster
v Rate of reaction increases as substrate concentration increases until
the reaction reaches a maximum rate
v After maximum rate, all active site were filled => enzyme become
saturated
Ø concentration of enzyme becomes a limiting factors
• Enzyme concentration
Ø concentration increases => more enzyme
molecules are available (more active site
ready for catalytic action) => rate of reaction
increases
Ø concentration of enzyme doubled => amount
of substrate (must excess of substrate)
converted to products also doubled.
Ø rate of reaction increases as the
concentration of the enzyme increases until
a maximum rate is achieved
Ø after the maximum rate, the concentration
of substrate becomes a limiting factor
Application of Enzyme in Daily Life

• Immobilized Enzymes Technology

– the use of immobilised enzymes that combine with
inert and insoluble substances => to increase the
resistance of enzymes towards change in factors
such as pH and temperature
– Enzyme will remain in the same position throughout
catalytic reaction and is easily separated from the
product.
 Application Enzymes used Uses
Dairy industry Rennin Coagulate milk proteins in cheese
manufacturing
Lipase Used in the ripening of cheese
Baking Amylase Breaks down of starch to glucose
industry
Protease from Breaks down and lower proteins in flour for
microorganisms biscuit manufacture
Processing Trypsin To pre-digest some baby foods
food
Amylase Converts starch to glucose syrup
Food industry Protease To tenderize meat
 Application Enzymes Uses
used
Brewing Amylase from Breaks down starch to glucose for
industry geminating fermentation by yeast
barley
Protease Breaks down protein to amino acids for yeast
Textile Amylase Removes starch that is applied to threads to
industry prevent damage during weaving
Manufacturing Biological Used in washing powder ( get rid of protein,
detergent enzymes starch and fats stains
(protease,
amylase and
lipase