METABOLISM

ENZYMES
Metabolism
Metabolism describes the totality of chemical reactions that occur within a cell or organism
• This complex web of interdependent processes are controlled and coordinated by enzymes

Metabolic reactions serve two key functions within organisms:

• They provide a source of energy for living processes (such as movement and reproduction)
• They enable the synthesis and assimilation of new organic materials for use within the cell

Nutrients are converted

into new materials and
energy (waste excreted)

C1.1.2 Role of enzymes in metabolism

Types of Metabolism
Metabolic reactions can be classed as either anabolic or catabolic
Ana Build
• Mnemonic: Anabolic = Anna Builder ; Catabolic = Cat Breaker

Anabolism:
• Building complex macromolecules from simpler biomolecules
• Examples: Photosynthesis and formation of organic polymers
Cat
Catabolism: Break

• Breaking down the macromolecules into simpler building blocks

• Examples: Digestion (via hydrolysis) and respiration (via oxidation)

C1.1.3 Anabolic and catabolic reactions

Enzymes
Enzymes are globular proteins that act as biological catalysts by increasing the rate of reaction
• Enzymes are not consumed by the reactions they catalyse and can be continually re-used

An enzyme will catalyse the chemical conversion of reactants (called substrates) into products
• Enzymes are named according to their substrate and end with the suffix ‘-ase’ (e.g. lipase)

Substrate + Enzyme Enzymatic Catalysis Products + Enzyme

C1.1.1 Enzymes as catalysts

Substrate Specificity
The region on the surface of the enzyme to which a substrate binds is called the active site
• An active site is complementary in shape and charge to a substrate (resulting in specificity)

The active site is only composed of a few amino acids but confers a unique overall 3-D shape
• Hence different enzymes are required to catalyse the conversion of different substrates

Enzymes are specific

to a given substrate
and can only catalyse
particular reactions

C1.1.4 Enzymes as globular proteins with an active site for catalysis

Activation Energy
Enzymes catalyse chemical reactions by lowering the activation energy needed to proceed
• The activation energy threshold (EA) is the level of energy required to trigger the reaction

Lower energy
High energy threshold
threshold (EA)
limits the reaction

Enzyme Absent = Higher Activation Energy Enzyme Present = Lower Activation Energy

C1.1.10 Effect of enzymes on activation energy

Chemical Energetics

* Click on the images to show the consequence of the addition of an enzyme on the rate of the reactions
Catalysis
According to the induced fit model, the enzyme’s active site is not a
completely rigid structure and will change shape to fit the substrate

• The active site will improve binding via a conformational change

This change in structure promotes catalytic activity in the enzyme:

• The conformational changes stresses bonds in the substrate and

increases the reactivity of the molecule (lower activation energy)

• The conformational change in shape allows for broad specificity

(for example, a lipase can bind to a variety of different lipids)

C1.1.5 Interactions between substrate and active site to allow induced-fit binding
Enzyme Activity
Enzyme activity can be measured via the consumption of substrates or formation of products
• The rate of reaction can be determined by the time taken to achieve a particular outcome

Examples of methodologies for measuring the activity of enzymatic reactions may include:

Enzyme Chemical Reaction Measurement

Catalase Hydrogen peroxide (liquid) → Oxygen (gas) Pressure change (data logger)
Pectinase Pectin (solid) → Simple sugars (liquid) Percentage weight loss
Pepsin Protein → Shorter polypeptide chains Colour change (Biuret’s test)
Rennin Casein (soluble) → Casein (insoluble) Mass of precipitate formed

C1.1.9 Measurements in enzyme-catalysed reactions

Factors Affecting Activity
A variety of factors may affect the rate of an enzyme-catalysed reaction by either:
• Affecting the frequency of successful collisions between the enzyme and the substrate
• Affecting the capacity for the substrate to interact with the enzyme (e.g. via denaturation)

Examples of factors that affect the activity of an enzyme-catalysed reaction include:

• Temperature (heat)
• pH (acidity vs alkalinity)
• Substrate concentration
pH
• Enzyme concentration

C1.1.8 Effects of temperature, pH and substrate concentration on the rate of enzyme activity
Molecular Collisions
For enzymes and substrates to interact, they must first collide in
the correct orientation (a substrate must bind to the active site)

The rate of enzyme activity can be improved by increasing the

frequency of successful collisions via two key interventions:
• Increasing the level of molecular motion ( kinetic energy)
• Increasing concentrations of particles (enzyme or substrate)
Movement is needed
Enzymes or substrates may be immobilised (e.g. embedded to for a substrate and an
a membrane) to localise the chemical reaction to a certain site active site to collide

C1.1.6 Role of molecular motion and substrate-active site collisions in enzyme catalysis
Denaturation
Enzyme activity is dependent on the 3-dimensional shape of a protein (i.e. tertiary structure)
• Catalysis will only occur if the substrate can successfully bind to the enzyme’s active site

Denaturation can diminish enzyme activity by breaking the bonds involved in protein folding
• This may cause the deformation of the active site, preventing the substrate from binding

Normal Reaction Substrate + Enzyme Denaturation

C1.1.7 Relationship between the structure of the active site, enzyme-substrate specificity and denaturation
Factor: Temperature
Low temperatures have insufficient thermal energy for
reactions to occur (limited motion / activation energy)

Rate of Reaction
Increasing the temperature increases the kinetic energy
of the enzyme and substrate (more frequent collisions)

At an optimum temperature the reaction rate will peak

(optimal temperature will be dependent on the enzyme)

Higher temperatures will cause a decrease in activity as

the active site of the enzyme will undergo denaturation Temperature (ºC)
Factor: pH
Changing the pH will alter the charge of the enzyme,
changing both the solubility and shape of the protein

Rate of Reaction
This will diminish the capacity for the substrate to bind
to the enzyme’s active site (so less successful collisions)

Enzymes will have an optimal pH at which the activity is

highest (the optimal pH will vary based on the enzyme)

Enzyme activity will decrease as the pH moves outside

of this optimal range (the enzyme becomes denatured) pH
Factor: Substrate Concentration
Increasing substrate concentration will increase the rate
of enzyme activity, but only up to a certain specific point

Rate of Reaction
More substrate means there is a greater chance of a
successful collision with the active site of the enzyme

At a certain point, the reaction rate will start to plateau

(i.e. the activity of the enzyme will level off and flatten)

This is because the solution becomes saturated with the

substrate and all active sites are occupied (maximal rate) Substrate Concentration
Topic Connections
Proteins
• Enzymes are a class of proteins involved in metabolic reactions (B1.2.4)

Cell Theory
• Metabolism is one of the fundamental features of organisms (A2.2.7)

Cell Respiration (HL)

• The digestion of carbon compounds is coordinated by enzymes (C1.2.8)

Epigenetics (HL)
• The activity of enzymes may be regulated by gene expression (D2.2.1)