All Cells need Energy to do

Work
Cells use energy to
grow, make new
parts, and reproduce.

Biological Work
Energy an be defined as the capacity to do work
Biological work has three basic forms
Chemical work
Growth
Protein synthesis
Information storage
Transport work
Move molecules across plasma membrane
Maintain concentration gradients
Mechanical work
Positioning & movement of organelles
Cell shape
Beating of cilia & flagella
Muscle contraction

Activation Energy and the

Net Free Energy Change of the Reaction
Activation energy is the
energy needed to get
the reaction started.
The net free energy
change is the difference
in free energy between
the reactants and
products.

Exergonic and Endergonic Reactions

Exergonic reactions release( Pelepasan ) energy or are energy producing
reactions. The products have a lower free energy than the reactants
C6H12O6 + 6O2 6H2O + 6CO2 + 36 ATP + heat

Endergonic reactions are energy utilizing reactions where part or all of the
activation energy is retained or trapped in the chemical bonds of the
products.
CO2 + H2O + Radiant energy C6H12O6 + 6O2

Enzymes
Means in yeast; 1st described by Buchner
Proteins are biological (organic) catalysts
promote rapid reaction rates

Substrate - substance an enzyme acts upon

Naming Convention
named for substrate with -ase as the suffix
amylase enzyme digests starch (amylose)

Lowers activation energy = energy needed to

get reaction started
enzymes facilitate molecular interaction

Enzymes and Activation Energy

Characteristics of Enzymes
1. Lower the activation energy of a reaction.
- Activation energy is the energy needed to get a reaction
started.

2. Increases the rate of a reaction but does not cause

a reaction to occur that would not occur in its
absence.
- Enzymes are biological catalysts
2H2O2 -> 2H2O + O2 One molecule of catalase can break 40
million molecules of hydrogen peroxide each second.

3. Are not used up or changed by the reaction.

4. Exhibit specificity, competition, and saturation.

Enzymes

Catalysts for biological reactions

Most are proteins
Lower the activation energy
Increase the rate of reaction
Activity lost if denatured
May be simple proteins
May contain cofactors such as metal ions
or organic (vitamins)
8

Name of Enzymes
End in ase
Identifies a reacting substance
sucrase reacts sucrose
lipase - reacts lipid
Describes function of enzyme
oxidase catalyzes oxidation
hydrolase catalyzes hydrolysis
Common names of digestion enzymes still use in
pepsin, trypsin
9

Classification of Enzymes
Class
Oxidoreductoases
Transferases
Hydrolases
Lyases
Isomerases
Ligases

Reactions catalyzed
oxidation-reduction
transfer group of atoms
hydrolysis
add/remove atoms
to/from a double bond
rearrange atoms
combine molecules
using ATP
10

Examples of Classification of
Enzymes
Oxidoreductoases
oxidases - oxidize ,reductases reduce
Transferases
transaminases transfer amino groups
kinases transfer phosphate groups
Hydrolases
proteases - hydrolyze peptide bonds
lipases hydrolyze lipid ester bonds
Lyases
carboxylases add CO2
hydrolases add H2O
11

How do enzymes increase the rate of a

chemical reaction?
Enzymes bind to their
substrates and bring them
together in the proper
orientation for the reaction
to begin.
The binding and aligning
of the substrates lowers
the activation energy of
the reaction.
enzyme + A + B C + D + enzyme

Substrate Binding
Lock and Key Model

Induced Fit Model

Cofactors
Enzyme activity relies on the binding of certain
inorganic molecules before substrate binding can
occur. Examples are Ca2+ and Mg2+.

Coenzymes

Coenzymes are organic molecules.

Do not alter (merubah) the enzymes binding site.

Accept electrons from an enzyme in one metabolic pathway and

transfer them to an enzyme in another.

They are not needed in large amounts.

The water soluble vitamins (thiamine (B1) niacin, riboflavin (B2)) are
all good examples of cofactors.
NAD (nicotinamide adenine dinucleotide)
FAD (flavine adenine dinucleotide)

Coenzyme NAD

NAD+ transports electrons from one

metabolic pathway to another

Factors Affecting Enzyme

Action: Temperature
Little activity at low temperature
Rate increases with temperature
Most active at optimum temperatures
(usually 37C in humans)
Activity lost with denaturation at high
temperatures

17

Factors Affecting Enzyme

Action
Optimum temperature

Reaction
Rate

Low
High
Temperature
18

Factors Affecting Enzyme

Action: Substrate Concentration
Increasing substrate concentration
increases the rate of reaction (enzyme
concentration is constant)
Maximum activity reached when all of
enzyme combines with substrate

19

Factors Affecting Enzyme

Action
Maximum activity

Reaction
Rate

substrate concentration
20

Factors Affecting Enzyme

Action: pH
Maximum activity at optimum pH
R groups of amino acids have proper
charge
Tertiary structure of enzyme is correct
Narrow range of activity
Most lose activity in low or high pH

21

Factors Affecting Enzyme

Action

Reaction
Rate
Optimum pH

11

pH
22

Temperature & pH Modulation

Enzymes are proteins, and
all proteins have a native
configuration which gives
them a particular function
(activity) or structure.
Changes in temperature
and pH greatly affect the
enzymes confirmation and
results in loss of activity.
We say it is denatured.

Proteolytic Activation
Some enzymes are
produced in an inactive
form called proenzymes
or zymogens.
The pro- prefix and
-ogen suffix signifies that
the molecule is inactive.

Chymotrypsinogen
Pepsinogen
Angiotensinogen
Prothrombin

Temperature & pH Modulation

Small changes in temperature, pH, or salt can increase or decrease

enzyme activity.
Once a critical level is exceeded, then the change in confirmation is
irreversible and the enzyme forever looses its activity.

Pepsin: pH of 1-2
Trypsin: pH of 8-9.5

Enzyme Inhibition
Inhibitors
cause a loss of catalytic activity
Change the protein structure of an enzyme
May be competitive or noncompetitive
Some effects are irreversible

26

Competitive Inhibition
A competitive inhibitor
Has a structure similar to substrate
Occupies (menempati) active site
Competes (bersaing) with
substrate for active site
Has effect reversed (membalikkan)
by increasing substrate
concentration
27

Noncompetitive Inhibition
A noncompetitive inhibitor
Does not have a structure like substrate
Binds (mengikat) to the enzyme but not active
site
Changes the shape of enzyme and active site
Substrate cannot fit altered active site
No reaction occurs (terdapat)
Effect is not reversed by adding substrate
28

Isozymes
Any of a group of enzymes that catalyze the same reaction
Have different structures and physical and biochemical
properties.
Lactate dehydrogenase (LDH) - widely distributed throughout the body
Cellular damage causes an elevation of the total serum LDH

Diagnostic usefulness is in the determination of which

fraction of LDH is elevated

LDH-1 is found mainly in heart muscle and RBCs

LDH-2 in white blood cells
LDH-3 is highest in the lung
LDH-4 is highest in the kidney, placenta, and pancreas
LDH-5 is highest in the liver and skeletal muscle

For future reference:

http://www.nlm.nih.gov/medlineplus/ency/article/003471.htm

Effect of Enzyme or Substrate

Concentration on Reaction Rate
The reaction rate is directly
related to enzyme
concentration.
What is the independent
variable in this graph?

The reaction rate can reach

a maximum (Vmax) when the
enzyme is saturated.
What is the independent
variable in this graph?

Feedback
Inhibition
Occurs when the product
of a series of enzymatic
reactions begins to
accumu- late within the
cell
Product may then inhibit
the action of the first
enzyme in its synthesis
Further production of the
enzyme is then halted

 Thank you.