2.

5 Enzymes
Essential Idea: Enzymes control the metabolism of the cell.

-Enzymes are globular proteins that function as biological catalysts which

can speed up/increase the rate of a chemical reaction
-they lower the activation energy (the energy required for the reaction to
take place)

-Enzymes are not used up because it is a catalyst

-not changed in the chemical reaction, as it only serves as a facilitator
-Composed of carbon, hydrogen, oxygen, and nitrogen

Parts of an Enzyme
-Activation site is the region of the enzyme where the substrate binds
-Substrate is a substance on which the enzymes act (eg: proteins, lipids)

Notice how the substrate perfectly fits the enzyme.

Types of Enzymes
-Divided into groups by the type of reaction they catalyze
-Named based on the type of substrate they act upon, followed by the suffix
ase (eg: protease act on proteins)
-Catabolic enzymes break down larger molecules into smaller molecules
-Anabolic enzymes forms larger molecules from smaller molecules

Enzyme Action
-Occurs when the enzyme and substrate collide
-During the collision the substrate slots into the active site of the enzyme
-collisions happen because of the rapid, random movement of the
molecules
Binding step:
-The enzyme and the substrate non-covalently bind to form an enzyme
substrate complex

Catalytic step:
The enzyme substrate complex then goes through a change to become the
enzyme and product

Lock and Key Model

-Substrate must fit into the enzyme at the active site
-The enzyme is the lock, the substrate is the key

Enzyme Specificity
-Varying degrees of specificity, some enzymes have absolute specificity for
one substrate and no others
-Others react with substrate with similar functional groups, side chains, or
positions on a chain

-Cell activity is determined by which enzymes are active in the cell at the
time
-Cell activity is altered by removing specific enzymes and/or synthesizing
new enzymes

Enzyme Denaturation
-Being proteins, enzymes can experience denaturation
-there are many conditions that affect enzyme activity

Temperature:
-All enzymes function within an optimum temperature range
-as temperature increases, the kinetic energy of substrate and enzyme
molecules increase
-this leads to more movement, more collisions, so therefore the reaction
rate increases
-At optimum temperature, the reaction rate is the highest
-the optimum temperature range for most is about 35-40 C
-If temperature is too high, the bonds in the enzyme begin to break, altering
the protein structure

pH:
-All enzymes have an optimum pH range where activity is highest
-most enzymes function in pH 6 to 8 (body conditions)
-Excessive acid or base cause protein molecules to denature

-common exception is pepsin, as it requires pH 1 to 2 to work because acid

changes shape of protein to expose active site

Concentration of Salt Ions:

-Salt refers other metal/non-metal combination beside NaCl
-Ions from salts can bind onto enzymes and interfere with bonding, causing
structural changes to the protein, affecting the enzyme activity
-eg: salt preserving; salt prevents enzymes in bacteria from working, so
meats dont spoil

-There are also other factors that affect enzyme activity

Concentration of Substrate:
-The more the substrate, the more collisions between enzyme and substrate
-therefore there are more chances of binding, resulting in more catalyzed
reactions, leading to a higher reaction rate
-Initially, there is a significant increase in rate
-As substrate concentration increases, rate does not increase as much
-Eventually all enzymes are continuously filled with substrate
-a maximum (constant) rate is reached
-regardless of the substrate concentration, all active sites are occupied so
any more substrate needs to wait for active site to be vacated

Concentration of Enzyme:
-The cell regulates the amount of enzymes present at any given time,
otherwise there may be
-unnecessary enzymes present or have products of one enzyme reaction
interfering with another reaction
-genes coding for enzymes can be turned on or off depending on which
enzyme is needed

Competitive Inhibition:
-Molecules structurally similar to substrate can bind to active site and
prevent substrate from binding
-thus these molecules compete with substrates for active site and
inhibits or stops enzyme action
-eg: cyanide blocks active site of cytochrome c oxidase (enzyme involved
in cellular respiration), penicillin blocks active site of enzymes found in
bacteria

Non-competitive Inhibition:
-Molecule binds to part of enzyme that is not active site and causes change
in shape/electrical charge
-results in decreased enzyme activity as substrates cannot bind as easily or
at all

-eg: heavy metals (Hg, Cu, Pb, etc.) bind to enzymes like cytochrome c
oxidase by binding to SH groups thus breaking the disulphide bonds
-nerve gases such as Sarin inhibit acetylcholinesterase, an enzyme that
breaks down acetylcholine (neurotransmitter); disrupts nerve message
transmission

Allosteric Inhibitors:
-Allosteric means other shape
-Sometimes, end products of a reaction bind to anallosteric site on an
enzyme from an earlier part of the reaction pathway
-causes enzyme to change shape, resulting in decreased activity
-Often referred to as feedback inhibition or negative inhibition
-prevents cell from having too much of a certain product made

Cofactors/Coenzymes:
-Many enzymes require non-protein helper molecule to function
-Cofactors are inorganic ions/molecules such as iron and zinc
-coenzymes are organic molecules such as vitamins are needed for the
synthesis of coenzymes
-eg: B12 needed to make coenzyme called FAD
-Can help change bonds of substrate so that it will react or can
accept/contribute atoms to the reaction

Immobilized Enzymes
The use of enzymes in industry wasnt wide spread until Hans and Eduard
Buchner in 1897 showed that a yeast extract could convert sucrose into
alcohol (fermentation). No yeast cells were used, which went against
Pasteurs claim that fermentation only worked with living cells (vitalism). The
Buchner brothers again showed this idea to be false. Now, more than 500
enzymes are used commercially.
Enzymes in industry are often immobilized, attached to surfaces like glass,
trapped within membrane or gel, or made into aggregations (binding
enzymes together into larger particles to restrict their movement).

Reasons for immobilizing Enzymes:

-Reaction can be easily controlled by quickly adding or removing the enzyme
-It is easy to separate the enzymes from products to prevent contamination
of products
-Once enzymes are removed, they can be easily recycled as they are
expensive
-Enzymes are more stable, as they are not as susceptible to pH and
temperature, so less degradation
-Can increase the concentration of enzymes

Production of Lactase Free Milk

-Through the use of lactase, lactose can be turned into galactose and glucose
-lactase can be free or immobilized on beads
-Galactose and glucose are sweeter than lactose; fewer sweeteners needs to
be added
-Lactose crystallizes in ice cream, gritty; glucose and galactose are more
soluble
-Glucose and galactose are easier for bacteria to ferment
-production of yogurt and cottage cheese is easier