Enzymes
All enzymes are globular proteins and round in shape
They have the suffix "-ase"
Intracellular enzymes are found inside the cell
Extracellular enzymes act outside the cell (e.g. digestive
enzymes)
Enzymes are catalysts → speed up chemical reactions
Reduce activation energy required to start a reaction between
molecules
Substrates (reactants) are converted into products
Reaction may not take place in absence of enzymes (each enzyme
has a specific catalytic action)
Enzymes catalyse a reaction at max. rate at an optimum state
Induced fit theory
Enzyme's shape changes when substrate binds to active site
Amino acids are moulded into a precise form to perform
catalytic reaction effectively
Enzyme wraps around substrate to distort it
Forms an enzyme-substrate complex → fast reaction
E + S → ES → P + E
Enzyme is not used up in the reaction (unlike substrates)
Changes in pH
Affect attraction between substrate and enzyme and therefore
efficiency of conversion process
Ionic bonds can break and change shape / enzyme is denatured
Charges on amino acids can change, ES complex cannot form
Optimum pH
pH 7 for intracellular enzymes
Acidic range (pH 1-6) in the stomach for digestive enzymes
(pepsin)
Alkaline range (pH 8-14) in oral cavities (amylase)
pH measures the conc. of H+ ions - higher conc. will give a
lower pH
Enzyme Conc. is proportional to rate of reaction, provided
other conditions are constant. Straight line
Substrate Conc. is proportional to rate of reaction until there
are more substrates than enzymes present. Curve becomes constant.
Increased Temperature
Increases speed of molecular movement → chances of
molecular collisions → more ES complexes
At 0-42 °C rate of reaction is proportional to temp
Enzymes have optimum temp. for their action (varies between
different enzymes)
Above ≈42°C, enzyme is denatured due to heavy
vibration that break -H bonds
Shape is changed / active site can't be used anymore
Decreased Temperature
Enzymes become less and less active, due to reductions in speed
of molecular movement
Below freezing point
Inactivated, not denatured
Regain their function when returning to normal temperature
Thermophilic: heat-loving
Hyperthermophilic: organisms are not able to grow below +70°C
Psychrophiles: cold-loving
Inhibitors
Slow down rate of reaction of enzyme when necessary (e.g. when
temp is too high)
Molecule present in highest conc. is most likely to form an
ES-complex
Competitive Inhibitors
Compete with substrate for active site
Shape similar to substrates / prevents access when bonded
Can slow down a metabolic pathway
[EXAMPLE] Methanol Poisoning
Methanol CH3OH is a competitive inhibitor
CH3OH can bind to dehydrogenase whose true substrate is C2H5OH
A person who has accidentally swallowed methanol is treated by
being given large doses of C2H5OH
C2H5OH competes with CH3OH for the active site
Non-competitive Inhibitors
Chemical does not have to resemble the substrate
Binds to enzyme other than at active site
This changes the enzyme's active site and prevents access to it
Irreversible Inhibition
Chemical permanently binds to the enzyme or massively denatures
the enzyme
Nerve gas permanently blocks pathways involved in nerve message
transmission, resulting in death
Penicillin, the first of "wonder drug" antibiotics,
permanently blocks pathways certain bacteria use to assemble their cell wall
component (peptidoglycan)
End-product inhibition
Metabolic reactions are multi-stepped, each controlled by a
single enzyme
End-products accumulate within the cell and stop the reaction
when sufficient product is made
This is achieved by non-competitive inhibition by the
end-product
The enzyme early in the reaction pathway is inhibited by the
end-product
The metabolic pathway contains a series of individual chemical
reactions that combine to perform one or more important functions. The product
of one reaction in a pathway serves as the substrate for the following
reaction.
Cells & Molecules
Cell Division
Cell Types
Cell Ultrastructure
Enzymes
Gene Technology
Genes, DNA, RNA
Large Molecules
Plasma Membrane
Respiration
Content
Enzymes
Changes in pH
Increased Temperature
Decreased Temperature
Inhibitors
End-product inhibition
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