0% found this document useful (0 votes)
108 views

Enzyme Lecture Notes

Enzymes are globular proteins that speed up chemical reactions by lowering their activation energy. They are not used up in reactions and can catalyze multiple reactions. Enzyme activity is affected by factors like pH, temperature, and inhibitors. pH can change enzyme shape and ability to bind substrates. Temperature affects molecular movement and above 42°C enzymes denature. Inhibitors bind enzymes and prevent substrate binding, either competitively resembling substrates, or non-competitively elsewhere on the enzyme. End-products can also inhibit enzymes in metabolic pathways.

Uploaded by

ryan
Copyright
© © All Rights Reserved
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
0% found this document useful (0 votes)
108 views

Enzyme Lecture Notes

Enzymes are globular proteins that speed up chemical reactions by lowering their activation energy. They are not used up in reactions and can catalyze multiple reactions. Enzyme activity is affected by factors like pH, temperature, and inhibitors. pH can change enzyme shape and ability to bind substrates. Temperature affects molecular movement and above 42°C enzymes denature. Inhibitors bind enzymes and prevent substrate binding, either competitively resembling substrates, or non-competitively elsewhere on the enzyme. End-products can also inhibit enzymes in metabolic pathways.

Uploaded by

ryan
Copyright
© © All Rights Reserved
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
You are on page 1/ 3

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
o Reduce activation energy required to start a reaction between molecules
o Substrates (reactants) are converted into products
o Reaction may not take place in absence of enzymes (each enzyme has a specific
catalytic action)
o Enzymes catalyse a reaction at max. rate at an optimum state
Induced fit theory
o Enzyme's shape changes when substrate binds to active site
o Amino acids are moulded into a precise form to perform catalytic reaction effectively
o Enzyme wraps around substrate to distort it
o Forms an enzyme-substrate complex fast reaction
o 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
o pH 7 for intracellular enzymes
o Acidic range (pH 1-6) in the stomach for digestive enzymes (pepsin)
o 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 42C, enzyme is denatured due to heavy vibration that break -H bonds
o 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
o Inactivated, not denatured
o Regain their function when returning to normal temperature
Thermophilic: heat-loving
Hyperthermophilic: organisms are not able to grow below +70C
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
o Compete with substrate for active site
o Shape similar to substrates / prevents access when bonded
o Can slow down a metabolic pathway
[EXAMPLE] Methanol Poisoning
o Methanol CH3OH is a competitive inhibitor
o CH3OH can bind to dehydrogenase whose true substrate is C2H5OH
o A person who has accidentally swallowed methanol is treated by being given large
doses of C2H5OH
o C2H5OH competes with CH3OH for the active site
Non-competitive Inhibitors
o Chemical does not have to resemble the substrate
o Binds to enzyme other than at active site
o This changes the enzyme's active site and prevents access to it
Irreversible Inhibition
o Chemical permanently binds to the enzyme or massively denatures the enzyme
o Nerve gas permanently blocks pathways involved in nerve message transmission,
resulting in death
o 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.

You might also like