Enzymes And Membranes Oops Flashcards
What is a biological catalyst?
- A protein that speeds up a metabolic reaction without being used up in the reaction.
What is an intercellular enzyme?
- An enzyme which works within cells.
- E.g catalase which catalyses the breakdown of hydrogen peroxide into oxygen and water.
What is an extracellular enzyme?
- An enzyme which works outside cells.
- Eg Amylase works in the saliva and catalyses the hydrolysis of starch into maltose in the mouth
- Eg Trypsin is produced in the pancreas and deferred into the small intestine, it catalyses the hydrolysis of peptide bonds.
How to enzymes speed up reactions?
- They reduce the amount of activation energy that’s needed meaning reaction can occur at lower temperatures speeding up the rate of reaction.
‘The Lock and key’
- Substrates fit into tenedume in the same way a key fits into a lock.
- The active site and substrate have a complementary shape.
- However, scientists soon realised that the enzyme-substrate complex changed shape slightly to complete the fit.
The ‘induced fit’ model.
- The substrate approaches he active site.
- The substrate binds to the active site is complementary to.
- This slightly changes the shape of the active site.
- Enzyme-substrate complex is formed.
- The substrate is then broken down into products.
- Enzyme-product complex is formed.
- The products then move away from the active site.
How does enzyme concentration affect enzyme activity?
-the rate of reaction increases as enzyme concentration increase -
there are more active sites for substrates to bind to.-
however increasing the enzyme concentration beyond a certain point has no effect on the rate of reaction.
- there are more active sites than substrates so substrate concentration becomes the limiting factor
How does substrate concentration affect enzyme activity?
- as concentration of substrate increases, rate of reaction increases
- more enzyme-substrate complexes are formed.
- However, beyond a certain point the rate of reaction no longer increases as enzyme concentration becomes the limiting factor
How does temperature affect enzyme activity?
- rate of reaction increases up to the optimum temperature,
- which is the temperature at which enzymes work at their maximum rate.
- Rate of reaction decreases above the optimum temperature.
- Enzymes denature.
How does PH affect enzyme activity?
- Each enzyme has an optimum pH range.
- Changing the pH outside of this range will slow enzyme activity.
- Extreme pH values can cause enzymes to denature.
What does the temperature coefficient show?
- How much the rate of reaction changes when the temperature is raised by 10*c.
How to draw a tangent to estimate the initial rate of reaction
- Draw a tangent at t=0.
- Calculate the gradient of the tangent (change in y/change in x).
- Workout the unit, units of y/units of x.
What is a coenzyme?
- organic cofactors which do not bind permanently to the enzyme.
- They facilitate the binding of substrate to enzyme.
What is a cofactor?
- a non-protein compound required for the enzyme’s activity to occur.
- There are three types of cofactors: coenzymes, activators and prosthetic groups.
What is an activator?
- inorganic metal ions which temporarily binds to the enzyme
- This alters the shape of the active site.
- Which makes the reaction more feasible.
Where are phosphetic groups?
A cofactor which permanently binds to the enzyme.
What is an inhibitor and what are the two types?
a -substance which slows down or stops a reaction by affecting the binding of substrate to the enzymes.
- Inhibitors can either be reversible and irreversible.
What does an irreversible inhibitor do?
- cause disulphide bonds within the protein structure to break
- causing the shape of the active site to change
- affecting protein activity.
What do Reversible inhibitors do? And what’s are the two types?
- They bind to the active site through hydrogen bonds and weak ionic interactions therefore they do not bind permanently.
- Reversible inhibitors can either be competitive or non-competitive.