Enzymes Flashcards
(27 cards)
Enzymes structure
- it is a globular proteins
- have a specific 3D shape according to their sequence of amino acids
- active site made up of small number of amino acids.
- substrate held with active site by forming temporary bonds between amino acids of the active site and groups on the substrate
Enzymes action model
Induced fit model:
- active site forms as the enzymes an substrate interact
- enzyme is flexible, it can mould itself around the substrate to change shape of active site to fit
- a change in environment of the enzyme lead to a change in the enzymes that forms the active site.
What happens when enzymes changes its shape?
- enzyme put a strain on the substrate molecule, the strain distorts a particular bond or bonds in the substrate which lead to lower activation energy needed originally to break the bond.
Definition of catalyst
- it can alter the rate of chemical reaction without under going permanent changes themselves.
- can be used repeatedly, effective in small amounts
E.g. enzymes speed up reactions
Factors affect enzyme action
- temperature
- PH
- enzymes’ concentration
- substrates’ concentration
Enzymes’ work depends on whether :
- it comes into physical contact with its substrate
- it has an active site which fits the substrate
What is the changing measurements of an enzyme catalysed reaction?
- the formation of products
OR - the reduction of substrates
Based on time course- how long it takes
What is the term used to describe the shape of active site and substrates as ?
They are complementary
Effect of temperature on enzymes
- increases kinetic energy of molecules so enzyme and substrates molecules move quicker and more frequent collision so more effective collision to form enzyme substrate complex so rate of reaction increases
Effect of temperature rising
- cause hydrogen bonds and other bonds to break which changes the shape active site
- slows down reaction at 45degrees
Denaturation
- is a permanent change and once occurred, enzymes does not function again = falling curve on the graph
- usually after optimum temp 40 degrees in human body
- high temp = high metabolic rate, but requires extra energy like food to maintain high temp.
- other proteins except enzyme can denature at high temp e.g. during illness
PH of a solution
- is a measure of its hydrogen ion concentration
PH on enzyme action
- in/decrease of PH can affect rate of reaction
- it alters the change on amino acids that make up the active site so substrates no longer fit in = enzyme substrate complex cannot be formed
- may cause the bonds of enzymes’ tertiary structure to break = active site changes shape
Active site of enzymes
- the arrangement of it partly determined by hydrogen and ionic bond between amino and carboxyl group of polypeptides
- the change in H+ ions affect the bonding = active site to change shape
Why does enzyme able to work at very low concentration?
- because it can repeat the procedure on another substrate once it acted on an active site
- means it is not being used up in a reaction
Effect of increasing enzyme concentration ( excess substrates)
- more enzyme means more active sites that substrate can act on so now increase enzyme conc can cause excess substrates now be acted upon so ROR increase
Effect of increasing enzyme concentration ( limiting substrate)
- not efficient to supply all enzymes active site so increase conc will have no effect on ROR
- ROR stay constant level bec existing enzyme already used up with available substrate
Effect of increasing sub conc
- increase ROR
bec. more substrate added, activities being filled and at full capacity until all of them work as fast as they can -) ROR max. -) So excess substrates will have no effect on ROR
What is the name of the point between flat and steep line of ROR graph
Point of saturation
Definition of enzyme inhibitors
Substances that directly or indirectly interfere with the functioning of acitve site of enzyme and so reduce activity
Types of enzyme inhibitor
- Competitive inhibitor
- Non competitive inhibitor
Structure of competitive inhibitor
- has molecular shape SIMILAR to the substrate, allow them to occupy the acitve site, compete with the orginal substrate
- block acitve site
Effect of competitive inhibitor
- reversible/ irreversible reaction
- sub conc. inverse proportional to effect of inhibitor
- greater inhibitor conc. Longer time it takes to get away from the A.S
Why is sub.conc inverse proportional to effect of inhibitor
Because inhibitor not permeantly bound to active site, so when it leaves, a sub or another inhibitor can take its place, depending on how much each conc are