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Cofactors
When a small, simple molecule or inorganic ion is the non-protein component of an enzyme
Coenzyme
When an organic molecule is the non-protein element of an enzyme
Function of cofactors and coenzymes
Some enzymes can only catalyse a reaction if another non-protein substance binds to the enzyme
e.g. inorganic ion cofactors may combine with either the enzyme or substrate
presence of the ion means that the ESC forms more easily
Some reactions require atoms to be carried from one reaction to another in a multistep pathway
difference between cofactors and coenzymes
coenzymes are organic molecules
cofactors are inorganic molecules (dont contain carbon)
Example of a cofactor
Cl- ions are cofactors for salivary amylase enzymes
Example of coenzyme
coenzyme NAD used in respiration to carry H atoms between different enzyme controlled reactions
Prosthetic groups
prosthetic groups on enzymes are a type of cofactor- differ if they are permanently attached by covalent or non covalent forces
prosthetic groups contribute to overall 3D shape of the enzyme
What is an inactive precursor?
An enzyme that requires a change in tertiary structure to activate the enzyme.
this prevents enzymes from causing damage within cells and ensures they are only used when needed
These are called;
zymogens
proenzymes
How is a change in tertiary structure brought about for inactive precursors?
action of another enzyme
change in conditions (e.g pH or temp)
what is the precursor protein ( inactive enzyme) known as
apoenzyme
what is an activated enzyme due to binding of a cofactor known as
holoenzyme
how is an enzyme activated by a cofactor
they bind to enzyme and causes change in shape of tertiary structure
active site becomes complemnetary in shape to substrate
What is an enzyme inhibitor?
Any substance or molecule that slows down or stops an enzyme-controlled reaction.
Two types of enzyme inhibitors
Competitive
Non-competitive
Competitive inhibitors
similar shape and structure to substrate
complimentary in shape to active site
bind with the active site of the enzyme
form enzyme-inhibitor complex
blocks active site and prevents enzyme from catalysing reaction
lowers rate of reaction
Are competitive inhibitors reversible?
Yes, they are usually reversible and have no permanent effect on enzyme
How can competitive inhibition be overcome?
Increasing the substrate concentration
more likely for enzyme active site to collide with substrate rather than inhibitor
can knock out the inhibitor
Non-competitive inhibitors
bind to an allosteric site
causes tertiary structure of the enzyme to change
active site changes shape
active site is no longer complementary to substra
enzyme substrate complexes form less frequently and rate of reaction is MUCH lower
What is an allosteric site?
A part of the enzyme other than the active site
Are non-competitive inhibitors reversible?
No, they often bind permanently to the enzyme. Their action is often irreversible.
Can non-competitive inhibition be overcome by increasing substrate concentration?
No. The level of inhibition is determined by the number of inhibitor molecules present.
Roles of inhibitors
Some metabolic poisons are enzyme inhibitors
e.g potassium cyanid is an irreversible non-competitive inhibitor of a vital enzyme in aerobic respiration called cytochrome c oxidase
e.g. organophosphates in insecticides are non-competitive inhibitors of an enzyme present at synapses
Some medicinal drugs work by inhibiting the activity of enzymes
e.g. aspirin is a competitive inhibitor of COX enzymes which synthesis prostaglandins (which cause pain and inflammation)
e.g. statins are competitive inhibitors of the enzymes responsible for cholesterol production
what is end product inhibition
the products of some reactions are reversible inhibitors for enzymes involved in controlling reaction
this enables reactions to be controlled
if there is a lot of product present, it will inhibit the enzymes and cause reaction to slow or stop
prevents resources being wasted