C4: Enzymes Flashcards
what are cofactors
- an additional non protein molecule is an enzyme that doesn’t take part in the reaction
- so it isn’t used up
- allows for EZ-SS reaction to occur by keeping the EZ and SS bonded together
one group of cofactors are called PROSTHETICS. explain what they are.
_ tightly bound together and a permanent part of the enzyme
- contributes to the 3D structure of the enzyme = it’s a vital property
- can be organic (eg. vitamins) or inorganic (eg. metal ions)
one group of cofactors are called COENZYMES
- theyre cofactors with organic molecules (eg. vitamins) only in their structure
- they only bond for a short period of time = loosely bound and easily released
- they’re changed in some way after the reaction but can be reused again
what are inactive precursor enzymes
enzymes that are made in an inactive form and can either cause damage within the cells, or can only be activated under certain conditions and needs to be controlled.
to activate a precursor enzyme ….. by …
.. they need to undergo a change in their shape (tertiary) by adding a cofactor
define enzymes
biological catalysts that speed up chemical/metabolic reactions by lowering the Ea
levels of temperature on enzyme activity (on a graph)
(A/N: should memorise/do the graph)
- peak of graph = optimum temperature, the maximum rate of reaction
- low temp, aka inactive = EZ don’t have much KE so they move very slowly.
- too high temp = EZ are denatured, so the active site is destroyed and SS no longer fits.
how temperature rise affects enzyme activity
- temperature rise = rise in KE, so particles collide more frequently = more successful collisions between SS and EZ = higher reaction rate
- but TOO HIGH temperature = molecules vibrate more = H bonds and ionic bonds break down = changes the active site of the EZ and less EZ SS complexes form = rate lowers and EZ completely denatures
on an enzyme graph Q10 = how rate increases with a 10ºc increase. what is the formula for this
Q10 = rate of reaction @ (x+10)º/ rate of reaction @ (x)º
Q10 is usually 2-3
how pH affects enzyme activity
- all enzymes have different optimum pH
- TOO MANY H+ ions (protons) interact with the polar groups in the amino acids and the H bonds + ionic bonds holding the tertiary structure = active site of EZ changes = SS can’t fit anymore
- NOT ENOUGH H+ ions means there aren’t enough interactions = loses the shape of active site
how enzymes catalyse intracellular and extracellular reactions
intracellular: occurs inside the cell that produces the enzyme, eg.
extracellular: nutrients in the form of proteins and polysaccharides need to be broken down to enter the cells
describe the lock & key theory
- only a specific substrate will fit into the active site of an EZ b/c they’re exactly complementary
- when the SS binds to the EZ it forms a EZ-SS complex, the SS reacts and products are formed in a product-SS complex, lowering the activation energy
- the products are released, leaving the EZ unchanged so it can react again
describe induced fit theory
- SS collides with complementary active site. EZ is flexible and conforms to the shape of SS so the active site fits closer
what part of the enzyme mechanism lowers the activation energy
the formation of an enzyme substrate complex
what 5 factors affect the rate of enzyme reactions
- pH
- substrate concentration
- enzyme concentration
- temperature
- inhibitors concentration