enzymes Flashcards
what does amylase digest starch to
to maltose
what’s a cofactor
a substance that has to be present to ensure that an enzyme catalysed reaction takes place at an appropriate rate. some cofactors such as prosthetic groups are part of the enzymes structure, and others (mineral ion cofactors or organic coenzymes) form temporary associations with the enzyme
are inorganic molecule or ion cofactors used up
no, they dont participate in the reaction
what do cofactors help do
help the enzyme substrate bind together
example of a cofactor (inorganic ion)
Cl- (cofactors for the enzyme amylase)
what’s a prosthetic group in relation to an enzyme
a prosthetic group is where the cofactor is part of the enzymes structure
an example of a prosthetic group
Zinc ions (Zn^2+)
what is the prosthetic group Zn^2+ for
for carbonic anhydrase which catalyses the production of carbonic acid and Co2.
whats a coenzyme
a small organic non-protein molecule that binds temporarily to the active site.
- they are changed in reactions and recycled continuously
when is the enzyme-substrate complex formed
when a substrate molecule successfully collides with an enzyme molecule
explain the induced fit theory
when the substrate molecules fit into the enzymes active site, the active site changes its shape slightly to mould itself around the substrate molecule.
( subtle changes in R group allow for this)
what bonds bind the substrate to the active site
via hydrogen bonds, ionic attractions van der walls forces and hydrophobic interactions
what do enzymes do to the activation energy of a reaction
lower the activation energy thus speeding up the reaction
what are the 4 things affecting enzyme activity
temperature
pH
conc of substrate
conc of enzymes
how does temp cause enzymes to denature
- weak bonds incl hydrogen bonds and ionic bonds break that hold the tertiary structure of the enzymes active site together
- active site shape changes, substrates can no longer fit well
- at high temp, irreversible changes occur to tertiary structure thus enzyme denatured
what bonds allow for enzymes to be stable
more disulphide bonds