Enzymes summary for AP biology
enzymes currenttheory
structure
induced fit model
suggests that substrate
a 30protein does not fit intoactive
site like a lock in akey
chemicalreactionsallow
binding
substrate can moldactive
site's R groups to
p a tertiarystructure
speedup chemical reactions
change in structure denatured
mGP
substrate
physical chemicalproperties of
substrate must be compatible with
enzyme is not changed from reaction instead reused
substrates requirespecific enzymes to facilitatereaction
denaturing factors
optimumtemp optimum pH
Ttemp fKMT
Y small ideal pitrange
M toohightemp denature tpit hpit denatured
wtemp slow run rate distrupt it bonds in active
temperature t KMT not denatured ph level
site
substrate enzyme concentration
one variable
mom
d d
efficiency only I constantly if both variable
concentrations increase
highprobability of binding
activation energy Ea
transitionalstate
a catalysts decrease the amount of
a free energy needed for reactants
to reach the transitional state
to make it work when needed
I
s something to an enzyme
sangtwo types of activators
cofactors
Genzymecannow
eg neme
coenzymes
friend organic function
cofactor egthiamine vitamins
how can you slow down an enzyme example competitive alcohol
1 competitive inhibition
O left substrate
using an inhibitor tobondintoactivesite
instead of substrate e
a'gppedistiteinhibitor
competitive inhibitorsmimics substrate's
shape notfunction
2 allosteric noncomeditiveinhibitions examplenoncompetitive heavymetals
inibitorbondstoallostericsite whichwill
initigmpeditive O Eistratechange activationsiteshape to stop
allostericsite
substrate fromfitting Etive