enzyme kinetics Flashcards
michaelic menten model
explains how the rate of an enzyme-catalysed reaction depends on the concentration of the enzyme and its substrate
k1
is the forward rate constant for enzyme association with the substrate
k-1
the backwards rate constant for enzyme dissociation from the substrate
k2
the forward rate constant of enzyme conversion of substrate to product (P)
vmax
maximal rate of enzyme catalisation
km
half vmax
linewweaver burkplot
enables accurate determination of vmax and km
low km meaning
enzyme
only needs a little substrate to
work at half-maximal velocity
high km
an enzyme
needs a lot of substrate to work at
half-maximal velocity
can enzymes display the same vmax and have different km
yes
do allosteric enzymes follow michaelic menten
no
curve on graph of allosteric enzymes
sigmoidal- s shaped insetad of hyperbola
example of allosteric regulation
oxygen to haemoglobin binding