Day 10 Flashcards
enzymes are complimentary to what
transition state
rate eon for a one substrate enzyme catalyzed reaction
micaelis menten eqn
what is Michaelis menten eqn
initial velocity = (vmax x [S])/km + [S]
for reactions with two steps, km equals what
km= (k2+k-1)/k1
what represents slope in line weaver burk
Km/vmax
what represents y int in line weaver burk
1/vmax
enzyme inhibition has two broad categories, what are they
reversible and irreversible
competes with the substrate for the active site of an enzyme
competitive inhibotr
increases km, vmax uneffected
competitive inhibotor
WHAT is value of alpha prime for competitive inhibitor
1
slope changes, y int stays the same
competitive inhibition
binds at a site distinct from the substrate active site
uncompetitive inhibitor
binds only to the ES complex
uncompetitive inhibitor
causes decrease in both km and vmax
uncompetitive inhibiton
alpha value for uncompetitive inhibiton
1
y int changes, slope stays the same
uncompetitive inhibition
binds at site distinct from the substrate active site
mixed inhibitor
binds to either E or the ES complex
mixed inhibitor
what does mixed inhibitor do to km and vmax
increases km, decreases vamx
bind covalently with or destroy a functional group on an enzyme that is essential for the enzymes activity or form a highly stable non covalent association
irreversible inhibitor
types of regulation of enzymes
positive or negative
activators cause the curve to become what
more hyperbolic, more to the left
inhibitor may cause the curve to become what
more sigmoidal, moving to right
inactive precursor that is cleaved to form an active protease enzyme
zymogen
precursors that are cleaved to form other proteins
pro protein or proenzyme
