Enzyme Kinetics Flashcards
enzyme reaction rates vary on what
substrate concentration
michaelis constant
Km
meausre of enzyme-substrate affinity
v= 1/2Vmax
compare 2 enzymes to determine which woudl function better under given circumstances
faster enzyme has high or low Vmax
high V max
which has a higher Km, fast or slow enzyme?
slow enzyme
which enzyme has a higher affinity, fast or slow enzyme?
fast enzyme
when comparing two Lineweaver-Burke plots, the enzyme that produces the graph with the steepest slope will have what?
the highest substrate concentration
coopertive binding
substrate binding at one subunit induces affinity change atothers
what shape is rate kinetics?
sigmoidal
noncompetitive inhibitors
bind to allosteric sites on the enzyme and enzyme-substrate complex
Vmax will decrease
competitive inhibitors
competes with the substrate at the active site
no direct change to the enzyme’s ability to bind to its substrate
Vmax is unchanged
uncompetitive inhibitors
binds to an allosteric site ont he enzyme-substrate complex and “lock” the substrate in place
Vmax will be lower
mix inhibition
bind to the allosteric site of the enzyme and the enzyme substrate complex but with unequal affinity
lower Vmax
what type of bonding is NOT broken when a protein is exposed to heat, causing a loss of 3D structure?
peptide bonding
as the bonds are held together by the primary structure of protein, peptide bonds are strong, covalent connections that don’t denature int eh presence of heat
in what type of structure do you find hydrogen bonding?
in secondary, tertiary, and quaternary structures
easily broken in the presence of heat
in what type of structures do you find hydrophobic interactions?
tertiary and quaternary structures
break apart in the presence of heat
