Biochem Exam 2 Questions and Answers (100 OUT OF 100) Already GRADED A
What does the initial rate of reaction depend on?
Concentration of substrate
What are some important assumptions of the MM model?
k-2 is small enough to be ignored, reaction is in steady state (formation and breakdown of ES are
equivalent)
What happens at maximal initial velocity?
The reaction is at equilibrium so it can't go any faster
What is Km?
substrate concentration required to react at 1/2 Vmax, a rate parameter (not a binding constant)
What is the MM equation?
What is the Lineweaver-Burk equation?
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What guides Km in cells?
Km is typically close to [S] in cells because it allows the biggest changes in product formation as
a means of control
What is the equation for Vmax?
Vmax = k2[E]T
What is turnover number?
The number of reactions that an enzyme molecule can catalyse per second, kcat
What does kcat/Km measure?
Catalytic efficiency (V0 = kcat/Km*[E]T[S]
What are the two MM enzyme models?
Sequential reaction ("normal") and double displacement (two products, enzyme modified in
between)
What is the difference between allosteric enzymes and MM enzymes?
Allosteric enzymes have multiple active sites and therefore regulatory properties from quaternary
structure, so their graphs have a sigmoidal shape.
What is feedback inhibition?
When allosteric enzymes are regulated by their own pathway's products
What is a committed step?
an effectively irreversible enzymatic reaction that occurs at a branch point during the
biosynthesis of some molecules, highly regulated
What is the concerted model for allosteric enzyme regulation?
All subunits must be in the same form, substrate binds to R and stabilizes it, which shifts
equilibrium and leads to more R conformations
What is the sequential model for allosteric enzyme regulation?
Doesn't assume all subunits have the same conformation, but one subunit changes affects the
chances of nearby subunits changing.