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enzyme III

QuestionAnswer
enzymes activity measured as the rate of product formation and varies with the substrate concentration
V = S ----> P velocity is disappearance of substrate and appearance of product
zero order velocity rate does not depend on substrate concentration
unimolecular first order velocity rate is dependent on the concentration of only one substrate V= A ----> P ; V= k [A]
bimolecular second order velocity rate is dependent on two substrate concentrations v = A + B ----> P v= k [A] [B]
many enzymes obey _________ kinetics Michaelis-Menten
Michaelis-Menten enzyme catalyzed reactions in terms of Km and Vmax
Problems? ES is difficult to measure
Michaelis Constant Km = k-1+k2 / k1
Michaelis Menten Equation v = Vmax [S] / Km + [S]
The Michaelis-Menten Equation is hyperbolic
Km substrate concentration at 1/2 Vmax
Km is unique for each enzyme substrate pair
Lower the Km more efficient the enzyme is at low substrate concentrations and vive versa
Kcat = catalytic rate constant aka turnover The number of substrate molecules transformed into product molecules by an enzyme per unit time when the enzyme is saturated with the substrate
kcat/KM = catalytic efficiency How avidly the enzyme binds its substrate and how rapidly it converts the substrate to product
The Lineweaver-Burk plot linearizes Michaelis-Menten kinetics data
Lineweaver-Burk 1 / V = ( Km / Vmax ) 1 / [S] + 1 / Vmax
The slope in a Lineweaver-Burk plot Km / Vmax
Not all enzymes fir the Michaelis-Menten model because some enzymes have multiple substrates
Not all enzymes fir the Michaelis-Menten model because some enzyme-catalyzed reactions have many steps
Velocity plot is sigmoidal
Allosteric enzymes exhibit cooperativity
substances that bind ________ to an enzyme can inhibit its activity irreversibly
competitive inhibitor increase Km without affecting Vmax
noncompetitive inhibitor decreases Vmax without affecting Km
Allosteric regulators can inhibit or activate enzymes
5-Fluorouracil a suicide inhibitor
competitive inhibitors bind to the sam site as the substrate
Transition state analogs often make better inhibitors than substrate analogs
allosteric regulation can inhibit or enhance enzyme activity ? T or F True, glucose ----> phosphofructokinase (ADP) ---> phosphoenolpyruvate
This type of inhibitor binds to a site other that the active site on the enzyme noncompetitive inhibitor
Created by: sofialorena
 

 



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