Chapter 7 Flashcards
(19 cards)
differentiate between first-order rate constant and a second order rate constant
1st order rate constant is a propotionality constance for reactions having only one reactant; it relates to to rate of reaction to concentration of sole reactant
second oder rate constant proportionalitiy constant for reactions having two reactants; it relates the rate of a reaction to concentration of both reactions
what is a pseudo first order reaction
a second order reaction that appears to be first order…if the concentration of one reactant is much greater than the second reactant, the velocity will appear to be first order with respect to reactant present in lower concentration
what is the biochemical advantage of having a Km approximately equal to the substrate concentration normally available to an enzyme?
at substrate concentrations near the Km, the enzyme displays significant catalysis yet is sensitive to changes in substrate concentration
what is the defining characteristic for an enzyme catalyzing a sequential reaction? a double displacement reaction?
characterized by formation of a ternary complex consisting of enzyme and both substrates.
double displacement rxn always requires formation of temporarily substituted enzyme intermediate
enzyme
protein catalyst
kinetics
the study of reaction rates
michaelis menten equation
describes kinetics of simple one-substrate reactions
michaelis constant (km)
substrate concentration that yields 1/2vmacx
lineweaver burk equation
double recipricol plot
turnover number
k2 or kcat
kcat/km
measure of enzyme efficiency
sequencial reaction
ternary complex is formed
double displacement (ping pong reaction)
includes substituted enzyme intermediate
allosteric enzyme
responds to environmental signals
what is feedback inhibition and why is it a useful property? (15)
inhibition of allosteric enzymes by end product of pathway controlled by the enzyme. feedback inhibition prevents the production of too much end product and consumption of substrates when product is not required
an allosteric enzyme that follows the concerted mechanism has T/R ratio of 300 in the absence of substrate. suppose that a mutation reversed the ratio. how would this mutation affect the relation between the velocity of the reaction and the substrate concentration
the enzyme would show simple michaelis menten kinetics because its essentiall always in the R state
differentiate between homotropic and heterotropic effectors
homotropic effectors are substrates of allosteric enzymes. heterotropic effectors are regulators of allosteric enzymes. homotropic account for sigmoidal nature of velocity vs substrate concentration curve. heterotropic alter midpoint of k, of curve. both work by altering T/R ratio
ATcase is an allosteric enzyme that regulates the synthesis of UTP and CTP. it can be separated intro regulatory subunits and catalytics subunits. if isolated regulatory subunits and catalytic subunits of ATCase are mixed, the native enzyme is reconsonstituted. what is the biological significance of the observation
the reconstitution shows that complex quaternary structure and resulting catalytic and regulatory properties are untimately encoded in primary structure of individual components
you have isolated a dimeric enzyme that contains two identital active sites. the binding of substrate to one active site decreases the substrate affinity of the other active site. can the concerted model account for this negative cooperativity?
sequential model more readily accounts for negative cooperativity than concerted model