biochem 005 kinetics and regulation part 2 (michealis-menten equation competitive inhibitor non-co

substitution of valine for glutamate

true

Km is equal to the substrate concentration at which the reaction velocity is half its maximal value

no, because the Km is a compilation of enzyme rate constants--each of which are unique to their respective enzymes

increasing the substrate concentration will increase the enzyme velocity IF the enzyme is not yet saturated (that is, if there isn't more substrate concentration than enzyme concentration). This is because, when an enzyme isn't saturated, adding more substrate means more substrate is converted into product by the more abundant enzyme

k is the rate constant. the rate of the reaction is directly related to the concentration of the reactant(s) by this constant.

a Lineweaver-Burk plot

false. experimental evidence suggests that the Km value provides an approximation of substrate concentration in vivo

the turnover number is the number of substrate molecules that an enzyme can convert into product per unit time when the enzyme is fully saturated with substrate

the turnover number is equal to the rate constant k₂, which is also called k_cat

kcat/K_M is the rate constant for the interaction of S and E. It is ameasure of the catalytic efficiency because it takes into account both the rate of catalysis with a particular substrate (kcat) and the strength of the enzyme-substrate interaction (K_M). For instance, by using kcat/K_M values, we can compare an enzymes preference for different substrates.

Look at the following table to see the kcat/K_M values for several different substrates of chymotrypsin:

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Compound F could stimulate e₁₀ but inhibit e₁ to balance the amount of I with F. Likewise, compount I could inhibit e₁₀ while stimulating e₁

homotropic

heterotropic