2. Write an expression for km for the reaction below using rates. k2 E+S ES →...
For enzymes in which the slowest (rate-limiting) step is the reaction: K2 ES → E+P Km becomes equivalent to: A) kcat. B) the [S] where V0 = Vmax. C) the dissociation constant, Kd, for the ES complex. D) the maximal velocity. E) the turnover number. The answer is C), could you please explain?
how we can solve q2 2. a) The Michaelis-Menten mechanism is +KTERE] - @s→Es (rateco nstant kl) ク ES→ E + S (rate constant k2) E S ES-XⓟHE) orate constant k3) So d[PVdt- k3[ES] Use the steady state approximation to show [El/[ES] (k2+k3)/(k1[S] b) let Km=(k2+k3)/kl and show that you get the expression ·J [EVIES]-Km/[S] c) We will talk in class about how this information eventually gives rise the expression d[P]/dt-k3E][S/(Km +IS) Usually [S>>Km. Show what this equation simplifies to...
3) For the simplified representation of an enzyme-catalyzed reaction shown below, the statement “ES is in steady-state” means that: A) k2 is very slow. B) k1= k2. C) k1= k-1. D) k1[E][S] = k-1[ES] + k2[ES]. E) k1[E][S] = k-1[ES]. 3) For the simplified representation of an enzyme-catalyzed reaction shown below, the statement “ES is in steady-state" means that: k, k, E+S <> ES Z E +P - k1 A) k2 is very slow. B) Kı= k2. C) K1= k-1....
)* (Vmax). 4. When [S] = KM, Vo=( A) 0.5 B) KM C) 0.75 D) kcat E) [S] 5. The overall transformation shown in the following reaction: E s. Es p + E For the reaction, the steady state assumption A) ES breakdown occurs at the same rate as ES formation B) [P]>>[E] C) implies that ki-k-1 D) implies that k., and k2 are such that the [ES] = k1[ES] E) [S] = [P]
Consider a description of an enzymatic reaction pathway that begins with the binding of substrate S to enzyme E and ends with the release of product P from the enzyme. E+S →ES → EP E+P Under many circumstances, KM = [E] [S] / [ES] What proportion of enzyme molecules are bound to substrate when [S] = KM? Why? Recall that when [S] = KM, the reaction rate is Vmax/2. Does your answer to Part A make sense in light of...
The Km can be considered to be the same as the dissociation constant K for E+ S binding it: the concentration of [ES] is unchanged k1 >> K2 ES --> E+ P is fast compared to ES -->E+S k2<<k-1 this statement cannot be completed because Km can never approximate Ks 2. Muscle contraction is triggered: by conformational change in myosin and actin in response to an increase in the cytoplasmic Ca2+ concentration in response to an increase in the cytoplasmic...
2. In a single substrate enzyme-catalyzed reaction, the forward rate constant (formation of ES) is 2.1x105 M-1 s-1 , the reverse rate constant (dissociation of ES to E +S) is 9.4x103 s-1 , and the catalytic rate constant (turnover of ES to P) is 7.2x102 s-1 . From this data, KM is:
michaelis menten and kinetics help 2. A few years after Michaelis Menten published their work Briggs and Haldane came along and expanded it using the steady state assumption. i) Based on kinetic scheme 2 how many different ways can ES be produced? i) Using the rate constants in kinetic Scheme 2 at what rate is the ES complex being produced? sed eci iv) Using the rate constants in kinetic Scheme 2 at what rate is the ES complex being destroyed?...
Problem 2: (Enzyme Kinetics) A competitive inhibitor I interferes with an enzyme-catalyzed reaction according to the mechanism: E+S →ES, rate constant = ki, ES → E+S, rate constant = k-1, ES → E+P, rate constant = k2, E + EI, rate constant = k3. EI → E + I, rate constant = k-3. Assuming that the concentrations of S and I are much larger than the total enzyme concentration, derive an expression for the initial rate of appearance of product,...
2. For reaction (E), write the expression for the steady-state concentration of N2O2, [N2O2]ss. What is the steady-state concentration of N2O2 given a concentration of [NO] = 1 ppb and [H2] = 500 ppb? Solve for the production rate (molecules cms-1) of N20. Assume the number density of air molecules is 2.5x1019 molecules cm3. The following reaction mechanisms we have discussed to some degree during class: (A) HNO3 → OH + NO2 (ka = 0.12 s-1) (B) CO+O → CO2...