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...
8. For the simplified representation of an enzyme-catalyzed reaction shown below, the statement "ES is in steady-state" means that: ki E+S ES – E+P kit2 a. kz is very slow. b. k1 = k. c. k1 = k-1. d. ki[E][S] = k-1[ES] + ka[ES]. e. ki[E][S] = k-1[ES]. 9. . You are examining the effects of a mutation in the proximal histidine of a heme-containing protein. This mutation has changed the histidine into an alanine. Based on your knowledge of...
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit of . The value of Vmax for. the same reaction is with the unit of . Be sure to give the values with the correct number of significant figures. You might have to construct a kinetic plot. For units, choose one answer from (uM, 1/ UM, HM/second, uM x second, mM, 1/mM, second, 1/second, mM/second, mM x second) vo (mM/sec) Glucose concentration (mm) 0.10...
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,...
)* (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]
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:
13. Suppose a second enzyme binds the substrate even more tightly than the enzyme shown in model 1 (the ES complex is more stable than the one shown in graph B). Draw this new E.S complex on graph B. What happens to the magnitude of the activation energy, AGact? 14. Suppose a third enzyme binds the transition state even more tightly than the enzyme diagramed Model 2. What happens to the magnitude of the activation energy, AGact? Model 2 Generalized...
1. The sequential mechanism for an enzyme, E, with two substrates, Si and S2 is shown below. Write the full rate equations for all species in the mechanism E+S ES ESI E S ESI S2 ESI S2 ESIS2 ESI S2 ki k. k2 k-2 k3 ESIS2 EP
4. The mechanism suggested for the reaction, 2 A + B +20 A+ AL I + B + 2C forward rate constant kı, backward rate constant k., constant k2 The rate law obtained on applying the steady state approximation is, A) Rate = kika[A] [B] B) Rate = kik[A] [B]/(k.1 + 2[B]) C) Rate = kık[A][B] D) Rate = kik[A]?/(k.1 +k2[B]) E) Rate = kika[A] [B]/(ki + k2[B])
The Lineweaver-Burk plots shown below are for enzyme catalyzed reactions. The reaction without and inhibitor is shown in blue. The reaction with an inhibitor is shown in red. Identify the type of inhibition in each plot. with I with I 1/vo without I without I 1/[S] 1/[S] with without I without I 1/[S] 1/[S] with I without I 1/[S] Problem 4 For each plot above describe how Km and Vmax are affected by the inhibitor.
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM