When the substrate concentration raising over the time , enzymes are performing at a high rate .When the substrate concentration reaches the saturation point , it will no longer provide the enzymatic activity. i.e The catalytic activity or enzyme conversion rate will raise at the beginning and it wil be maximum when substrate concentration reaches satuaration point. At this point the velocity at which reaction is occuring is maximum after utilization of the specific substrate concentration. Beyond that substrate concentration even if we raise the substrate concentration, it will not increase the velocity anymore. Therefore,the end velocity that they can maximum reach is known as Maximum Velocity or Vmax. .Now----
(Kindly Please give a LIKE for the answer. Thank You)
Based on the plot below, what is the Vmax? enzyme rate (s:1) 0 500 1000 1500...
What is the rate of an enzyme catalyzed reaction if the Vmax is 100µmol S→P/min and the Km is 7 mM and the substrate concentration is 11mM? Is the enzyme working at Vmax? What if the substrate concentration is raised to 25mM?
6. The Michaelis-Menten curve for enzyme X is shown below for substrate A. Indicate where on the plot you would determine Kcat, Km and kca/Km- (1 points) 400 300 F 200F 100 500 1000 1500 2000 substrate A, HM 6. The Michaelis-Menten curve for enzyme X is shown below for substrate A. Indicate where on the plot you would determine Kcat, Km and kca/Km- (1 points) 400 300 F 200F 100 500 1000 1500 2000 substrate A, HM
4. What does enzyme kinetics study? What is Vo, km, Vmax, Kcat, respectively? If you plot Vo versus (substrate), or 1/Vo versus 1/[substrate], how the curves would look like, and how to get Vmax and Km values?
17. An enzyme-catalyzed reaction has a Vmax of 6 M/s and V, of 4.5 nM/s when the substrate concentration is 1.5 M. What is the Km of this reaction? 2.0.5 b. 1.1 c. 22.5 d. 39 18. From the reaction data below, determine whether the reaction is first-order or second-order. Time (8) Reactant (M) 0 6,67
17. An enzyme-catalyzed reaction has a Vmax of 6 M/s and V, of 4.5 nM/s when the substrate concentration is 1.5 M. What is the Km of this reaction? 2.0.5 b. 1.1 c. 22.5 d. 39 18. From the reaction data below, determine whether the reaction is first-order or second-order. Time (8) Reactant (M) 0 6,67
The Lineweaver-Burke Plot for the enzyme in question 1 is shown below. In this plot, the y intercept (0.019153) is 1/vmax and the x intercept (-0.0449) is -1/km. What are the exact km and vmax based on this graph (show your work)? Km= Vmax=
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a series of assays where you measured the rate of reactions as you varied the concentration of substrate in each assay (Table A). Estimate from a Michaelis-Menten plot approximate values for Vmax, KM, Kcat, and the specificity constant for this enzyme and substrate. (The only information that is given is this paragraph and the table below). Table 1: [S] (μM) v (μmol/L/min) 0 0 5...
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be: a. 98% Vmax (show your work) (2) b. 99% Vmax (answer only) (1) c. 99.9% Vmax (answer only) (1)
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be: a. 98% Vmax (show your work) (2) b. 99% Vmax (answer only) (1) c. 99.9% Vmax (answer only) (1)
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...