Cyanide is a non-competitive inhibitor of Cytochrome c Oxidase. What Km would you expect if you treated 4µM cytochrome oxidase with enough cyanide to lower the enzymes Vmax to 10 units of activity?
In case of Non-competitive inhibition, the inhibitor binds to the enzyme or enzyme substrate complex and reduces the activity of the enzyme. Vmax is changed (reduced) in case of non competitive inhibition while Km remains same.
Since Cyanide is a non-competitive inhibitor of Cytochrome c Oxidase so Km will remain unchanged.
Cyanide is a non-competitive inhibitor of Cytochrome c Oxidase. What Km would you expect if you...
Would you expect anaerobic bacteria to possess the enzyme Cytochrome Oxidase? Why or why not?
Sodium azide is known to inhibit Cytochrome c Oxidase. Using sodium azide at a concentration of 2 µM, you run an enzyme assay. After careful data analysis, you determine the following values. Vmax = 50 µM/sec Vmax(app) = 50 µM/sec Km = 6 µM Km (app) = 18 µM Determine the type of inhibition present. Calculate the associated Ki(a), and (or) Ki(b), if applicable. Show your work.
Mitochondrial enzyme- cytochrome c oxidase activity lab 1. What are the four main components of complex 4 or cytochrome c oxidase? 2. What happened to the absorption 55nm after addition of mitochondrial preparation and why?
c. Describe the properties of i, competitive inhibitor and ii, noncompetitive inhibitor for this enzyme. Draw Lineweaver Burk plots for each and indicate where you can obtain Km and Vmax values for each plot and how they change with the addition of each type of inhibitor 3
This is a diagram of a known inhibitor of amylase. If you were to make a prediction, what type of inhibitor (competitive or non-competitive) is it? What is your reasoning?
10.What type of inhibitor is this? How do you know? (2) 11.For your assigned inhibitor 1, what are the apparent Km & Vmax? (NOTE: apparent Km& Vmax are just the Km & Vmax in presence of inhibitor, at a given concentration.) (2) Kinetics experiments were performed on PGI. Enzyme activity (initial velocity, Vo) was measured at varying concentrations of Glucose-6-phosphate (G6P). The enzyme concentration used in all experiments was 1.5 μM. 12.What will be the reaction rate with 0.500 mM...
a. what are the values of Vmax and Km in the abscence if the inhibitor what are the values of Vmax and Km in the presence of the inhibitor? b. what type of inhibition is it? c. what is the dissociation constant (Ki) of the inhibition? ***d. graph a linear scatter plot including equation. Homework (CHE 407) The initial velocity for an enzyme-catalyzed reaction is measured at various initial substrate concentration [S]o, in the absence and in the presence of...
You have an inhibitor for an enzyme that you are studying. The concentration of inhibitor used is 5.50 µM. The following data was collected for the non-inhibited reaction as well as the reaction that was inhibited. mmol/(mL min) mmol/(mL min) mM Substrate Vo Substrate Vo + Inhibitor 0.200 5.000 3.751 0.400 7.500 4.998 0.800 10.000 5.995 1.000 10.700 6.173 2.000 12.500 6.807 4.000 13.600 7.143 a. Plot this data using Excel or a graphing program. Make sure you give your graph has a...
An enzyme binds to a competitive inhibitor with Kd = 1.2 × 10-6 M at pH 7.0 and 25°C.(a)At what inhibitor concentration will 75% of the enzyme be bound to the inhibitor if there is no substrate present? (b) This enzyme has a Km of 4.0 × 10-5 M and a Vmax of 50 μM/s. At a substrate concentration of 3.0 × 10-4 M, calculate (i) the velocity of reaction in the presence of the inhibitor at 4.8 x 10-5 M (ii) the degree of...
1. What effect would the inhibitor Phenylalanine have on the Km and Vmax values when added to a solution with Tyrosinase. 2. Explain why Kojic acid is an inhibitor of Tyrosinase? 3. What is the difference in using D-DOPA vs. DOPA in a substrate experiment with Tyrosinase?