Catalase has a Km of 25 mM and a kcat of 4.0 x 107 s−1 with H2O2 as a substrate. Carbonic anhydrase has a Km of 26 mM and a kcat of 4.0 × 105 s−1. What do these data tell you about these two enzymes?

a newly identified bacterium called Nomore biochem is unable to synthesize ubiquinone. A mobile electron carrier called CXC3 is used as a substitute. From the information provided in the table, calculate delta G' and Keq value at 298K for the redox reaction that occurs in the Nomore Biochem electron transport chain. (constants: R=8.3 J/degree x mol, F= 96.1 kJ/v x mol Half Reactions E' (V) ubiquinone + 2e- + 2H+--> Ubiquinol + H2 0.045 NAD+ + 2e- + 2H+ --> NADH + H+ -0.320 CXC3 + 2e- + 2H+ --> CXC3H2 -0.450 explain the impact that using CXC3 instead of ubiquinone will have on ATP production in the cell. How might the cell adapt to this situation?

The Keq (25C) of the reaction below is 635.67.  Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the  standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy change

The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…

The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)

The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"

The glucose oxidase used in this experiment has a concentration of 27 U/mg. Calculate the mass (in g) of solid glucose oxidase required to react with all the glucose in 4.00 µL of10.0- mM glucose sample assuming the reaction proceeds for 30 minutes.

Write the balanced reaction catalyzed by phophoenolpyruvate carboxylase (P PC). Remember to add any cofactors, and to draw the structure formulas (a line-bond representation is fine) for the main substrate and product of the reaction.

The lipase substrate emulsion contains 0.500 mg of olive oil per 3 mL  Also, the molar mass of the olive oil is 885 g/mol.  If all of the olive oil in a 3 mL reaction is "digested" by pancreatic lipase in a reaction, how many molecules of olive oil have been degraded?