Choose the correct answer from the options in brackets. The [positive/negative] standard free‑energy change favors the oxidation of succinate by covalently‑bound FAD. This is consistent with K′eq [ >1 / =1 / <1 ]. Oxidation by NAD+ would require a large, [positive/negative] standard free‑energy change, with K′eq favoring the synthesis of succinate.

Give typed explanation of both questions otherwise leave it

Consider the malate dehydrogenase reaction, part of tricarboxylic acid cycle, shown below. malate + NAD+ oxaloacetate + NADH + H+ ΔGo ’ = 29.7 kJ/mol. It has been reported that the concentrations of NAD+ and NADH in yeast mitochondria were 20 mM and 0.3 mM, respectively. If we performed similar measurements and also determined that the concentration of malate in yeast mitochondria was 0.5 mM and that of oxaloacetate was 0.1 µM at pH 7.0 at 37˚C, use this information to calculate the free energy of the reaction of yeast in mitochondria.

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 . 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 activity of the enzyme β-galactosidase produced bywild-type cells grown in media supplemented with different carbon sources is measured. In relative units, thefollowing levels of activity are found:Glucose Lactose Lactose + glucose0 100 1Predict the relative levels of β-galactosidase activity incells grown under similar conditions when the cells arelacI−, lacIS, lacO+, and crp−.

Consider the malate dehydrogenase reaction, part of tricarboxylic acid cycle, shown below. malate + NAD+ oxaloacetate + NADH + H+ ΔGo ’ = 29.7 kJ/mol. It has been reported that the concentrations of NAD+ and NADH in yeast mitochondria were 20 mM and 0.3 mM, respectively. If we performed similar measurements and also determined that the concentration of malate in yeast mitochondria was 0.5 mM and that of oxaloacetate was 0.1 µM at pH 7.0 at 37˚C, use this information to calculate the equilibrium constant for the given reaction.

The glutamate dehydrogenase (GDH) catalyses the following reaction: *H3N- C H - CH₂ - CH₂ COO™ acide glutamique -COO + NAD+ + H₂O Time (min) A340 GDH COO™ с 5 1 2 3 4 1.760 1.718 1.675 1.635 1.595 CH₂ The answer: -1 - Vo 1.1.107 M.s-¹ - EA in 0.1 mL of GDH = 0.33 nkat CH₂ The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL protein to start the reaction. COO CO acide a-cétoglutarique The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M¹.cm¹ -1 + NH4+ NADH + H+ 6 1.550 7 8 10 9 1.510 1.489 1.476 1.451 Calculate the initial rate Vo of the reaction in M.s¹. - Calculate the enzyme activity of the volume of…

The Beutler test is used to diagnose GALT (UDP-glucose uridyltransferase) deficiency in infants.  Blood from the heel is spotted onto filter paper and the spot is then subjected to an enzyme assay.   Galactose 1-phosphate, NADP+ and UDP-glucose are added as substrates to the dried blood.  The increase in absorbance at 340nm is measured over time which corresponds to reduction of NADP+ to NADPH .   The amount of GALT activity in the blood of patients is therefore measured by stoichiometric relationship to the amount of NADPH produced from NADP+.   However, GALT does not directly reduce NADP+ as you can see in the above diagram.  Instead, the glucose 1-phosphate product from this reaction is shuttled into the oxidative phase of the pentose phosphate pathway by enzymes also present in RBCs.  Which three (or possibly more if you must) enzymes downstream of GALT allow for quantitative correlation of a product of GALT with the appearance of NADPH?  What is the stoichiometric relationship…

Assume that 2.5 ATPs are generated per NADH and 1.5 ATPs per FADH2. How many ATPs are generated from the FADH2 and NADH molecules from each repetition of the ββbeta-oxidation pathway? Express your answer as an integer.

Calculate the osmotic concentration of a solution consisting of 33.15 g NAD (C21H27N7014P2; mw = 663 g/mol) and 15.72 g FAD(C27H33N9O15P2; mw = g/mol) in 100g of water. 786 Your answer should be expressed in mOsm. YOU MUST SHOW YOUR CALCULATIONS WITH YOUR ANSWER.