The compound below which is labelled in two positions with 13c (as represented by the shaded spheres) was prepared and used to probe the mechanism of the aldolase enzyme employed in glycolysis. он о но OH Predict the pattern of 13c radiolabelling observed in the products: OH но. OH но,
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- Aerobic degradation of an organic compound by mixed cultureof organism in wastewater can be represented by following reaction. C3H6O3 + a O2 + b NH3 → c C5H7NO2 + d H2o + e CO2 A. Determine a, b, c, d and e, if YX/S = 0.4 d X/g S. B. Determine the yield coefficients YX/O2 and YX/NH3. C. Determine the degree of reductions for the substrate, bacteria and RQ for the organismsTable 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-1. Outline and describe the reaction scheme of the production of glucose from maltodextrin by using glucoamylase.Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-¹. Table 1: Glucoamylase Activity at different temperatures Maltodextrin Concentration (μmol/L) 0.5 1 1.5 2.2 5.5 11 Initial Reaction Velocity (μmol/L.s) T = 40°C 2.1 3.5 4.9 5.6 589 8.3 9.3 T = 60°C 5.2 9.7 13 16 23 31
- During enzyme analysis to determine glucose concentration (sample used is corn syrup stock sol. and enzymes are glucose oxidase and peroxidase), what conditions must be in place to ensure accurate results for such coupled reaction?Because of the position of arsenic in the periodic table, arsenate (AsO43- ) is chemically similar to inorganic phosphate and is used by phosphaterequiring enzymes as an alternative substrate. Organic arsenates are quite unstable, however, and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
- The following data were obtained in a study of an enzyme that is known to follow the Michaelis-Menten kinetics. Approximately, what is the value of Km tor this enzyme? Substrate added, umol/L Vo uM/sec 48 97 175 187 192 197 2 16 100 1000 198 OA 1 uM O8.2 pM OC 4 uM. OD. 8 uM OE 16 IM OF 1000 uM OG 97 uM/sec OH 175 UM/sec33333333333333333333333 Using the table below, differentiate the effect of two varying pH levels (as indicated by by the color) to the amylase enzyme. How does pH level affects the enzymatic reaction (enzyme-substrate complex)? Tube 1 Tube 2 Tube 3 Tube 4 Ingredients StarchAmylaseBuffer pH 7 StarchAmylaseBuffer pH 2 MaltoseWaterBuffer pH 7 StarchWaterBuffer pH 7 Color (1) (2) Orange BlueThe standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1 kJ/mol. Calculate the equilibrium constant for the reaction. Calculate AG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM. Is the reaction spontaneous under these conditions? HOCH, -20;POCH, H H H H H H ОН Н НО ОН Н H НО ОН H ОН H. ОН Glucose-l-phosphate Glucose-6-phosphate
- In the hexokinase reaction (in glycolysis) Keq caclualtion, what is the OBVIOUS problem with getting a Keq of 678? what should keq be normally? how can you EXPLAIN a Keq of 678?There is another class of aldolase enzymes known as Class II. These enzymes are found in fungi, algae, and some bacteria. This class differs for Class I in that these enzymes do not have a Lys residue associated with their active sites, but contain a divalent cation (usually Zn2+ or Fe2+) in the active site. Outline a possible mechanism for a Class II aldolase and explain the function of the metal ion in the reaction.(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90