11. Quantitative Relationships between Rate Constants to Calculate K, Kinetic Efficiency (kcat/Km) and Vmax -II Triose phosphate isomerase catalyzes the conversion of glyceraldehyde-3-phosphate to dihydroxyacetone phosphate. Glyceraldehyde-3-P dihydroxyacetone-P The Km of this enzyme for its substrate glyceraldehyde-3-phosphate is 1.8 x 10-5 M When [glyceraldehydes-3-phosphate] =30 μM, the rate of the reaction, v, was 82.5 μmol mL-1 s-1. a. What is Vmax for this enzyme? b. Assuming 3 nm/mL of enzyme was used in this experiment (E total = 3nm/mL for this enzyme? c. What is the catalytic efficiency (kcat/km) for triose phosphate isomerase? d. Does this enzyme reach catalytic perfection?
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- Arrange the balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of glyceraldehyde 3-phosphate (the preparatory phase of glycolysis). First step Last step Answer Bank Fructose 1,6-bisphosphate - dihydroxyacetone phosphate + glyceraldehyde 3-phosphate Fructose 6-phosphate + ATP →→→→ fructose 1,6-bisphosphate + ADP Glucose + ATP → glucose 6-phosphate + ADP Dihydroxyacetone phosphate glyceraldehyde 3-phosphate Glucose 6-phosphate →→→→ fructose 6-phosphateGlucosidase I catalyzes hydrolysis of specific glucosidase I is a synthetic trisaccharide, glucose-al-2- glucose-al-3-glucose-a-O(CH₂) #COOCH3. Kinetic measurements oligosaccharides containing glucose. obtained using this trisaccharide as substrate in the deoxynorjirimycin at concentrations of 50 μM (), 100 μM absence (x-x) and presence of the inhibitor 1- A) were used to prepare the (-), and 200 μM (4 Lineweaver-Burk plot below: b) Page 3 12) 7. a) V/V (nmol/hr)-1 1.S 1.0- 0.5 1/Trisaccharide (mM)-! Estimate the values for Vmax and KM for the trisaccharide substrate in the absence of the inhibitor. 0.0 -1.0 0.0 One substrate for 1.0 2.0 Determine whether inhibition by 1-deoxynorjirimycin is competitive, non-competitive or neither.The Vmax of muscle glycogen phosphorylase is much larger than that of the liver enzyme. Discuss the functional signifi cance of this phenomenon.
- In working skeletal muscle under anaerobic conditions, glyceraldehyde 3-phosphate is converted to pyruvate (the payoff phase of glycolysis), and the pyruvate is reduced to lactate. Write balanced biochemical equations for all the reactions in this process, with the standard free-energy change for eachreaction. Then write the overall or net equation for the payoff phase of glycolysis (with lactate as the end product), including the net standard free-energy change.What is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s15) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8
- In humans, the biosynthesis of L-glutamine is catalyzed by the L-glutamine synthetase. The global reaction can be written as follows: ATP + glutamate + NH3 ADP + phosphate + glutamine The A,Gº' value for this reaction is -16.3 kJ.mol-1 (from left to right). 1- Explain the significance this information. 2- This reaction can be considered as the sum of two component reactions which are exergonic and endergonic, respectively, under standard conditions. Write these two component reactions and evaluate A,Gº of the endergonic reaction. Data: A,Gº of ATP hydrolysis = -30.4 kJ mol-¹41 The following data describe an enzyme-catalyzed reaction (hydrolysis of carbobenzoxyglycyl-L-tryptophan) Plot these results using the Lineweaver-Burk method, and determine values for KM and Vmax Velocity (mM.sec-) 0 024 0 036 0 053 0 060 0 061 0 062 Substrate Concentration (mM) 25 50 10 0 15 0 200 25 0 42 If the KM of an enzyme for its substrate remains constant as the concentration of the inhibitor increases, what can be said about the mode of inhibition and why? 43 Calculate the turnover number for an enzyme, assumıng Vmax IS 05 M sec1 and the concentration of the enzyme used is 0 002 M Why is it useful to know this? 44 Dıscuss the mechanism of the Bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues Make use of relevant graphs and diagrams to explain your answerPyruvate carboxylase catalyzes the first step of gluconeogenesis. ATP + HCO3─ + pyruvate → oxaloacetate + ADP + Pi ∆G0’ = ─2.1 kJ mol-1 a) Calculate ΔG for this reaction under the following physiological conditions: 370C, pH 7 [pyruvate] = [HCO3─] = 4.0 mM [oxaloacetate]= 2.0 mM [ATP] = 3.5 mM [Pi] = 5.0 mM [ADP] = 1.8 mM
- Indicate what will happen (increase, decrease or no effect) to the activity of enzyme or rate of the metabolic pathway given the following conditions: 1. epinephrine to the activity of glycogen synthase 2. high [2-carboxyarabinitol-1-phosphate] to the carboxylase activity of RuBisCO28. If 20 mM solution of Acetyl-phosphate is transformed to acetate by incubating with a catalytic amount of acetate kinase until equilibrium is reached. Acetyl-phosphate -> Acetate + Pi At equilibrium, the concentration of Acetyl-phosphate is 8 mM. Determine Keq and AG" for the hydrolysis of Acetyl-phosphate reaction. (R = 0.008314 kJ/mol K) .make a schematic diagram of BChE/AChE inhibitory determination Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide(AChI) molecules were utilized as substrate compounds of the reaction. Inthis regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) wasused to estimate BChE/AChE activity. In summary, 100 μL Tris buffersolution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of thesample solution (50‐200 mL) were added in deionized water and also20 μL of BChE/AChE enzymes solutions added. The mixture was thenincubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and25 mL) BChI/AChI were added to the incubator mixture. The reactionwas also started by adding 50 μL BChI/AChI. The activity of theseenzymes was evaluated using spectrophotometric spectra with awavelength of 412 nm.