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asrealize.com/assignments/viewer/classes/61227fd32e355544e0a77ded/assignr ng of Enzymes nzymes Effects of Enzymes This graph shows the effects of an enzyme on a particular reaction. The red line on the graph shows the reaction without the enzyme while the blue line shows how the reaction progresses with the enzyme. 2. According to the graph, the enzyme V Choose... affect the initial energy of the reactants. The enzyme V Choose... the activation energy. The overall energy released Check Answer

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Please answer questions 10 and 11 using the first picture for reference.

=display&toolld3calendar-mybb, Gmail YouTube Maps calendar-tool Home Courses C A Question Completion Status: 20 3D 70 100| 11凸|12D|| 130 14 150 16 170 QUESTION 14 A newly isolated bacterial isocitrate dehydrogenase is found to have a molecular mass of 180KDA and SDS-PAGE shows it to be a homodimer. 1mg of enzyme produces 0.05 mmoles of product per minute per mL. What is the turnover number of this enzyme in µmol product produced per pmol of enzyme subunit per mL? O a. 4.5 Ob.4500 O c. 9000 O d.9 QUESTION 15 The absorption spectrum of NAD" and its reduced form NADH are shown below: Absorption 2,4 2,0 1,6 Click Save and Submit to save and submit. Click Save All Answers to save all answers. Save All Ar 8 11 JAN 9. tv W ... LO

Please answer number 5 and highlighted answers are wrong please provide me a explanation why it is wrong and what is the correct answer for it. Thank you.

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 s1

The glucose/glucose-6-phosphate substrate cycle involves distinct reactions of glycolysis and gluconeogenesis that interconvert these two metabolites. Assume that under physiological conditions, [ATP] = [ADP]; [P;] = 1 mM. Consider the glycolytic reaction catalyzed by hexokinase: ATP + glucose ADP + glucose-6-phosphate AG = - 16.7 kJ/mol (a) Calculate the equilibrium constant (K) for this reaction at 298°K, and from that, calculate the maximum [glucose-6-phosphate]/ Iglucose] ratio that would exist under conditions where the reaction is still thermodynamically favorable. (b) Reversal of this interconversion in gluconeogenesis is catalyzed by glucose-6-phosphatase: glucose-6-phosphate + H20 = glucose + P AG" = -13.8 kJ/mol

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64 Consider docosanoic acid, C2H43 CO₂H. a. Label the x and ß carbons. b. Draw the acyl CoA derived from this fatty acid. c. How many acetyl CoA molecules are formed by complete B-oxidation? d. How many cycles of ß-oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complete catabolism of this fatty acid? Required:

The standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol  K=1.987 cal/mol K

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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 RuBisCO

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Draw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I I

Degradation of normal glycogen results to 97.2% glucose 1-phosphate and 7.2% glucose. Assuming a ratio of glucose 1-phosphate to glucose recorded in a glycogen sample from a patient with a liver disease was 100,  The patient’s most likely enzymatic deficiency is _________

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The table below shows the purification of liver lactate dehydrogenase. Purification Table of liver LDH Step Crude Extract Ammonium Sulfate DEAE-Sephadex 5'AMP-Sepharose Volume (mL) 200 100 112 40 LDH activity (Units/mL) (mg/mL) [Protein] 47.0 50.00 90.0 63.00 51.0 1.50 137.0/ 0.4 Calculate the LDH yield for the ammonium sulfate step. Provide answer to one decimal only. Show Transcribed Text this is biochemistry and the topic is protein purification could you pleaae show me the full workings even the workings for the comversions

The glucose/glucose-6-phosphate substrate cycle involves distinct reactions of glycolysis and gluconcogenesis that interconvert these two metabolites. Assume that under physiological conditions, [ATP] = [ADP] and [Pi] =1 mM. Consider the following glycolytic reaction catalyzed by hexokinase: ATP + glucose = AG' = -16.7 kJ/mol ADP + glucose-6-phosphate (a) Calculate the equilibrium constant (K) for this reaction at 298 K, and from that, calculate the maximum [glucose-6-phosphate]/[glucose] ratio that would exist under conditions where the reaction is still thermody- namically favorable. (b) The reverse of this interconversion in gluconeogenesis is catalyzed by glucose-6-phosphatase: glucose-6-phosphate + H,0 = glucose + P, AGr = -13.8 kJ/mol K= 262 for this reaction. Calculate the maximum ratio of [glucose]/ [glucose-6-phosphate] that would exist under conditions where the reaction is still thermodynamically favorable. (c) Under what cellular conditions would both directions in the…

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Glucosidase 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.

Many metabolites are maintained at steady-state concentrations that are far from equilibrium. A comparison of Kéq and Q, the mass-action ratio, can determine whether a metabolic reaction is far from equilibrium. The equation for this equilibrium is, fructose 6-phosphate + ATP = fructose 1,6-bisphosphate + ADP Calculate Kg for this reaction at T = 25.0 °C. Ka 1.8 x10-6 AG' = -14.2 kJ/mol Incorrect Calculate the mass-action ratio, Q, from the approximate physiological concentrations for rat heart tissue shown in the table. Metabolite Concentration (µM) Q = 3 fructose 6-phosphate 81.0 fructose 1,6-bisphosphate 15.0 Incorrect ATP 12,500 ADP 1,340

Name: Hendric Nduwuba DNP and Cellular Respiration Summary https://www.youtube.com/watch?v=eLtRan2qFx0 Your assignment today is to summarize in two paragraphs (8 sentences total) the effects of dinitrophenol (DNP) on the human body. Make sure you explain what DNP is, the stages of cellular respiration, and how DNP alters the metabolism of the person using it (side effects). The following vocabulary terms need to be used: cellular respiration, adenosine triphosphate, and dinitrophenol (DNP). Your objective is to describe the role of ATP in cellular respiration in order to explain how DNP affects the rate of metabolism. The first paragraph is an introduction to the summary and the second paragraph is an explanation of the main idea. You will be graded on this criteria: main idea, explanation of cellular respiration, explanation of DNP, and paragraph structure.

The standard state free energy change for Step 4 of glycolysis (where an aldolase enzyme splits fructose 1,6-bisphosphate into GAP and DHAP) is +23.8 kJ/mol. Yet, glycolysis still proceeds spontaneously in the vast majority of cells. Why does this step in particular proceed spontaneously under typical cellular conditions?

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