(i) Explain the PFK-1 activity in the absence and presence of fructose 2, 6- bisphosphate. (ii) Explain the effect of increased ATP on PFK-I
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![Refer to Figure 3 which shows the relationship between phosphofuctokinase-1 (PFK-1)
activity and fructose 2,6-bisphosphate.
100
+F2,6BP
80
60
40
-F2,6BP
20
0.05 0.1 0.2 0.4 0.7 1.0 2.0 4.0
EFructose 6-phosphate] (mm)
Figure 3
(i)
Explain the PFK-1 activity in the absence and presence of fructose 2, 6- bisphosphate.
(ii)
Explain the effect of increased ATP on PFK-I
PFK-1 activity (% of Vma)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F875cac72-0f82-4647-92a7-f5dce3b969ce%2F5f3c2013-6732-4d16-b97e-1e650daac0f5%2Fpnjs76i_processed.jpeg&w=3840&q=75)
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- uizzes/67365/take Based on the image below, select the correct statements. Note: There may be more than 1 correct response. I Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP > 5-Phosphoribosylamine I adenylosuccinate PRPP lyase 9 steps Adenylosuccinate AMP IMP <-- ADP - AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP - XMP ADP ATP GMP يمد XMP-glutamine amidotransferase Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. O Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels. 8 OBCBased on the image below, select the correct statements. Note: There may be more than 1 correct response. Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP -> PRPP 5-Phosphoribosylamine I adenylosuccinate lyase 9 steps Adenylosuccinate AMP IMP <-- ADP <- AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP. XMP ADP ATP XMP-glutamine amidotransferase GMP يا Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels.Upon careful analysis, you discover that mutation causes the patient's glucokinase to behave exactly like hexokinase (i.e. an increased affinity for glucose with decreased Km value and a decrease in the Vmax). Which of the following lines on the Lineweaver-Burk Plot (Figure 1) best represents the mutated enzyme compared to normal glucokinase? Explain. B Normal Glucokinase [V] 1 [S] Figure 1
- You have a crude lysate sample (CL) containing a mixture of six proteins (1, 2, 3, 4, 5, ẞ- galactosidase), and your goal is to obtain purified ẞ-gal. Some characteristics of these proteins are shown in the table below. Protein Alcohol dehydrogenase Carbonic anhydrase Insulin B chain Phosphorylase B Glutamic dehydrogenase B-galactosidase 45% Concentration of ammonium sulfate (AS) required for precipitation Molecular Weight (kDa) Isoelectric point (pl) 38 3.7 80% 65% 20% 30% 45% 28 4.8 4 5.3 98 6.8 49 9.5 115 5.3 You begin your purification by performing an ammonium sulfate (AS) precipitation. You add the appropriate concentration of AS to your CL sample, incubate overnight at 4°C, then centrifuge to generate a supernatant (AS-S) and pellet (AS-P). What concentration of AS will you use to precipitate Glutamic dehydrogenase? © 20% O 30% 45% 65% 80%One of your colleagues has obtained a sample of muscle phosphorylase b that is known to be relatively inactive. She has approached you for advice on how to set up an appropriate assay. She has the following items available, not all of which are appropriate for this study. Help her out by selecting the items that she should use and what their purpose is in the assay, and then explain why each of the other items would not be useful. 1. 100 UM AMP 2. 100 UM GTP 3.100 uM glucose 4. 100 uM glucose 6-phosphate 5. Branched glycogen 6. Amylose (i.e. unbranched glycogen) 7.50 mM HEPES buffer, pH 7.5 8. 50 mM potassium phosphate buffer, pH 7.5 Write out a short explanation for each of the above items, and upload your answers by the due date.In class, I mentioned that fructose is metabolized differently in the liver compared to glucose. Refer to the figure shown below to calculate the number ofATPs you would expect from the metabolism of fructose in the liver. Show your work! Fructokinase Fructose Fructose-1-P АТР ADP Aldolase B Dihydroxy- acetone phosphate Glyceraldehyde АТР Triose kinase Triose phosphate isomerase ADP 4 - Glyceraldehyde-3-P Glycolysis Руruvate Acetyl-CoA Fatty acids and triglycerides
- We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: I- *H₂N- glutamate H - C-COO CH₂ CH₂ COO 0.1 M phosphate buffer pH 7.4 : 550 μL 1.2 M alanine: 100 μL CH3 pyruvate CH3 C time (min) A340 CIO O COO The enzyme reaction is alized in the following conditions: In a 1 cm-cuvette are added: COO™ pyruvate lactate dehydrogenase* (LDH, 300 µμg.mL-¹): 50 μL 1.5 mM NADH : 200 μL 0.04 M a-ketoglutarate: 500 µL serum containing ALAT: 600 μµL ALAT NADH + H+ 0 0.915 a-cétoglutarate COO LDH * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. с=0 CH₂ 1 0.741 Reaction 2: NAD+ CH₂ COO™ H-C CH3 OH COO™ lactate alanine H + *H3N-C The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: ENADH at 340 nm =…Explain why people with a hereditary deficiency of carnitine acyltransferase II have muscle weakness. Why are the symptoms more severe during fasting? (Keep your answer to at least a paragraph)We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: +H3N- glutamate H C CH₂ CH₂ COO -COO + pyruvate CH3 C=0 0.1 M phosphate buffer pH 7.4 : 550 µL 1.2 M alanine : 100 μL CH3 time (min) A340 COO COO™ pyruvate lactate dehydrogenase* (LDH, 300 µg.mL-¹): 50 μL 1.5 mM NADH: 200 μL 0.04 M a-ketoglutarate: 500 μL serum containing ALAT: 600 μL The enzyme reaction is realized in the following conditions: In a 1 cm-cuvette are added: 0 0.915 ALAT NADH + H+ LDH a-cétoglutarate COO * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. Reaction 2: NAD+ 1 0.741 C=O H CH₂ CH₂ COO™ CH3 C-OH COO lactate The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: alanine ENADH at 340 nm = 6220 M¹.cm1. One…
- BIM-46187 is a protein inhibitor that binds to the a-subunit of the G, protein. It prevents the GDP/GTP exchange and prevents activity of the G protein. Which of the following would you expect to see lower levels of as a result? You can select more than one answer. S-S Mol. W: 795.11 Image: https://aobious.com/aobious/protein-inhibitors/1086-bim-46187.html Select one or more: O a. Cyclic AMP (CAMP) O b. Tyrosine kinase HSP O d. Adenylyl Cyclase (AC) O e. DAG O f. JAK O g. IP3A solution of [U 14C] glucose-1-phosphate (specific activity = 16,000 cpm/mmole) was incubated with glycogen and glycogen phosphorylase, an enzyme which adds glucose units on to glycogen. Radioactivity was incorporated into the glycogen primer at a rate = 2550 cpm/min. The rate of the enzymatic reaction in units of mmole glucose incorporated per minute is: (a) 0.016 mmol/min (b) 0.57 mmol/min (c) 0.16 mmol/min (d) 5.7 mmol/min1. A Lineweaver-Burk Plot is shown below. 30 25 Curve A y = 3.1207x + 2.4978 20 15 Curve B y = 1.0003x + 2.3602 10 5 -3 1 5 7 11 1/[Catechol] (mM1) With these curves, determine the following enzyme parameters. Show all pertinent solutions. a. Km of Curve A and Curve B b. Vmax of Curve A and Curve B c. Assuming that one of these curves corresponds to the kinetics of one enzyme and one substrate, which curve represents the effect of an inhibitor? Why do you say so? d. What type of inhibition is exhibited by your answer in question c? Why do you say so? 1/V, (units of activity 1)
