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- 3. Acetylcholinesterase is a serine hydrolase enzyme im- portant in nerve signal transmission, hydrolyzing acetylcho- line, an ester molecule with a positively charged quaternary nitrogen group. The structure of the physiologically relevant substrate of this enzyme is shown on the right. The quater- H₂C nary nitrogen group serves to anchor the molecule in the active site Gly121 Oxy- anion hole Gly122 Ala204 Substrate ACh His447 Catalytic triad Ser203 Glu202 Glu334 Ser229 CH3 N+ CH3 CH3 The a Scale document down rine protease family, consisting of a catalytic triad Ser203- His447-Glu334 with Ser203 supplying the nucleophilic hydroxyl group and an oxyanion hole com- prised of peptide NH groups of Gly121, Gly122, and Ala204, illustrated in the diagram above, for which carbon (green), nitrogen (blue), and oxygen (red) atoms are shown while hydrogen atoms are white. The enzyme catalyzed reaction can be represented by the following scheme: (a)( k1 K2 E + S = ES K-1 K3 EYE + P where ES…3. Calculate the ATP that is produced when linoleic acid (9,12-octadecadienoic acid; 18:2) is (a) oxidized to CO2 and H20 or (b) converted to the ketone body acetoacetate in the liver and then oxidized to CO2 and H20 in the peripheral tissues. 4. Explain the role of AMP-dependent protein kinase in regulating fatty acid metabolism. What are the ways hormonal control of fatty acid metabolism works between fed and fasted states? Please draw by hand/digitally, schematics showing this regulation in adipose tissue, muscle and liver.3.) As mentioned in the March1 outline a critical step in the glycolysis metabolic pathway (conversion for glucose to pyruvate that produces 2 ATP's) is the attachment of dihydroxyacetone phosphate to an isomerase enzyme via an iminium bridge (step1). There is a second step that takes the imine to the enamine that sets up the C-C formation reaction with an enol that you'll cover in two weeks. Show the mechanism for steps 1 (mild acid catalysis) and 2 (draw resonance forms for the iminium cation). In your mechanism, show the intermediate hemiaminal (carbinolamine). Step 2 may address one of the questions asked in Wednesday's class about the water taking out the N-H proton of the iminium cation versus a C-H proton? CH₂OPO3² E-NH₂ + O=C (step 1) CH₂OH Dihydroxyacetone phosphate Iminium (+) cation intermediate (step 2) Enamine (Enol) Intermediate H CH₂OPO32- E-N-C H C. OH H₂O E
- 5. The keto acids of the TCA cycle are also the other substrates of the aminotransferase family. How does this family of enzymes play a role in maintaining the NAD re-oxidation of NADH to NAD during glycolysis? (Use the amino acids alanine, aspartate, and glutamate in your explanation)3. In your textbook the termi- nal enzyme catalyzing the ter- minal step of glycolysis is known as pyruvate kinase (PK). No indication is given that in mammalian tissues there are four different iso- forms of this enzyme. The four mammalian isoforms are known as PKL, PKR, PKM1 and PKM2. PKL is expressed in the liver, and PKR is ex- pressed in red blood cells. C PKM1 and PKM2 are derived from altemative splicing of the PKM gene. PKM1 is a constitu- tively active isoform expressed Active Site A PKM2 Monomer B Fructose-1,6-Bisphosphate N Phe, Ala, Ser Binding Site PKM2 Tetramer "Activator" Binding Site in differentiated cells from various tissues. In contrast, PKM2 has low basal activity and is activated by an effector molecule fructose 1,6-bisphosphate (FBP). PKM2 is expressed in most proliferating cells. In addition, the regulation of PKM2 pyruvate kinase activity plays an essential role in cancer metabolism and is crucial for the growth and survival of cancer cells. Recently, PKM2 has…5. Based on your understanding of allosteric regulation and using terminology related to the allosteric (MWC) model, explain how the enzyme glycogen phosphorylase is affected by the binding of AMP and what affect this binding would have on the overall activity of the enzyme. Predict what would happen to the activity of the enzyme when glycogen phosphorylase is covalently modified and there are high levels of ATP in the cell.
- 1. ( . tion can be represented by the so-called Michaelis equation ) The velocity of an enzyme catalyzed reac- Vmax [S] Vo = Km Vo = max kcat [Eo] [So] (Км + [Sol) V max where [So] is the initial substrate concentration, [Eo] is the total enzyme concentration, kcat is the cataly- tic rate constant or turnover number, and KM repre- sents the Michaelis constant. The graph on the right illustrates the dependence of the velocity of the reaction as a function of substrate concentration. Ex- Km [S] (mm) plain why the maximal velocity can be represented by the expression Vmax = Kcat [Eo] at very high substrate concentrations. Vo (µm/min)Assume that the gene for pyruvate dehydrogenase kinase is mutated and the mutatedenzyme remain active in the presence or absence of upstream regulatory signals. Patients withsuch a gene mutation exhibit all the symptoms of beriberi. Do you think beriberi, resulting fromsuch mutations of pyruvate dehydrogenase kinase, can be successfully treated by placing suchpatients on a thiamine-enriched diet? Briefly explain your reasonings.(d) of glucose oxidation in diabetic human patients treated with Metformin (●) and in (nondiabetic) control human patients (0). At –150 min both groups of subjects were started on an intravenous feed of 3-(®H)-glucose, and at t = 0 min they were started on an oral glucose tolerance test whereby a measured amount of glucose in water (a syrupy mixture) was swallowed followed by measure- ment of blood glucose levels at 30 min intervals. The flux of glucose oxidation was measured by the appear- ance of 3H2O in the blood stream. While the information The diagram to the right compares the rate 8000 ORAL GLUCOSE 6000- 4000- 2000- -120 -60 60 120 180 240 300 Minutes cannot be directly extracted from the reaction mecha- nism diagrams in the textbook, the glycolytic step in which the tritium is first released into water is that catalyzed by TPI, as illustrated at the beginning of Question #3. Explain why this step is suitable for measuring the flux of glycolysis through the release of °H…
- 4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.1. Opine dehydrogenases (ODH) have evolved in invertebrate marine organisms with wide-ranging physiological roles. The first class of this family of enzymes provides an alternative pathway for the lactate dehydrogenase pathway in anaerobic energy production. The lactate dehydrogenase pathway is found in higher organisms and in mammals including humans. One class of opine dehydrogenases catalyzes the reductive coupling of pyruvate to N-a-carboxyalkyl-L-amino acids represented by the re- action below: དང་ NH₂ ODH ས HO S མིནྟཱ ཨཱར པ 'ནཔི ཏཏྭཱ ཡཾ དསྨཱ ཨབྷིནྡནྟི ཨཱ R₂ OH NAD(P)H NAD(P)* R OH R₁ R₂ where R1 is the side chain of the amino acid, R2 represents the alkyl group of the a-keto acid that is coupled to the amino acid, and NAD(P)H/NAD(P)* are the reduced/oxidized forms of nicotinamide ad- enine dinucleotide phosphate, a cofactor of the enzyme that catalyzes oxidation-reduction reactions. (a). : The product of the reaction has two chiral centers as shown: The Ca atom of the amino acid…1. Opine dehydrogenases (ODH) have evolved in invertebrate marine organisms with wide-ranging physiological roles. The first class of this family of enzymes provides an alternative pathway for the lactate dehydrogenase pathway in anaerobic energy production. The lactate dehydrogenase pathway is found in higher organisms and in mammals including humans. One class of opine dehydrogenases catalyzes the reductive coupling of pyruvate to N-a-carboxyalkyl-L-amino acids represented by the re- action below: NH₂ ི་ ODH HO R 요 OH སྨིཾནྟཱ ར པ དརཱ ཨཱཋཏྭཱ… … ཨཱསྨིཾ ཏྟཏྟིནྡནྟི ཨཱ HO NAD(P)H NAD(P)* S R₁ R₂ where R1 is the side chain of the amino acid, R2 represents the alkyl group of the a-keto acid that is coupled to the amino acid, and NAD(P)H/NAD(P)* are the reduced/oxidized forms of nicotinamide ad- enine dinucleotide phosphate, a cofactor of the enzyme that catalyzes oxidation-reduction reactions. (a). The product of the reaction has two chiral centers as shown: The Ca atom of the amino acid…