glutamate dehydrogenase e NH3 -C-CH-CH2-CH2-C + H20 + NAD CH2-CH2-C-O + NH NADH + H (a) Label the correct substances as the substrate, enzyme, and co-enzyme. (b) Which of the six classes does the enzyme of this reaction belong to? Why? (c) What is the name of the first molecule in this reaction? (d) Which metabolic pathway is this reaction likely to be a part of?
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- The enzyme that catalyzes reaction below can be classified as: CoO COO NAD+ NADH + H* Но- | malate -C- H-Ć- dehydrogenase Охaloacetate Malate isomerase lyase hydrolase oxidoreductase ligase transferaseThe glutamate dehydrogenase (GDH) catalyses the following reaction: +H₂N- H - - CH₂ - CH₂ COO acide glutamique COO™® + NAD+ + H₂O GDH COO C: CH₂ CH₂ COO™ O + NH4+ NADH + H* The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: -0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min - Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. acide a-cétoglutarique The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data: ENADH at 340 nm = 6220 M¹.cm¹ Time (min) 1 2 3 4 5 6 7 8 9 1.760 1.718 1.675 1.635 1.595 1.550 1.510 1.489 1.476 A340 10 1.451 - Draw the graph A = f(t). Calculate A340 at t = 0 and place this point on the curve. - Comment the shape of the curve, particularly the portion that corresponds to a…1. The first step in the payoff phase of glycolysis is catalyzed by the enzyme glyceraldehyde 3-phosphate dehydrogenase, an enzyme that contains a nucleophilic cysteine playing a central role in the reaction. A) In the direction of gluconeogenesis, what reaction does this enzyme catalyze? AG° = -6.3 kcal/mol for this reaction in the direction of gluconeogenesis. Based on what you know about the substrates involved, provide two chemical reasons as to why the AGO of this reaction is negative.
- The glutamate dehydrogenase (GDH) catalyses the following reaction: H +H₂N- -C -COO CH₂ CH₂ COO™ acide glutamique + NAD + H₂O GDH Time (min) A340 COO™ c=o CH₂ 5 1 2 3 4 1.760 1.718 1.675 1.635 1.595 CH₂ COO + NH4+ NADH + H+ acide a-cétoglutarique The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M¹.cm7 6 7 8 9 10 1.550 1.510 1.489 1.476 1.451 Calculate ammonium sulphate, NADH, concentrations in the reaction medium at t = 0. proteins - Draw the graph A = f(t). Calculate A340 at t = 0 and place this point on the curve. -…Order the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 2 3 4 answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD1. Cyanide, oligomycin, and 2,4-dinitrophenol are all inhibitors of oxidative phosphorylation in mitochon- dria. Provide an explanation to the following conditions regarding these potent inhibitors. (a) Explain why adding cyanide to an active in vitro suspension of mitochondria blocks ATP synthesis. What happens to the rate of ATP synthesis when 2,4-dinitrophenol is added to this mitochon- drial suspension after it was treated with cyanide? (b) Explain why the rate of oxygen consumption decreases in an in vitro suspension of mito- chondria when oligomycin is added. What happens to the rate of oxygen consumption in this oligomycin- inhibited system after adding 2,4-dinitrophenol? Explain.
- Indicate the general type of enzyme that mediates each glycolysis reaction depicted below. (e.g. Transferase, Oxidoreductase, Kinase, Hydrolase, Lyase, or Isomerase) iii. O H Glyceraldehyde-3-phosphate → 1,3-Bisphosphoglycerate H-C-OH + NAD CH₂O-P + P₁ H-O- -C-H Glucose →→ Glucose-6-phosphate H b 0 OH HO OH H-C- 0 -H HO- H ОН H-C-OH + NADH +H+ CH₂O P P ATP ADP 1 H (P-O- -C- H H HO OH 2-Phosphoglycerate → Phosphoenolpyruvate 0 OH H ОН -O~(P) + HOHOrder the cofactors based on their use in the mechanism of the a-ketogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 (Choose ] [Choose ] FAD Lipoamide 2 Fe 2S cluster TPP Biotin 3. NAD+ 4 [Choose ] 2.In relation to Carbamoyl Phosphate Synthetase enzyme, answer the following: A- What are the two isoforms of this enzyme, explain why there are two isoforms? B- What are the clinical manifestations associated with the deficiency of these two enzymes? C- Write down the biochemical reaction and the name of the metabolic pathway that these two isoforms are involved in, and how many ATP is utilized by these two isoforms?
- Von Gierke’s disease is also known as glycogen storage disease type I. Patients with von Gierke’s disease lackglucose 6-phosphatase activity. Two prominent symptoms of this disorder are fasting hypoglycemia and lactic acidosis (elevated lactate levels in the blood), especially during strenuous exercise. Explain why these symptoms occur. What chemical reaction does this enzyme catalyze? Which pathways involve this enzyme? Lacking thisthe enzyme will cause impairment of which pathways?• Pls consider what pathways are affected by Von Gierke’s disease. Include in your explanation involving Cori’s cycle. can you please do not write by your hand? I mean computer if you can. thank youVon Gierke’s disease is also known as glycogen storage disease type I. Patients with von Gierke’s disease lackglucose 6-phosphatase activity. Two prominent symptoms of this disorder are fasting hypoglycemia and lactic acidosis (elevated lactate levels in the blood), especially during strenuous exercise. Explain why these symptoms occur. What chemical reaction does this enzyme catalyze? Which pathways involve this enzyme? Lacking thisenzyme will cause impairment of which pathways?• Pls consider what pathways are affected by Von Gierke’s disease. Include in your explanation involving the Cori’s cycle.. Because of the position of arsenic in the periodic table, arsenate (AsO}-) is chemically similar to inorganic phosphate and is used by phosphate-requiring enzymes as an alternative substrate. However, organic arsenates are quite unstable and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.