Explain why the coordinated regulation of isocitrate lyase and isocitrate dehydrogenase is advantageous to an organism
Homework Answers
enzymes are regulated to assure production of intermediates and products at the rates required to keep the cell in a stable steady state and to avoid wasteful overproduction of intermediates. Isocitrate lyase is a key enzyme in the glyoxylate cycle and is essential as an anapleurotic enzyme for growth on acetate and certain fatty acids as carbon source.Most microorganism growing on acetate or fatty acids as the sole carbon source employ the glyoxylate bypass for the biosynthesis of cellular material . Isocitrate dehydrogenase is a digestive enzyme that is used in the citric acid cycle. Its main function is to catalyze the oxidative decarboxylation of isocitrate into alpha-ketoglutarate.
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Explain why the coordinated regulation of isocitrate lyase and
isocitrate dehydrogenase is advantageous to an organism
Explain the regulation of the enzyme glutamate dehydrogenase & discuss the physiological significance of this regulation.
Explain the regulation of the enzyme glutamate dehydrogenase & discuss the physiological significance of this regulation.
Question 5: Below is the chemical equation catalyzed by isocitrate dehydrogenase (i... the third reaction in...
Question 5: Below is the chemical equation catalyzed by isocitrate dehydrogenase (i... the third reaction in the citric acid cycle). α-ketoglutarate + CO2 + NADH + H+ isocitrate NAD (a) Calculate the physiological ΔG of the isocitrate dehydrogenase reaction at 25°C and pl 17.0 given: [NAD+]IN ADH]-8; [α-ketoglutarate] = 0.1 mM: [isocitrate] = 0.02 mM; standard state conditions for CO2 and H: and ΔG (b) Is this reaction a likely site for metabolic control? Explain. 。,--21.0 kJ/mol?
If a sample is positive on the Glutamate dehydrogenase, what organism is present (genus and species)...
If a sample is positive on the Glutamate dehydrogenase, what organism is present (genus and species) in the sample? Does this mean the organism is causing disease? Why or why not?
please explain answer Regulation of Lactate dehydrogenase (same enzyme described above). Lactose dehydrogenase (LDH...
please explain answer
Regulation of Lactate dehydrogenase (same enzyme described above). Lactose dehydrogenase (LDH) is a tetramer that can be regulated in several different ways. The crystal structure of the four subunits of lactate dehydrogenase is shown below. In the heart, lactose has a higher affinity for pyruvate than in the skeletal muscle. Analysis of LDH has identified that it is a substrate of FGFR tyrosine kinase, which results in an increase in the production of lactate. Some types of...
Acetyl COA + H2O Coo- o coo- Citrate synthase CH2 -OH -ooc— CH2 CH2 NADH +...
Acetyl COA + H2O Coo- o coo- Citrate synthase CH2 -OH -ooc— CH2 CH2 NADH + H+ COO- Oxaloacetate Coo- Citrate Aconitase Malate dehydrogenase NAD+ - Çoo- Çoo- ---OH -O00—-H HO-CH CH2 CH2 Coo- Malate Coo- Isocitrate Isocitrate lyase Malate synthase COO- COO- Coh CH2 Acetyl COA + H2O Ho Glyoxylate coo Succinate Figure 17.23 Biochemistry, Seventh Edition 2012 W. H. Freeman and Company Question 1 (10 pts) Using diagrams show the pathway that is used to convert succinate to...
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As an counter argument, explain why government control or regulation may be required to optimize social...
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Question 5: Below is the chemical equation catalyzed by isocitrate dehydrogenase (i... the third reaction in the citric acid cycle). α-ketoglutarate + CO2 + NADH + H+ isocitrate NAD (a) Calculate the physiological ΔG of the isocitrate dehydrogenase reaction at 25°C and pl 17.0 given: [NAD+]IN ADH]-8; [α-ketoglutarate] = 0.1 mM: [isocitrate] = 0.02 mM; standard state conditions for CO2 and H: and ΔG (b) Is this reaction a likely site for metabolic control? Explain. 。,--21.0 kJ/mol?
please explain answer
Regulation of Lactate dehydrogenase (same enzyme described above). Lactose dehydrogenase (LDH) is a tetramer that can be regulated in several different ways. The crystal structure of the four subunits of lactate dehydrogenase is shown below. In the heart, lactose has a higher affinity for pyruvate than in the skeletal muscle. Analysis of LDH has identified that it is a substrate of FGFR tyrosine kinase, which results in an increase in the production of lactate. Some types of...
Acetyl COA + H2O Coo- o coo- Citrate synthase CH2 -OH -ooc— CH2 CH2 NADH + H+ COO- Oxaloacetate Coo- Citrate Aconitase Malate dehydrogenase NAD+ - Çoo- Çoo- ---OH -O00—-H HO-CH CH2 CH2 Coo- Malate Coo- Isocitrate Isocitrate lyase Malate synthase COO- COO- Coh CH2 Acetyl COA + H2O Ho Glyoxylate coo Succinate Figure 17.23 Biochemistry, Seventh Edition 2012 W. H. Freeman and Company Question 1 (10 pts) Using diagrams show the pathway that is used to convert succinate to...
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