Enzymes occasionally display weak "side" activities. Draw the structure of the product (other than ADP) of the reaction that results when pyruvate kinase, operating in reverse, uses lactate as a substrate.
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- Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.Radiotracer Labeling of Pyruvate from Glucose Determine the anticipated location in pyruvate of labeled carbons If glucose molecules labeled (in separate experiments.) with 14C at each position of (.tie carbon skeleton proceed through the glycolytic pathway.
- Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.1) Sketch out the schematic diagram for the enzymatic mechanism of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) Please provide the structure of the functional groups of the substrate and enzyme involved in the reaction at each step (rest of the structure can be indicated as R) Indicate clearly the flow of the electrons at each step Indicate in short form the cofactor involved and the acid or basic groups of the enzyme involvedThere are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…
- Sketch out the schematic diagram for the enzymatic mechanism of pyruvate dehydrogenase complex Please provide the structure of the functional groups of the substrate and enzyme involved in the reaction at each step (rest of the structure can be indicated as R) Indicate clearly the flow of electrons in the E-1 and E-2 reaction Indicate in short form the cofactor involvedDetermine if true or false 1. Isopentyl pyrophosphate (activated isoprene) undergoes cyclization during cholesterol biosynthesis 2. Malonyl CoA transacylase catalyzes the committed step in fatty acid biosynthesis. 3. Oxaloacetate carries acetyl CoA to the cytosol which is the site of fatty acid biosynthesis. 4. During fatty acid biosynthesis, propionyl CoA is the donor of the acetyl group. 5. During fatty acid biosynthesis, NADPH is used as the reducing equivalent in the process.ATP is both an inhibitor and substrate of adenyl cyclase. As a substrate, the enzyme converts ATP to cyclic AMP only when the energy sources of cells are low. cAMP mediates the synthesis of a kinase that adds a phosphate to glycogen synthase and phosphorylase. The Km value of the active site is 3.5 x 10-5M while the Km for the allosteric site is 1.7 x 10-3M. What is the implication of the difference in Km value of the active and allosteric site in terms of the utilization of the stored sources of energy of cells? Explain.
- SEARCH ABOUT Diphenylurea-derived cytokinin oxidase/dehydrogenase inhibitors for biotechnology and agricultureBecause it resembles the two physiological substrates, phosphonacetyl L - aspartate (PALA) is a strong inhibitor of ATCase. Low concentrations of this unreactive bisubstrate analog, on the other hand, enhance reaction velocity in the presence of substrates. The reaction rate rises as PALA is added, until three molecules of PALA are attached per molecule of enzyme. This maximum velocity is 17 times higher than it would be without PALA. With the addition of three additional molecules of PALA per molecule of enzyme, the reaction rate drops to practically nil. Why does PALA activate ATCase at such low concentrations?b) Following this experiment, you would like to elucidate the mechanism of action of pyruvate kinase. Unfortunately, the crystal structure of pyruvate kinase is not available, which requires the enzyme to be modelled based on the available three-dimensional structures of related enzymes. Suggest a bioinformatics approach that can be conducted to perform this study.