What type of variables are both lactose concentration and enzyme concentration in these experiments? a.Control variables b.Dependent variables c.Experimental variables What type of variable is pH in Part A of this experiment a.Experimental variable b.Control variable c.Dependent variable
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- Amino AcidMetabolism. a. What are the SIXprecursors used in amino acid biosynthesis? b. What are the SEVEN metabolic intermediates that result from amino acid degradation? c. Circle the metabolites found in your answers to both a) & b) above. d) What is the difference between glucogenic and ketogenic amino acids? List the glucogenic amino acids, the ketogenic amino acids & the amino acids that are both glucogenic & ketogenic.How Is Metabolism Regulated? (Integrates with Chapter 15.) Metabolic regulation is achieved via regulating enzyme activity in three prominent ways: allosteric regulation, covalent modification, and enzyme synthesis and degradation. Which of the.se three modes of regulation is likely to be the quickest; which the .slowest? For each of these general enzyme regulatory mechanisms, cite conditions in which cells might employ that mode in preference to either of the other two.Comparing Glycolysis Entry Points for Sucrose Sucrose can enter glycolysis by either of two routes: Sucrose phosphorylase: Sucrose + Pi fructose + glucose-1-phosphate Invertase: Sucrose + H20 fructose + glucose Would either of these reactions offer Jin advantage over the other In the preparation of hexoses fur entry into glycolysis?
- Energetic of Fructose-1 ,6-bis P Hydrolysis (Integrates with Chapter 3.) The standard free energy change (G) for hydrolysis of fructose-1. 6-bisphosphate (FBP) to fructose-S-phosphate (F-6-P) and P: is -16.7 KJ/mol: FBP + H2O fructose-6-P + Pi The standard free energy change (G) for ATP hydrolysis is -30.5 KJ/mol: ATP + H2O ADP + Pj What is the standard free energy change for the phosphofructokinase reaction: ATP + fructose-6-P ADP + FBP b. What is the equilibrium constant for this reaction? c. Assuming the intracellular concentrations of [ATP] and (ADP] are maintained constant at 4 mM and 1.6 mM, respectively, in a rat liver cell, what will be the ratio of [FBP]/[fructose-6-P] when the phosphofructokinase reaction reaches equilibrium?Understanding Enzyme Mechanisms Related to Pyruvate Carboxylase Based on the mechanism for pyruvate carboxylase (Figure 22.3), write reasonable mechanisms for the reactions that follow:Factors Affecting Enzyme Activity: Catalase 3. What is the marker for the enzyme’s optimum condition?
- Of the steps illustrated how many are unidirectional? Identify the substrate and product of each of these steps. Identify the three enzymes that are likely to be regulated in glycolysis? How did you make this determination. Glycogen synthase is an enzyme that catalyzes the synthesis of glycogen from glucose. Glucose 6 phosphate activates glycogen synthase by allosteric regulation. Illustrate and describe how this allosteric modulation is likely to occur? Glycogen phosphorylase, an enzyme that catalyzes the breakdown of glycogen to form glucose, is active when a phosphate group is added. This is an example of enzyme regulation by ____________________________.Discuss the glycogen degradation. Give the three enzymes required for this process and their functions.A 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/min
- Make tables of reactions of the Glycolysis and Gluconeogenesis with enzyme names and DGo’ values. I provided a template for the table below. With this information, determine the overall free energy of each pathway. Discuss the differences in these values and suggest a reason for this difference. Please answer very soon will give rating surelyHi, help please. Discuss each method of regulating phosphofructokinase below as indicated by the circle. Discuss 1.) The type of regulation occurring, 2.) What compound or condition performs the regulation, 3.) How/why it influences the enzyme activity.Calculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilution