Let's do the Tricarboxylic Acid Cycle thing. Structural Enzyme, Formula activator and formula of the of the substrate Steps Structural Is the reaction reversible or irreversible? coenzyme product required
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- BIOC 384 Regulation of Enzyme Activity Q7.1: Describe how ATP and CTP regulate ATCase enzyme activity and why these two effectors are considered heterotropic allosteric effectors.384 Overview of Enzymes Q6.1: Three critical features of enzyme structure and function contribute to the overall efficiency of enzymes as biological catalysts and to their central role in biochemical processes. Articulate these three key features and describe a specific enzyme example that illustrates each one.Reaction centers PSI and PSII are also called as per the wavelengths at which they have a maximumabsorbance. What are these wavelengths?
- The maximum saturation, 28.3ug of enzyme in 25ml water catalyzes the oxidation of ethanol at a rate of 2.5mm/min. Calculate the kcat in units of seconds if the enzyme has a molar mass of 65kg/mol.Glycolysis: Summary: Where does it occur?Enzyme Activity and Physiological Function, The Vmax of the enzyme glycogen phosphorylase from skeletal muscle is much greater than the Vmax of the same enzyme from liver tissue. (a) What is the physiological function of glycogen phosphorylase in skeletal muscle?
- Chapter: Lipid Metabolism Individuals with abnormally low levels of carnitine in their muscles suffer from muscular weakness during moderate exercise. In addition, their muscles have significantly increased levels of triacylglycerols. (a) Explain these two effects. (b) Can these individuals metabolize muscle glycogen aerobically?Velocity (mmol/minute) [S], (mM) No inhibitor Inhibitor 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8 The kinetics of an enzyme are measured as a function of substrate in the presence and the in absence of 2mM inhibitor (I). What are the values of Vmax and KM in the absence of inhibitor? In its presence? In its presence? What is the type of inhibition?Trend observed in graph and conclusion about the effect of temperature on enzyme activity. i) include a concise description of the trend observed in the graph shown in question 3 above, and explain this trend using the language presented in this unit and your biochemical knowledge of enzymes and reactions. In your conclusion, provide a logical argument supported by molecular theory that would explain any change observed in enzyme activity.
- Exercise 5-9 Phenylalanine deaminase Phenylalanine deaminase positive bacteria can remove the amine functional group from the amino acid and the amine group is released as ammonia waste. Phenylpyruvic acid is also produced by this reaction. What can phenylalanine deaminase positive bacteria do with phenylpyruvic acid?385 Synthesis of Fatty Acids and Triacylglycerols Q6.1: Under what metabolic conditions are excess carbohydrates be converted to stored tricylglycerols in adipose tissue? List the six steps required.What biochemical alterations facilitate the switch to aerobic glycolysis?
