A patient suffers severe tachycardia upon consuming even a small amount of alcohol. What enzymatic issue might be the cause? Failed alpha-helix formation Enzymatic Km increase Failed beta-sheet formation Enzymatic Km decrease Loss of enzyme half-life
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- Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a biomolecule at least partially different from the pathway for its catabolism? Why is the pathway for the biosynthesis of a biomolecule inherently more complex than the pathway for its degradation?In _____________ inhibition, the EI complex readily dissociates and the enzyme is again available for substrate binding.The active (catalytic) site of an enzyme contains the side chains of amino acid residues that areconserved because they participate in the protein’s catalytic activity. The bulk of the enzyme,however, is not part of the active site. A substantial amount of energy is required to synthesizeenzymes. Why are these molecules so large?
- Many isolated enzymes, if incubated at 37°C, will be denatured. However, if the enzymes are incubated at 37°C in the presence of substrate, the enzymes are catalytically active. Explain this apparent paradox.Enzymes act by reducing the activation energy of areaction. Describe several ways in which this isaccomplished.Enzyme Triacylglycerol Lipase Rennin Catalase Hexokinase Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly)
- When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Zymogen activation Covalent modification Competitive inhibition Allosteric activation Allosteric inhibitionIn any given enzyme, the active site is only a small portionof the entire molecule. Synthesis of such a relatively largemolecular machine requires an enormous amount of cellular energy. Explain why this inefficiency is tolerated.A sample of glycogen from a patient with liver disease is incubated with Pi, normal glycogen phosphorylase, and normal debranching enzyme. The ratio of G1P to glucose formed in the reaction mixture is 100. What is the patient’s most probable enzymatic defi ciency?
- When enzyme solutions are heated, there is a progessive loss of catalytic activty over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 degrees Celsius lost 50% of its activity in 12 minutes, but when incubated at 45 degrees Celsius in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates.the amino acid glutamic acid is at the active site of an enzyme. Normally the enzyme is active at pH 7. at pH 4 (higher concentration of H+), the enzyme is inactive. Explain there observationsWith a ∆G°´ of -16.7 kJ/mol, the reaction catalyzed by hexokinase is considered to be _____. at equilibrium substrate and product concentration dependent freely reversible metabolically irreversible none of the above