Explain how the position in the active site and function of the oxyanion hole of chymotrypsin supports the theory that enzymes preferentially bind the transition state of the reactions they catalyze
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Explain how the position in the active site and function of the oxyanion hole of chymotrypsin supports the theory that enzymes preferentially bind the transition state of the reactions they catalyze
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- Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)Phosphonacetyl-L-aspartate (PALA) is a potent inhibitor of aspartate transcarbamoylase because itmimics the two physiological substrates of the enzyme. However, in the presence of substrates, lowconcentrations of PALA increase the reaction rate of aspartate transcarbamoylase. Explain this result.Explain the basis for the following statement: As a coenzyme, pyridoxal phosphate is covalently bound to enzymes with which it functions; yet during catalysis the coenzyme is not covalently bound.
- Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that some references may not break out each of these steps individually, but all steps should be ordered. There will be eight steps.ATP is a (+) allosteric effector, and CTP is a (-) allosteric effector of theenzyme ATCase. Both of these heterotropic effectors bind to the regulatorysubunits on ATCase. The substrates of ATCase, aspartate and carbamoylphosphate, bind the enzyme active site with positive cooperativity (i.e.,they exert a “+” homotropic effect on activity). As the concentrations ofthe substrates change from values where [S] ≪ KM to values where [S] issaturating ([S]≫ KM), how will the binding constants for each of the twoallosteric effectors change? In other words, does ATP bind ATCase withhigher affinity when [S] is low or high? Does CTP bind ATCase with higheraffinity when [S] is low or high?One mechanism by which lead exerts its poisonous effect on enzymes can be stopped by chelation therapy with EDTA. Describe this type of lead poisoning and explain why it is reversible.
- A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates. It is impossible for this result to be true. OA. Adding the substrate increases the weak forces that stabilize the enzyme. OB. The high concentration of substrate forms a barrier around the hexokinase. D. Adding the substrate results in protective covalent bonding.There is another class of aldolase enzymes known as Class II. These enzymes are found in fungi, algae, and some bacteria. This class differs for Class I in that these enzymes do not have a Lys residue associated with their active sites, but contain a divalent cation (usually Zn2+ or Fe2+) in the active site. Outline a possible mechanism for a Class II aldolase and explain the function of the metal ion in the reaction.An example of an enzyme-catalyzed reaction proceeding via a transition-state stabilization mechanism is the hydrolysis of peptides by chymotrypsin while, Lysozyme is often cited as an example of an enzyme which operates by strain mechanism. Discuss both mechanisms in the context of each enzyme.
- When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates.When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 450C lost 50% of its activity in 12 minutes, but when incubated at 450C 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 substratesIn the liver, fructose can be converted into glyceraldehyde 3- phosphate and dihydroxyacetone phosphate without passing through the phosphofructokinase-regulated reaction. Show the reactions that make this conversion possible. Why might ingesting high levels of fructose have deleterious physiological effects?