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A:
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- The enzyme that catalyzes reaction below can be classified as: CoO COO NAD+ NADH + H* Но- | malate -C- H-Ć- dehydrogenase Охaloacetate Malate isomerase lyase hydrolase oxidoreductase ligase transferaseUsing 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.Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
- Trypsin uses a nearly identical mechanism as chymotrypsin (including the catalytic triad his57-ser195-asp102. beginning with the enzyme substrate complex draw the complete steps in the trypsin mechanism that occur to release the first product and create the acyl enzyme intermediate in the trypsin active site. The substrate for trypsin to be used is gly-lys-gly-alaDescribe the mechanism of a-chymotrypsin. Explain the roles of constituents of the catalytic triad, their modes of catalysis, and the significance of the oxyanion hole in the catalysis.Diagram the hydrogen-bonding interactions of the catalytic triad His–Lys–Ser during catalysis in a hypothetical hydrolytic enzyme.
- 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.The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active site that will have all H-bonding potential satisfied only during the catalytic cycle of the reaction. True or False? The catalytic triad residues are all next to each other in the primary sequence of trypsin. True or False?Because 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?
- When regulating phosphofructokinase, why is there such extensive regulation of this reaction and enzymatic reactions, in general?In serine protease catalytic triad mechanism, the first and second products that leaves the active site are Carboxylic acid and amide respectively Amide and carboxylic acid respectively Ester and amide respectively Carboxylic acid and ester respectivelyWhen 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.