Phosphonacetyl-L-aspartate (PALA) is a potent inhibitor of aspartate transcarbamoylase because it mimics the two physiological substrates of the enzyme. However, in the presence of substrates, low concentrations of PALA increase the reaction rate of aspartate transcarbamoylase. Explain this result.
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Phosphonacetyl-L-aspartate (PALA) is a potent inhibitor of aspartate transcarbamoylase because it
mimics the two physiological substrates of the enzyme. However, in the presence of substrates, low
concentrations of PALA increase the reaction rate of aspartate transcarbamoylase. Explain this result.
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- Using 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.Fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. The mammalian enzyme is tetrameric, negatively regulated by both Fructose 2,6-bisphosphate and AMP. Propose three (3) distinct models for how these molecules regulate FBPase activity. Also, describe how the enzyme might differentiate between Fructose 1,6 bisphosphate and Fructose 2,6-bisphosphate binding to the allosteric site on the enzyme with particular emphasis on amino acids comprising the allosteric binding site(s).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?
- The sedimentation value of aspartate transcarbamoylase decreases when the enzyme switches to the R state. On the basis of the allosteric properties of the enzyme, explain why the sedimentation value decreases.The enzyme aspartate transcarbamoylase catalyzes an early step in pyrimidine biosynthesis. The two states of the multi-subunit enzyme are shown below. Note that the binding of the regulatory molecule CTP (cytosine triphosphate) causes the enzyme complex to be inactive. Is this situation an example of positive or negative regulation? Explain why the use of CTP as the regulatory molecule is logical givén the overall function of this particular enzyme. INACTIVE ENZYME: T STATE catalytic subunits regulatory subunits OFF 6 CTP ON ACTIVE ENZYME: R STATEThe mechanism of chymotrypsin can be viewed as a two-step process, acylation of the enzyme active site followed by a deacylation reaction. What accounts for the observed "burst" in rapid kinetic studies of the hydrolysis of N-acetyl-L-phenylalanine p-nitrophenyl ester by chymotrypsin? The rate of hydrolysis of the acyl-enzyme intermediate is faster than the rate of forming the acyl-enzyme intermediate. The rates of the acylation and deacylation reactions are equal. The rate of the acylation reaction is slower than the rate of the deacylation reaction. The rate of the acylation reaction is faster than the rate of the deacylation reaction.
- When the identical subunits of chicken liver fatty acid synthase are dissociated in vitro, all of the activities can be detected in the separated subunits except for the β-ketoacyl synthase reaction and the overall synthesis of palmitate. Explain these observations.UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?Aspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the human body. In the below graph, which line represents the rate of the reaction catalyzes by Aspartate transcarbamoylase? Explain.
- Glyphosate, which inhibits the EPSP synthase reaction of the shikimic acid pathway, is a phosphonic acid derivative of glycine; hence its name (glycine phosphonate). Based upon your knowledge of the EPSP synthase reaction (see pages 908–909), would you expect the inhibition to be competitive or noncompetitive with respect to each of the substrates? Briefly explain your answer.The KMof the enzyme for the substrate adenosine is 3 × 10ꟷ5M. The product inosine acts as an inhibitor of the reaction, with an inhibition constant (KI, the dissociation constant for enzyme-inhibitor binding) of 3 × 10ꟷ4M. However, a transition state analog,Inhibits the reaction with KIof 1.5 × 10ꟷ13M. Explain why 1,6-dihydroinosine serves as a better inhibitor of adenosine deaminase than inosine. Elaborate on your answeIn this experiment, thearubigins were studied for their ability to inhibit the activity of amylase. a. How could you experimentally determine the inhibitor constant, K, of thearubigins? b. What are the potential health benefits of this inhibition?