Its 3. Aspartate transcarbamoylase (ATCase) catalyzes the reaction: carbamoylphosphate + aspartate carbamoylaspartate and phosphate. The charge of carbamoylaspartate is activity is allosterically regulated by CTP and ATP. ATCase has six catalytic subunits and six regulatory subunits. CTP is an allosteric inhibitor and also a possible inhibitor. a) -1; noncompetitive b)-1; uncompetitive c) -2; noncompetitive d) -2; uncompetitive
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- The enzyme mutase which is important for the synthetic of tyrosine and phenylalanine in saccharomyces cerevisiae has been studied as an example of an allosteric enzyme. Tyrosine acts as a negative effector for this enzyme. What effects would you see on the action of the enzyme were you to increase the concentration of tyrosine? The chorismate mutase would shift to its R conformation The curve showing the kinetics or chorismate mutase would shift to the right The curve showing the kinetics of chorismate mutase would shift to the left The chorismate mutase would become saturated more rapidlyTrypsin 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-ala4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.
- UDP-glucose pyrophosphorylase catalyzes the removal of a pyrophosphate group from UTP as it synthesizes UDP-glucose. Why is this necessary, from a biochemical perspective? Both of the phosphate groups from UTP are needed to form UDP-glucose. There is no particular reason: wasteful reactions just happen sometimes. The pyrophosphate (after hydrolysis) is required to free up more phosphate for the synthesis of ATP by oxidative phosphorylation. The subsequent hydrolysis of pyrophosphate is a highly exergonic reaction, which pulls the equilibrium over towards UDP-glucose. Pyrophosphate is an allosteric activator of glycogen synthase, so this helps glycogen synthesis to proceed at a faster rate.Explain the basis for the following statement. For efficient conver- sion of galactose to glucose-1-phosphate, UDP-glucose need be present in catalytic amounts only.ATCase catalyzes the conversion of carbamoyl phosphate and aspartate into N-carbamoylaspartate, a precursor in pyrimidine biosynthesis. What roles do ATP and CTP play in this reaction? uncompetitive inhibitors heterotropic modulators homotropic modulators mixed inhibitors
- 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 answeAspartate 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.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?
- #1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)2A. Red blood cells synthesize and degrade 2,3-bisphosphoglycerate (2,3-BPG) by a detour of the glycolytic pathway, as shown below: glyeeraldehyde 3-phosphate GAP dehydrogenase 1,3-bisphosphoglycerate bisphosphoglycerate mutase ADP phosphoglycerate kinase 2,3-bisphosphoglycerate ATP 3-phosphoglycerate 2,3-bisphosphoglycerate phosphatase phosphoglycerate mutase 2-phosphoglycerate (i) The bisphosphoglycerate mutase/2,3-bisphosphoglcerate phosphatase reaction is catalyzed by a single enzyme, BPGM. At alkaline pH, BPGM favors the mutase activity while at lower pH, BPGM favors the phosphatase reaction. Use this information, along with the Bohr effect, to explain in the space below how red blood cells respond to a metabolic defect where a patient experiences chronic, elevated levels of lactic acid. I (ii) Individuals with red blood cell phosphoglycerate kinase deficiency suffer from moderate hemolytic anemia (a condition where red blood cells self-destruct before their normal lifespan). They…5. Protein tyrosine phosphatase-1B (PTP1B) is an important enzyme regulating insulin signaling be- cause it catalyzes the hydrolysis of phosphorylated tyrosine residues on the insulin receptor and on insulin receptor substrates, proteins of approximately 200,000 molecular weight that serve as cell sig- naling intermediates. The reaction has been shown to adhere to the following mechanism in the scheme below: k3 E-P 2- E + AROPO, НОРО,* 2- E • AROPO, ArОH where ArOPO32- represents the phosphorylated aromatic group. (a) (. ) With p-nitrophenyl-phosphate (PNPP), a syn- thetic organic substrate under conditions [So] >> Eo], the traces illustrated in the diagram to the right were obtained whereby the optical density at 410 nm monitors the release of the p-nitrophenolate anion (see reaction scheme above) upon cleavage of the ArOPO32- substrate. What is this phe- nomenon called? What information does this observation 0.14 0.12 [PTP1]=0.054 mM 0.1 0.08 0.06 [PTP1]=0.027 mM 0.04 provide about…