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- 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?16. The overall reaction for the glycolysis reaction is C6H₁2O6(aq) + 2NAD+ (aq) + 2ADP³(aq) + 2HPO(aq) + 2H₂O(1) 2CH3COCO₂ (aq) + 2NADH(aq) + 2ATP4 (aq) + 2H3O+ (aq). What is A,G at chemical equilibrium?4. 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.
- 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…2. The precise biochemical mechanisms underlying the rapid shutdown of glycolysis in skeletal muscle upon termination of muscle contraction have remained poorly understood for many decades. It is known that glycolytic flux declines after exercise even though Pi, ADP, and AMP remain high; however, while these adenosine-5'- nucleotides are allosteric activators of phosphofructokinase-1 (PFK-1), this enzyme remains of low ac- tivity despite their presence. The diagrams (A and B) on the right illustrate the increase in the concentrations of glycolytic in- termediates downstream of PFK-1 during exercise for 60 sec followed by the abrupt decline in their concentrations upon ces- sation of muscle contraction. Diagram C shows changes in the concentrations of phosphate metabolites pre- and post-exer- cise. A. Summed concentration of glycolytic intermediates down- stream of PFK-1 (F1,6P2 + DHAP + G3P + GAP + 1,3BPG + 3PG + 2PG + PEP; G3P, glycerol-3-phosphate). B: PFK-1 flux (grey) and the PGK +…2. The precise biochemical mechanisms underlying the rapid shutdown of glycolysis in skeletal muscle upon termination of muscle contraction have remained poorly understood for many decades. It is known that glycolytic flux declines after exercise even though Pi, ADP, and AMP remain high; however, while these adenosine-5'- nucleotides are allosteric activators of phosphofructokinase-1 (PFK-1), this enzyme remains of low ac- tivity despite their presence. The diagrams (A and B) on the right illustrate the increase in the concentrations of glycolytic in- termediates downstream of PFK-1 during exercise for 60 sec followed by the abrupt decline in their concentrations upon ces- sation of muscle contraction. Diagram C shows changes in the concentrations of phosphate metabolites pre- and post-exer- cise. A. Summed concentration of glycolytic intermediates down- stream of PFK-1 (F1,6P2 + DHAP + G3P + GAP + 1,3BPG + 3PG + 2PG + PEP; G3P, glycerol-3-phosphate). B: PFK-1 flux (grey) and the PGK +…
- 3. Acetylcholinesterase is a serine hydrolase enzyme im- portant in nerve signal transmission, hydrolyzing acetylcho- line, an ester molecule with a positively charged quaternary nitrogen group. The structure of the physiologically relevant substrate of this enzyme is shown on the right. The quater- H₂C nary nitrogen group serves to anchor the molecule in the active site Gly121 Oxy- anion hole Gly122 Ala204 Substrate ACh His447 Catalytic triad Ser203 Glu202 Glu334 Ser229 CH3 N+ CH3 CH3 The a Scale document down rine protease family, consisting of a catalytic triad Ser203- His447-Glu334 with Ser203 supplying the nucleophilic hydroxyl group and an oxyanion hole com- prised of peptide NH groups of Gly121, Gly122, and Ala204, illustrated in the diagram above, for which carbon (green), nitrogen (blue), and oxygen (red) atoms are shown while hydrogen atoms are white. The enzyme catalyzed reaction can be represented by the following scheme: (a)( k1 K2 E + S = ES K-1 K3 EYE + P where ES…6F. What conformational state is stabilized by y in ATP synthase? Why might achieving this state require energy input from the PMF?IX. Insulin, a hormone vital in blood sugar regulation and having a polypeptide chain with disulfide linkages, loses its regulatory activity when heated at nearly 100°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of insulin relative to its native structure and function. I--
- 25. Overall oxidation of glucose can be represented as (2 Points) Glucose + 2ADP + 2GDP + 4 Pi +8NAD+ + 2FAD + 2H2O-----> 6CO2 + 2ATP + 2GTP +8NADH + 6H+ + 2FADH2 Glucose + 4ADP + 2GDP + 4 Pi +8NAP+ + 2FAD + 2H2O-----> 6CO2 + 2ATP +2GTP +8NADH + 6H+ + 2FADH2 Glucose + 2ADP + 2GDP + 4 Pi +8NADP+ + 2FAD + 2H2O-----> 2CO2 + 2ATP + 2GTP +8NADHP + 6H+ + 2FADH2 Glucose + 2ADP + 2GDP + 2 Pi +6NAD+ + 2FAD + 2H2O-----> 6CO2 + 2ATP + 2GTP +6NADH + 6H+ + 2FADH2.Intramitochondrial ATP concentrations are about 5 mM, and phosphate con- centration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP](d) of glucose oxidation in diabetic human patients treated with Metformin (●) and in (nondiabetic) control human patients (0). At –150 min both groups of subjects were started on an intravenous feed of 3-(®H)-glucose, and at t = 0 min they were started on an oral glucose tolerance test whereby a measured amount of glucose in water (a syrupy mixture) was swallowed followed by measure- ment of blood glucose levels at 30 min intervals. The flux of glucose oxidation was measured by the appear- ance of 3H2O in the blood stream. While the information The diagram to the right compares the rate 8000 ORAL GLUCOSE 6000- 4000- 2000- -120 -60 60 120 180 240 300 Minutes cannot be directly extracted from the reaction mecha- nism diagrams in the textbook, the glycolytic step in which the tritium is first released into water is that catalyzed by TPI, as illustrated at the beginning of Question #3. Explain why this step is suitable for measuring the flux of glycolysis through the release of °H…
