2. (: A diagram of the residues defining the binding site of 2,3-bis-phosphoglycerate (BPG) is shown on the right. Given the mutation in Hb Great Lakes, Leu(B68)His, show on either O2 binding plot whether its p(O2)50% will be altered in the presence of a 10-fold excess of BPG and in which direction with respect to that of HbA. Explain.
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- Understanding the Mechanism of Hemolytic Anemia Genetic defects in glycolytic enzymes can have serious consequences for humans For example, defects in the gene for pyruvate kinase can result in a condition known as hemolytic anemia. Consult a reference to learn about hemolytic anemia, and discuss why such genetic defects lead to this condition.Consider the synthesis and degradation of tyrosine as shown in Figures 25.37, 25.38, and 25.48 to determine where the carbon atoms in PEP and erythrose-4-P would end up in acetoacetate and fumarate.A point mutation in Hb diminishes hydrophobicity at the heme. Which of the following impacts would you predict? . Increased oxidation of Fe2+ and loss of O2 binding b. Decreased negative charges needed at the dimer/dimer interface to stabilize the T-state c. Decreased positive charges needed at the dimer/dimer interface to stabilize the T-state d. Shift the O2 binding curve of Hb to the left e. Decreased affinity for BPG in the T-state
- The mutation in hemoglobin at β82 Lys→Asp results in lowered O2-bindingaffinity compared to normal hemoglobin. β82 is one of the residues thatlines the 2,3-BPG binding site (as shown; β82 is adjacent to His 143). Based on the location of this residue and the differences between Lys and Asp, suggest a rationale for the observed reduction in O2-binding affinity.Phosphoglucokinase catalyzes the phosphorylation of the C6-OH group of G1P. Why is this enzyme important for the normal function of phosphoglucomutase?2,3-Bisphosphoglycerate lies in a central cavity within the hemoglobin tetramer, stabilizing the T state. What would be the effect of mutations that placed the BPG-binding site on the surface of hemoglobin?
- Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Construct a Lineweaver–Burk plot to answer the following questions: (a) What are the apparent KM and Vmax values in the presence and absence of the inhibitor? (b) What kind of an inhibitor is threo-sphingosine? Explain.Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Construct a Lineweaver-Burk plot to answer the following questions: (a) What are the apparent KM and Vmax values in the presence and absence of the inhibitor? (b) What kind of an inhibitor is threo-sphingosine? Explain.Lithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate. Explain this apparent paradox.
- The interconverison of DHAP and GAP greatly favors the formation of DHAP at equilibirum. Yet the conversion of DHAP by triose phosphate isomerase proceeds readily. Why?Phosphoglycerate kinase shows induced fit resulting from the binding of both substrates to form the closed catalytic conformation. Maintainence of the closed conformation depends on the formation of a salt bridge between R62 and D200. What would be the effect of the mutation of D200 to the unusual amino acid shown below? Explain.Phosphoribosyltransferase (PRT) catalyzes the attachment of a salvaged purine nitrogenous base on the activated form of ribose-5-phosphate called 5-phosphoribosyl- α α-pyrophosphate ( α α-PRPP). True Or False