A diagram of the residues defining the binding site of 2,3-bis-phosphoglycerate (BPG) is2. (shown on the right. Given the mutation in Hb Great Lakes, Leu(B68)His, show on either O2 binding plotwhether its p(O2)50% will be altered in the presence of a 10-fold excess of BPG and in which directionwith respect to that of HbA. Explain.B1B1-subunitHis 143Lys82His 2BPGa-NH,*a-NH,*B2-subunitLys 82His 2His 143B2

2,3 bis phosphoglycerate (BPG) is an allosteric regulator of Hb. BPG binds to central cavity of…

Answered: 2. (: A diagram of the residues…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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8. In a patient with anemia, the presence of Heinz bodics in the RBCS was the result of the hemoglobin subunits aggregation due to the oxidation of -SH groups of Hb cysteine residues with active oxygen forms and the formation of disulfide bonds. What metabolic disorders in the RBC can be the cause of this clinical case? To solve the problem: a) indicate which reactions maintain cysteine residues in a reduced state; b) name the coenzyme involved in this process, write a diagram of the process in which the reduced form of this coenzyme is formed; c) indicate the enzyme which deficiency may lcad to a lack of the reduced cocnzyme and be the cause of the clinical case described above.
6. A. List all of the ionizable functional groups that are found in insulin when in aqueous solution. List which amino acid residues have these ionizable groups and list all of the pka and pKb values (including the R groups) that are on both polypeptide chains that make up insulin. (see the table at the end of this HW set; note that tyrosine and cysteine both have unusual pka's, since these side groups ionize above the pKR's given to have a negative charge). B. The isoelectric point of insulin is reported to be around 5.3-5.35. Using the method covered in class, estimate the isoelectric point of insulin and compare your answer to the values above. C. For a polypeptide to be soluble in an aqueous solution, is it good to be near the isoelectric point? Why or why not? Notes: a couple of unusual R group's that ionize (cysteine and tyrosine have R groups that have pka values; histidine has a pkb). The table at the end of this homework set (also in the lecture notes) lists the pka's and…
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. 5.1. The outer layer of the placenta expresses an enzyme that facilitates production of 2,3- bisphosphoglycerate (BPG). Explain-with biochemical detail-how this impacts the ability of the fetus to get oxygen. 5.2. You measure the reaction velocity for converting your favorite substrate (YFS)to product by your favorite enzyme (YFE) over a range of substrate concentrations. The relationship is sigmoidal. Based on this information alone, what do you know about YFE? 5.3 Is the transformation shown below possible. If so, draw a reasonable electron pushing mechanism showing each step and any intermediates. *-4 HO + CO₂
PTP1B Substrate kcat Km kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEPYLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 ± 0.22 0.53 + 0.02 34.7 + 0.25 52.7 ± 0.7 0.066 + 0.001 (d) (. ) The units for kcat/KM in the above are given according to standard scientific notation. On this basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?
PLP can catalyze both \alpha, \beta elimination reactions and \beta, \gamma - elimination reactions. Propose a mechanism for the following PLP - catalyzed \beta, \gamma elimination
3. Aspartate aminotransferase (AspAT) catalyzes the following reaction: COO™ C=O CH₂ COO Oxaloacetate The AspAT enzyme has two active-site arginines, Arg 386 and Arg 292, that interact with the a- carboxylate and ß-carboxylate groups on the aspartate substrate, respectively. Investigators stud- ied the mechanism of AspAT in more detail by constructing mutant AspAT enzymes in which either or both of the essential arginines were replaced with a lysine residue. The kinetic parame- ters for the wild-type enzyme and nutant enzymes are shown in the table. NH—CH-COO T CH₂ COO™ Aspartate α-Amino acid Enzyme 1. Wild-type Asp AT(Arg 292 Arg 386) 2. Mutant Asp AT(Lys 292 Arg 386) 3. Mutant Asp AT(Arg 292 Lys 386) 4. Mutant Asp AT(Lys 292 Lys 386) Asp-AT a-Keto acid KM (MM) 4 326 72 300 Kcat (S-1) 530 4.5 9.6 0.055 (a) The Michaelis constant is strictly not equivalent to an equilibrium binding constant; however under certain conditions the Michaelis constant does approach the equilibrium (dissoci-…
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.
1. Acid phosphatases are an important group of enzymes that can be detected in human bloodserum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyzebiological phosphate esters as follows:R-O-P-O3-2 + H 2O R-OH + HO-P-O3-2.Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver,and prostrate gland. The enzyme from the prostrate gland is clinically important because anincreased activity in the blood is frequently an indication of cancer of the prostrate gland.Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acidphosphatases from other tissues. How can you use the information above to develop a specificprocedure for measuring the activity of the acid phosphatase of the prostrate gland in humanblood serum?
. The mutation in hemoglobin at B82 Lys → Asp results in lowered O2-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site. A rationale for the observed reduction in O2-binding affinity is: A. The positive charge on the Asp side chain can form salt bridges with other negative charged side chains stabilizing R-conformer. B. The negative charge on the Asp side chain can form salt bridges with other positive charged side chains stabilizing the T-conformer. C. The Asp side chain mimics the positive charge on BPG. D. The Asp side chain mimics the negative charge on BPG. E. The Asp side chain is a nucleophile that attacks the BPG. F. BPG attacks the Asp side chain. G. Stabilization of the R-conformer favors O, release. H. Stabilization of the T-conformer favors O, release.
VDAC1 mitochondrial protein plays an important role in human diseases and many strategies can be taken to utilize the therapeutic potential of VDAC1. what are these diseases and strategies?
1. The second high energy intermediate metabolite of glycolysis that can be used for substrate level phosphorylation is also a precursor molecule for the synthesis of several amino acids. Name 5 of these amino acids. 2. Explain the indirect effect that allosteric effectors have on pyruvate dehydrogenase activity through phosphorylation/dephosphorylation of components within the PDH-complex.

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