Just 15-3
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Just 15-3
![15-3
15-6
Can proceeed as written
Consider the reaction
Glucose-6-phosphate + H₂O
Keg = Iglucosel [P₁1
glucose-6-P₁]
Glucose + P₁
Keq at pH 8.5 and 38°C is 122. Can you determine the rate of the
reaction from this information? Why or why not?
Why is it necessary to define a modified standard state for
biochemical applications of thermodynamics?
→ If not defined it is not useful!
→ thermodynamic standard state
Usually refers to pH-0!](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F39daa170-02bb-4dcb-bc72-b495e5cddda9%2F81d82268-8726-4d26-bd49-f21d25e0ea44%2F9mko9j8_processed.jpeg&w=3840&q=75)
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Solved in 2 steps
- In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea#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)
- Gout is a medical condition usually caused by a deficiency of the salvage enzyme hypoxanthine-guanine phosphoribosyltransferase. Uric acid accumulates in the joints and causes pain, inflammation, and in advanced disease gouty tophi. Allopurinol, an inhibitor of the enzyme xanthine oxidase, is used to treat chronic gout. Explain briefly the biochemical basis for this treatment.uizzes/67365/take Based on the image below, select the correct statements. Note: There may be more than 1 correct response. I Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP > 5-Phosphoribosylamine I adenylosuccinate PRPP lyase 9 steps Adenylosuccinate AMP IMP <-- ADP - AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP - XMP ADP ATP GMP يمد XMP-glutamine amidotransferase Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. O Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels. 8 OBCAt 37 °C, the serine protease subtilisin has kcat = 50 s-1 and KM = 1.4 × 10-4 M. It is proposed that the N155 side chain contributes ahydrogen bond to the oxyanion hole of subtilisin. J. A. Wells and colleagues reported (1986, Phil. Trans. R. Soc. Lond. A 317:415–423) the following kinetic parameters for the N155T mutant of subtilisin: kcat = 0.02 s-1 and KM = 2 × 10-4 M.(a) Subtilisin is used in some laundry detergents to help remove protein-type stains. What unusual kind of stability does this suggest for subtilisin?(b) Subtilisin does have a problem in that it becomes inactivated by oxidation of a methionine close to the active site. Suggest a way to make abetter subtilisin.(c) Is the effect of the N155T mutation what you would expect for a residuethat makes up part of the oxyanion hole? How do the reported values ofkcat and KM support your answer?(d) Assuming that the T155 side chain cannot H-bond to the oxyanion intermediate, by how much (in kJ/mol) does N155 appear to stabilize…
- Enzyme hydrolysis of glucose-6-sulfate occurs in a marine microorganism. The activity test is based on the rate at which glucose is metabolized. Its KM is 6.7 x 10-9 M and its Vmax is 300 nM min-1 in cell-free extract. Galactose-6-sulfate competes with the enzyme to inhibit it. When glucose-6-sulfate and galactose-6-sulfate are present at 2 x 10-5 M, the starting speed is 1.5 nM min-1. Take a look at the Ki for galactose-6-sulfate and figure out what it is.HEPES, 4-(2-hydro)-1-piperazine ethane sulfonic acid, shown below. fully protonated, has pKa’s of 3.00 and 7.55. It is a commonly used buffer for tissue culture and organ storage during transplantation due in part to its effectiveness over a wide temperature range. One-way oxalic acid can be produced in fungi by hydrolysis of oxaloacetate, an intermediate in the Kreb’s citric acid cycle, to produce oxalic acid and acetic acid. This reaction, shown below, is catalyzed by oxaloacetase. [O2CC(O)CH2CO2] 2− + H2O → C2O44−+ CH3COO− + H+ oxaloacetate oxalic acid acetate In a 1-ml reaction mixture containing 50 mM NaCl, 50 mM HEPES, pH 7.8, 5 mM oxaloacetate and 5 pmol oxaloacetase, complete hydrolysis of the oxaloacetate was achieved in 10 minutes of incubation at 30°C. What was the pH of the reaction mixture at the end of the reaction?The rate constant for the uncatalyzed reaction of two molecules of glycine ethyl ester to form glycylglycine ethyl ester is 0.6 M- 1s - 1. In the presence ofCo2 +, the rate constant is 1.5 x 106 M- 1s - 1. What rate enhancement does the catalyst provide?
- The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.A synthetic substrate, the para-nitrophenylacetate (PNPA), is used to monitor enzyme activity of protein P. The product of the hydrolysis reaction absorbs at 410 nm with a molar extinction coefficient of 4 000 M-¹.cm-¹. 1- Write the reaction catalyzed by the protease P using the pNPA substrate. 2- The enzyme extract is too concentrated and a 1/300 dilution is needed for enzyme tests. Considering that you would need at least 600 µL of diluted enzyme extract for activity tests, indicate which volume of buffer and enzyme extract you must use for the dilution.EGTA (ethylene glycol-bis(β-amino ethyl ether)-N,N,N′,N′-tetraacetic acid) is a chelating agent with high affinity and specificity for Ca2+. By microinjecting acell with an appropriate Ca2+-EGTA solution, an experimenter can prevent cytosolic [Ca2+] from rising above 10+7 M. How would EGTA microinjection affect a cell’s response to vasopressin ? To glucagon?
