An enzyme that exhibits positive cooperativity in binding its substrate is a homotrimeric protein with C3 symmetry. If you determined the Hill coefficient for this enzyme, what range would you expect it to be, if the cooperatively is fairly high? Group of answer choices
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![An enzyme that exhibits positive
cooperativity in binding its substrate is a
homotrimeric protein with C3 symmetry. If
you determined the Hill coefficient for this
enzyme, what range would you expect it to
be, if the cooperatively is fairly high?
Group of answer choices
2.6 - 2.8
1.75 - 1.9
1-1.2
3.4 - 3.6
3.75 - 3.9](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F25388e77-5167-4e08-905a-6574eebe3f8a%2F831b4b67-fe4e-4767-b82f-21a17bcc4e68%2Faxncyg_processed.jpeg&w=3840&q=75)
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- A plot of 1½5 venut VSL, Glld a Br-weaver Burk or double-reciprocal plot, is a useful tool for identifying the type of Madily each gaph by dragging the endpoints to show the various types of enzyme inhibition. What is the inhibition mechanism for the competitive inhibitor? The inhibisr binde cenly in recemyne The inhibitor bindx only lo cozyme- substrate complexe The inhibike binds tas bath free enzyme and enzyme xubxirale completes with identical binding axolante. The inhibikr binds to both free enzyme and cozyme substrate completes with different binding constants. What is the inhibition mechaniam for the uncompetitive inhibitor? The inhibitor binds only to free ENZYMES. The inhibitor bind is both tree enzyme and enzyme auhdraic compleaca with identical binding coulants. The inhibar binds only in enzyme ubrale complex.ca. The inhibir bindis in bath free enzyme and cxyme aubairale complicaca with dill crcnt binding costanix. LAST Nompumps dve shk with inbibus WHEY Pullie mechanism kot…The equil ibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200.In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1.What is the rate constant for the loss of the unreacted substrate from the active site?Please explain how it is that you approach a problem like this. For example, how would i be able to answer it if instead of met it said Lys, but also explain how you chose the enzyme for met. Thank you, i'll give a positive rate if the taks above is done.
- The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is AOn the right the Hill plot com- (b) pares the O2 binding properties of Hb Ya- kima with those of HbA in 0.1 M NaCl buff- Hb-Yakima ered to pH 7 with 0.01 M bis-Tris. Focus first on the line for "stripped Hb". This is the term for hemoglobin isolated from erythro- cytes with removal of all organic phosphate molecules that might bind to the protein in RBCS. You can see that 2,3-bisphospho- glycerate (BPG; labeled DPG according to old terminology) does not alter the O2 bind- ing affinity of Hb Yakima in contrast to HbA (although it was shown that BPG did bind to the deoxyHb Yakima molecule). Also, Hb Yakima is associated with markedly decreased allostery in the absence and presence of BPG, in comparison to HbA. IHP = inositol hexaphosphate, an artificial allosteric modifying ligand that binds more tightly than BPG. stripped Hb Hb-A •DPG +DPG n= 1.0 n = 2.3 n=2,5 +THP +IHP 0.5 0.5 1 5 10 50 po, ( mm Hg ) %3D On the right is a diagram copied from the lecture handout "Hemoglobin and Allo-…-Inhibitor +Inhibitor [S] (mM) V0&νβσπ; (μmol/sec). V0&νβσπ:&νβ σπ: (μmollsec) 0.0001 33 17 0.0005 71 50 0.001 83 67 0.005 96 91 0.01 98 95 What is the Km of this enzyme WITH iinhibitor?
- An enzymatic reaction with KM = 4.4 x 10-5 M, is carried out in 400 μL of of solution containing 0.20 nmoles of enzyme. It is observed that Vmax = 6.6 x 10-3 M/s. What is the kcat value for the enzyme? (HINT: Keep an eye on the units)!!! a. 1.50 x 102 s-1 b. 7.56 x 10-5 min-1 c. 1.32 x 104 s-1 d. 3.3 x 106 s-11. - - Substrate Enzyme - 1 2 3 BOO - Look at the above diagram and understand what is being shown. Explain AND draw a graph depicting how the rate of the reaction depicted here is changing. ☐ L 2. How will the rate of the reaction change with time after 3? How can we increase the rate of the reaction after 3? I 100 B LDetermine how reaction rate (velocity) varies with substrate concentration. F3 $ 4 Substrate concentration R F Additional substrate is added when substrate concentration is low. F4 % 5 T Rate increases G 6 HOLL F5 & H 7 F6 YU J *00 8 DELL F7 K ( 9 Substrate is added when enzyme is saturated with substrate. F8 Rate decreases O Answer Bank F9 P W F10 { [ + 11 F11 } 1 F12 Additional substrate is added when substrate concentration is high but is not yet saturating. Backspace Rate is unchanged Enter Insert Print Screen Delete Home Scroll Lock End 8:26 PM 2 10/15/2023 + PgUp Pause Break PgDn
- Consider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?Explain the mechanism by whicha single substrate reaction catalyzed by an enzyme with a single binding site for the substrate is able to exhibit sigmoidal kinetics.You wish to separate and purify enzyme A from contaminating enzymes B and C. Enzyme A is found in the matrix of the mitochondria. Enzyme B is embedded in the mitochondrial membrane, and enzyme C is found in the peroxisome. Enzymes A and B have molecular weights of 60,000 Da. Enzyme C has a molecular weight of 100,000 Da. Enzyme A has a pI of 6.5. Enzymes B and C have pI values of 7.5. Design an experiment to separate enzyme A from the other two enzymes.
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