The data below show the inhibition of rat liver alcohol dehydrogenase (ADH) by tetramethylene sulfoxide, a drug that is used to treat methanol poisoning. What form of ADH does tetramethylene sulfoxide bind to?8A[1] =0.6 mM0.4 mMミ。0.2 mM20.5 1.0 1.5 2.0 2.51/(ethanol), mM -1O Only to the free enzyme, E.O Only to the enzyme-substrate complex, ES.O To both E and ES, but with higher affinity for E.O To a serine residue at the enzyme active site.O To both E and ES, with equal affinity.

Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that facilitate the…

Answered: The data below show the inhibition of…

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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Figure 1 shows the catalytic triad of a-chymotrypsin. Identify A, B and C. Describe the subsequent steps of stage 1 and stage 2 of a- chymotrypsin mechanism. Illustrate with diagrams. A B CH2 H-N N: H-O Figure 1
Given the initial rate data for the reaction A + B → C, determine the rate expression for the reaction. [A], M [B], M A[C]/At (initial) M/s 0.0418 0.122 2.73 x 10-4 0.0836 0.122 10.9 × 10 4 0.0418 0.488 2.73 x 104 O A[C] At ○ A[C] ΔΙ = 0.439 Ms[A][B]² = 1.27 M²s¹ [A][B] ● A[C] = 6.53 × 10³ s¹ [A] At O A[C] = 0.156 M's¹[A]² At ○ A[C] At = 5.35 x 102 M2s[A][B]
The hexapeptide Ala-Met-Leu-Lys-Phe-Asp is digested in the same tube with both Cyanogen Bromide and Trypsin at the same time at pH=7. Draw the structure of the product(s) that would bind to a cation exchange column. (Relevant pKa values are 2.2, 3.9, 9.5 and 10.5. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.5 and 2.2 respectively)
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
can you explain what is happening in the attached graph? Figure 3: Lineweaver-Burke plot of alkaline phosphatase activity without inhibitor
Which of the following drugs is a less potent microsomal triglyceride transfer protein (MTP) inhibitor, which reduces cholesterol levels? O Structure 1 (IC50 = 23 nM) O BMS-200150 (IC50 = 2.2 µM) O Hybrid Structure (IC50 = 12 nM) %3! O Hit compound (IC50 = 36 µM) %3D Lomitapide (IC50 = 0.5 nM)
A researcher wants to look for glucaronic acid conjugated metabolites in sample of urine(glucaronic acid conjugation is a common method of metabolism for excretion.) Pronotated glucaronic acid conjugated metabolite ions often lose anhydroglucaronic acid(176 Da) during low energy CID. Which triple quadrupole experiment might be best for finding these conjugates?
Acetocholinesterase is an enzyme possessing a single active site that metabolizesacetylcholine with a turn over number of 1.4 x 10^4s-1. How many grams of acetylcholine(molecular formula C7NO2H16+) will 2.16 x 10^-6 g acetocholinesterase metabolize in 60minutes? (The enzyme’s molecular mass is 4.2 x 10^4 g/mol).
[References) The AG" for the reaction ATP + H₂O ADP + P + H+ is -30.5 kJ mol'¹, Other organophosphate species also undergo hydrolysis of the phosphate moiety via a similar reaction. Determine the value of AG for the following reactions and indicate if the reaction will proceed spontaneously in the direction written if the reactants and products are initially in a 1:1 molar ratio. a. ATP + Glucose ADP+ Glucose-1-phosphate AG⁹¹ = kJ mol-1 The reaction is (The hydrolysis reaction for glucose-1-phosphate is Glucose-1-phosphate + H₂0 Glucose + P + H+; AG-20.9 kJ mol ¹.) b. ATP + Glutamate Carbamoyl phosphate + ADP AG The reaction is kJ mol-1 (The hydrolysis reaction for carbamoyl phosphate is Carbamoyl phosphate + H₂0 Glutamate + P, + H+ ; AG¹ = -51.4 kJ mol ¹.) Submit Answer Try Another Version 3 item attempts remaining
Triosephosphate isomerase catalyzes the conversion of glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. This reaction has a Keq of 22.2. What is the standard free-energy change for this reaction? -7,680 kJ/mol -7.68 kJ/mol -3.34 kJ/mol -0.644 kJ/mol 7.68 kJ/mol
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM
If we were handed a tuke of 2mg/mL BSA how much is required 20μL of each of the following Concentrations? to make zoul total bring up to volume with dH ₂0 @ 01125 mg/mL (1) 0,150 mg Ⓒ 0.50 mg/mL @ 0.75 mg/mL Ⓒ 1.0mg/ml /ML Can it be solved using C₂ C₁V₁ = C₂ V₂ If CI= V₁ yes, please show work. Vz

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