Chemical labeling of chymotrypsin by the compound tosylphenylalanine chloromethyl ketone (TPCK) modifies the His 57 in the enzyme's active site. The structure of this derivative is shown below. TPCK inactivates the enzyme because the bulky addition prevents it from cleaving nearby covalent bonds. HCI + CH, C-O Chymotrypsin-His 57 TPCK Modified enzyme True O False
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- An inhibitor that specifically labels chymotrypsin at histidine 57 is Ntosylamido-l-phenylethyl chloromethyl ketone. How would you modify the structure of this inhibitor to label the active site of trypsin?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.An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-l-phenylethyl chloromethylketone. How would you modify the structure of this inhibitor tolabel the active site of trypsin?
- The mechanism of chymotrypsin can be viewed as a two-step process, acylation of the enzyme active site followed by a deacylation reaction. What accounts for the observed "burst" in rapid kinetic studies of the hydrolysis of N-acetyl-L-phenylalanine p-nitrophenyl ester by chymotrypsin? The rate of hydrolysis of the acyl-enzyme intermediate is faster than the rate of forming the acyl-enzyme intermediate. The rates of the acylation and deacylation reactions are equal. The rate of the acylation reaction is slower than the rate of the deacylation reaction. The rate of the acylation reaction is faster than the rate of the deacylation reaction.a What would be the appropriate name for an enzyme that catalyzes each of the following reactions: b H3C iOH OH NH₂ alanine ligase alanine oxidoreductase alanine isomerase alanine transferase OH H3C CH3 H3C NO₂ propanone transferase propan-2-ol hydrolase propan-2-ol oxidoreductase propan-2-ol isomerase OH H3C CH3Triose phosphate isomerase In a key reaction of glycolysis, dihydroxyacetone phosphate (DHAP) is isomerized into glyceraldehyde 3-phosphate (G3P) by the action of the enzyme triose phosphate isomerase: CH₂OH C=O CH₂OPO3²- DHAP CHO HC-OH CH₂OPO3²- G3P AG°¹ +7.5 kJ/mol Because AG is positive, the equilibrium lies to the left. (a) Calculate the equilibrium constant for this reaction, assuming a temperature of 37 °C. (b) In the cell, depletion of G3P makes the reaction proceed. What is the value of AG if the concentration of G3P is kept at 1/100 of the value of the concentration of DHAP? C ZOOM +
- The visible spectrum of B-carotene (C40oHs, MW 536.89, the orange pigment in carrots) dissolved in hexane shows intense absorption maxima at 463 nm and 494 nm, both in the blue-green region. Because light of these wavelengths is absorbed by B-carotene, we perceive the color of this compound as that of the complement to blue-green, namely red-orange. B-Carotene Amax 463 nm (log e 5.10); 494 nm (log e 4.77) Calculate the concentration in milligrams per milliliter of B-carotene that gives an absorbance of 1.8 at 463 nm.Lithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate.Explain this apparent paradox.The substitution of His 64 of carbonic anhydrase II with Ala results in a sharp decrease in the activity of the enzyme in HEPES buffer (molecular weight of HEPES = 238.3 g/mol). However, increasing concentrations of imidazole (molecular weight = 68.1 g/mol) restores the reaction rate close to that of the wild-type enzyme. Propose an explanation for these results.
- The sedimentation value of aspartate transcarbamoylase decreases when the enzyme switches to the R state. On the basis of the allosteric properties of the enzyme, explain why the sedimentation value decreases.H. OH co co2 но H co, 1-isopropylmalate 2-isopropylmalate Biosynthesis of leucine involves conversion of 1-isopropyimalate to 2-isopropylmalate (see above). This proceeds in four steps under basic enzymic catalysis via an isolable compound produced in step 2. Write a detailed mechanism for this conversion. Then, draw the intermediate compound) produced in step 2. • You do not have to consider stereochemistry. • Draw uninvolved carboxyl groups in the anionic state, and enolates as carbanions. When needed, abbreviate CoenzymeA-S- as CH3S- In your drawing. aaleThe nitrogenase complex can reduce molecules other than N2. Provide the structures for the products for each of the following substrates (real and hypothetical) that contain triple bonds: hydrogen cyanide, dinitrogen, and acetylene.