Please answer it 4. Enzyme regulation. Aspartate transcarbamoylase (ATCase) is the first enzyme in the metabolic pathwayfor pyrimidine biosynthesis. Explain how allostery regulates ATCase through conformational switchesbetween T and R states. Describe the subunit composition of ATCase. What stabilizes each conformationalstate? [200 words or less.]

The enzymes are important in metabolism and biosynthesis. Every metabolic pathway requires enzymes…

Answered: 4. Enzyme regulation. Aspartate…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 12P

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IX. Insulin, a hormone vital in blood sugar regulation and having a polypeptide chain with disulfide linkages, loses its regulatory activity when heated at nearly 100°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of insulin relative to its native structure and function. I--
.Intramitochondrial ATP concentrations are about 5 mM, and phosphate con- centration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
Need help, please. Not too sure why my answer is incorrect. Please show all steps/work.
a. Protein X can be phosphorylated. Why would the phosphorylated form of protein X elute AFTER the unphosphorylated form from an ANION exchange column? Please describe in terms of: The chemical properties of phosphorylation modification b. The chemical properties of an anion exchange column and how it works c. Why is an inhibitor that mimics the transition state more effective at enzyme inhibition than an inhibitor that mimics the substrate? d. Protein X can be covalently modified with many methyl groups. What two general properties would be different between the unmethylated protein versus the methylated protein?
protease mechanism: you isolate a new protease which cleaves the peptide bond 2 aa residues before a F residue. You might expect to fınd... O An I residue in the S2'pocket AL residue in the S2 pocket O aV residue in the oxyanion hole An Lresidue in the catalytic triad in Michaelis-Menton kinetics, cutting the enzyme concentration in half will O will double the reaction rate O will not change Vo and Vmax will change Vo but not turnover number decrease Km by half
Amino acid alanine
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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.
Not hand written please.
Activity (% Max.) Using your knowledge of aspartyl proteases, develop a plausible explanation for why protein activity changes when pH is increased or decreased from pH 4, as shown in the graph. 06 08 09 10+ 4. 9. Hd Which statements are true? The protein is active when one asp residue is protonated and the other is deprotonated. O Both asp residues are protonated at more basic pH values. O Active aspartyl proteases have only one asp residue in the active site. Only one asp side chain is protonated at low pH (below pH 3.5). Both asp side chains are deprotonated at higher pH values.
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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