Discuss the role of feedback inhibition in the anabolism ofpurine-containing nucleotides.
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Q: Discuss the mechanism of action of the enzyme chymotrypsin.
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Q: Radioactive uracil can be used to label all of the pyrimidine residues in DNA. Using either names or…
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Discuss the role of feedback inhibition in the anabolism of
purine-containing
Step by step
Solved in 2 steps
- Explain why methotrexate inhibits the synthesis of histidine and methionine.Discuss the degradation of sphingolipidsRadioactive uracil can be used to label all of the pyrimidine residues in DNA. Using either names or structures, present pathways for con- version of uracil to dTTP and to dCTP. For each reaction, show the involvement of cofactors, and identify sites of allosteric regulation.
- Define aminoacyl (A) siteSome of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.Describe how the concentrations of the four deoxyribonucleotides are balanced by ribonucleotide reductase.
- Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, IIIProvide a simple sketch of the covalent intermediate likely to form between active site serine residue and diphenylcarbamyl chloride. Is DPCC more likely to covalently bind to serine, aspartate, or histidine?Proteases are enzymes that cleave peptide bonds using general acid–base catalysis. General acid–base catalysis relies on a proton donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin’s active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding.
- Which of the following statements are descriptions of metal ion catalysis or examples of metal ion catalysis? Choose all correct answers a Zn²+ cofactor may properly orient the substrate in the active site through ionic interactions. a covalent bond forms between enzyme and substrate lowers the energy or stabilizes the transition state or intermediate catalyst retains its original form after reaction occurs catalysts may participate in oxidation-reduction reactions by changes in the oxidation stateUnbranched homopolymer of N-acetyl glucosamine is : 1.Cellulose 2.Chitin 3.Curcumin 4.Concanavalin ADetermine the amino acid sequence of Peptide A, which was obtained by hydrolyzing a larger peptide with trypsin, using the data below: Total hydrolysis of Peptide A produces (Ala2, Arg, Glu, Gly, Met, Pro2, Ser, Tyr). Sequential Edman degradation of Peptide A produces a derivative of Ala in the first cycle; a derivative of Serine in the second cycle; and a derivative of Proline in the third cycle. Cleavage of Peptide A with chymotrypsin yields two peptides: a tripeptide III containing Ala, Arg and Gly; and a heptapeptide IV containing Ala, Glu, Met, Pro2, Ser and Tyr. Edman treatment of tripeptide III generated a derivative of Alanine. Cleavage of Peptide A with cyanogen bromide (which cleaves peptides on the C-terminal side of Methionine) yields two pentapeptides labeled I and II. Total hydrolysis or peptide I indicate that it contains Ala, Arg, Gly, Pro and Tyr; pentapeptide II contains Ala, Glu, Met, Pro, and Ser.