Outline the role of amino acids as precursors of other nitrogen-containing compounds in the cell, using either the purine or pyrimidine biosynthesis pathway as an example.
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Outline the role of amino acids as precursors of other nitrogen-containing compounds
in the cell, using either the purine or pyrimidine biosynthesis pathway as an example.
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- Explain the role that Gla residues play in complexes. Explain the role of vitamin K / warfarins in the synthesis of protease factors and list the Vitamin K-dependent factorsCompare the pathways of purine and pyrimidine nucleotide synthesis with respect to (a) precursors, (b) energy cost, (c) acquisition of the ribose moiety, and (d) number of enzymatic steps.Discuss the role of feedback inhibition in the anabolism ofpurine-containing nucleotides.
- Please describe four different modes of the regulation of the pentose phosphate pathway.The pathway shown below is used by a fungus to create Fructose-1,6-diphosphate from glucose. A silent mutation occurs in the gene that encodes enzyme 3. This fungus is grown on media that only contains the precursor. Discuss the effects of this mutation on: (i) The function of Enzyme 3 (ií) The production of Fructose-1,6-diphosphate Enzyme 1 Glucose-6- Enzyme 2 fructose-6- Enzyme 3 Fructose-1,6- Glucose phosphate phosphate diphosphatecreate a detailed flow chart or diagram to illustrate all possible fates of amino acid degradation products. What will happen to the carbon portion and nitrogen portion of the amino acid? Give specific examples if possible.
- Describe which enzymes are required for lactose and tryptophan metabolism in bacteria when lactose and tryptophan, respectively, are (a) present and (b) absent.Which of the 20 amino acids can be synthesized directly from a common metabolic intermediate by a transamination reaction?Determine 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.