D Threonine 6. You have identified some intermediates in threonine synthesis: A, B, C, D and E. You grow a few of your mutants in the presence of these different intermediates to determine the order in which the gene products act. Below are your results. A (+) means growth and a (-) means no growth. Given these data, draw the best possible pathway for the synthesis of threonine. The diagram should use arrows to indicate one intermediate being changed to another intermediate. Indicate which gene produces the product responsible for the conversion by listing the mutant in that gene above the arrow. Mtl Mt2 Mt4 Mt7
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- Serine protease enzyme mutation To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic Please answer completely will give rating surelybiosynthesis of Thymidine monophosphate from ATP, HCO3-, Gln, Asp, quinone, and methylene THF. Show your work and don’t forget that the conversion of U to T only happens AFTER Ribonucleotide Reductase processes the 2’, 3’ ribose to the 3’ deoxy riboseEnzyme: Crystal Structure of Wild-Type Human Phosphoglucomutase-1 (PGM1) the description of the mechanism of how this enzyme is regulated (e.g., depending on the enzyme, the mechanism could range from being solely dependent on gene regulation to protein structure-based mechanism).
- Reposting - What would the tertiary structure of the dipeptide Asp-Ser be if it was made into a polypeptide chain? (Would it form a beta pleated sheet, an alpha helix, etc) Why would it do this? What properties of this polypeptide causes this? This sub part still needs to be solved - What would the tertiary structure of Pro-ala and Glycl-L-alanine be?Molecular detail of spike Y453FMutation identity- GLY Outline the effects the mutation of cysteine with GLY on the 3D structure and function of the 3GRS glucathione reducatse protein.
- 38. Glycogen isolation 1. The liver is a major storage site for glycogen. Purified from two samples of human liver, glycogen was either treated or not treated with a -amylase and subsequently analyzed by SDS-PAGE and western blotting with the use of antibodies to glycogenin. The results are presented in the adjoining illustration on the next page. (a) Why are no proteins visible in the lanes without amylase treatment? (b) What is the effect of treating the samples with a - amylase? Explain the results. (c) List other proteins that you might expect to be associated with glycogen. Why are other proteins not visible?Anabolism & Catabolism of Nitrogenous Bases. a. Differentiate the processes of purine nucleotide biosynthesis & pyrimidine nucleotide biosynthesis. What are the starting materials for each process? b. Differentiate the processes of purine nucleotide degradation &pyrimidine nucleotide degradation. What are the end products of each process? c. Explain how purine & pyrimidine biosynthesis is regulated to produce balanced levels ofall four nucleotides (ATP, GTP, UTP & CTP)?Protein: QQICIMFELTQISS Predict the products of the following reactions with the protein given, if there is none, write NO RXN. Also indicate, if the reaction is fast or slow.
- As described in 4C above, PLP-dependent enzymes can generate formaldehyde from serine. This compound would be toxic if widely distributed in the cell, so normally the formaldehyde is captured by tetrahydrofolate, generating N^5 ,N^10-methylene tetrahydrofolate a) Draw a general acid/general base mechanism that an enzyme might use for this transformation b) Explain the role of the coenzymes N^5 , N^10-methylene tetrahydrofolate, and NADPH in thymidylate synthase, which converts dUMP to dTMP (no mechanism needed; an accurate written description will do,1. Draw the structure of the L-isomer of the Fisher projection of one epimer of D-allopyronoside. Discuss why is this an epimer of the monosaccharide. 2. Is this saccharide a good substrate for glycolysis? Explain.Make an electron-flow-mechanism for this synthetic scheme. This involves predicting major and by-products using electronic and structural effects. The arrow push mechanism must be shown.(from the reaction of α-ketoacids and oxaprolines to proteins that contain native serine residues ) with label