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The reaction mechanism of alpha-amylase going through a Nelson Somagyi Assay. (please draw the structure of the steps)
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- One mechanism by which lead exerts its poisonous effect on enzymes can be stopped by chelation therapy with EDTA. Describe this type of lead poisoning and explain why it is reversible.Multivitamin B complex are essential compounds that are used as derivatives for compounds necessary for many metabolic activities. Give 3 vitamin B compounds and explain where and how they are used along the metabolic pathway.Orotic aciduria results when one of the enzyme activities of UMP synthetase is absent. This syndrome is characterized by large amounts of orotic acid in the blood and urine, megaloblastic anemia (characterized by large, immature , and dysfunctional red blood cells) and retarded growth. Suggest a possible treatment for this condition.
- Catalase is the enzyme. experiment with h2O2 3. What is the marker for the enzyme’s optimum condition?true or false: A high dTTP concentration shifts the specificity of ribonucleotide reductase toward ADP reduction.Lactate dehydrogenase is a tetramer of MW 134000 g/mole composed of subunits which are equal in size. It is found in the cytoplasm of eukaryotic and prokaryotic cells. Describe the secondary, tertiary and quaternary structures of lactate dehydrogenase.
- Normal cells die in a nutrient medium containing thymidine and methotrexate, whereas mutant cells defective in thymidylate synthase survive and grow. Explain.The text describes a form of gout that results from HGPRT deficiency. Propose one or two additional enzyme abnormalities that might similarly lead to hyperuricemia.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.
- The enzymatic activity of PFK1 is generally measured by set- ting up a coupled enzyme assay system whereby aldolase, triose phos- phate isomerase, and glycerol-3-phosphate dehydrogenase are added to the assay mixture. For the latter enzyme, NADH is added and its change in concentration is readily monitored at 340 nm. Write the chain of reactions catalyzed by these enzymes using structural formulas, label substrates and products, and explain why the coupled en- zyme assay system leads to oxidation of NADH. While the chain of reac- tions is similar to those in glycolysis, there is a critical difference because of the dehydrogenase enzyme. Describe how this enzyme causes the chain of reactions to differ from those in glycolysis.Typical activity curves of enzymes that are analyzed in the test tube, like the one presented below, flatten out with time. Provide two possible reasons why this is observed. Must be less than 50 words totalTyrosinase enzyme activity is assayed by monitoring the oxidation of 3, 4-dihydroxyphenylalanine (dopa) to the red-colored dopachrome. Calculate the tyrosinase activity (U/mL) by using the experimental data given below
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