19. From the various reactions you have learned in catabolism of amino acids; list three reactions inwhich NH4 is used as substrate to yield different products, in other words, reactions that will reduceNH4 concentration in the cell.

Catabolism of proteins releases amino acids which composed of mainly two parts-amino nitrogen (in…

Answered: From the various reactions you have…

Biology: The Unity and Diversity of Life (MindTap Course List)

14th Edition

ISBN:9781305073951

Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Chapter7: How Cells Release Chemical Energy

Section: Chapter Questions

Problem 7SQ

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7. During amino acid catabolism, how is amino group removed and excreted in the form of urea? Please write the reactions starting from a generic amino acid to the formation of urea. Please indicate the names of enzymes, cofactors, names of substrates, and products of each reaction and the location of the reaction i.e. whether in cytoplasm or mitochondria.
1. Please identify the substrate and type of reaction, and explain how these reactions work for the following two enzymes Two enzymes: succinate dehydrogenase and L-amino acid reductase
1. There are two major categories of enzyme, inhibition, name, and describe them. 1a. Reverse inhibition can be overcome to allow the enzyme to resume is Catley activities. Describe how reversible inhibition can occur and how it can be over come.
5. a) Why would an enzyme that is effective with one reaction have no effect on another reaction?
1. Describe the reaction catalyzed by salivary amylase. To which class of enzymes does amylase belong? Explain thoroughly.
. 1 Which enzyme catalyzes the first step of glycolysis? explain the whole pathway in detail?
1. List the main coenzymes in metabolism and describe their roles.
1, Using Model 10.9, draw the structure of the substrates of the pentose phosphate pathway and write down the enzymes and coenzymes that are involved in the reaction
1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain
1.A student was given two test tubes. One tube contains a reaction catalyzed by an inorganic catalyst, while the second tube contains a reaction catalyzed by an enzyme which is protein in nature. Give two laboratory procedures which you can perform to differentiate which of the two tubes contain an enzyme-catalyzed reaction. 2. List the enzymes whose levels are elevated in blood serum as a result of hepatitis or cirrhosis of the liver.
6. Reciprocal regulation of opposing pathways is necessary to avoid the wasteful synthesis anddegradation of metabolic intermediates. Provide two distinct examples of reciprocal regulation. Bespecific, and be sure to explain the conditions that signal enzyme activation and/or inhibition.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.

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From the various reactions you have learned in catabolism of amino acids; list three reactions in which NH4 is used as substrate to yield different products, in other words, reactions that will reduce NH4 concentration in the cell.