. The keto acids of the TCA cycle are also the other substrates of the aminotransferase family. How does this family of enzymes play a role in maintaining the NAD re-oxidation of NADH to NAD during glycolysis? (Use the amino acids alanine, aspartate

. The keto acids of the TCA cycle are also the other substrates of the aminotransferase family. How does this family of enzymes play a role in maintaining the NAD re-oxidation of NADH to NAD during glycolysis? (Use the amino acids alanine, aspartate

Name: 5.The keto acids of the TCA cycle are also the other substrates of the
Uploaded: 2024-03-20T06:42:55.000Z
Channel: Bartleby
Description: 5.The keto acids of the TCA cycle are also the other substrates of the aminotransferase family. How does this family of enzymes play a role in maintaining the NAD re-oxidation of NADH to NAD during glycolysis? (Use the amino acids alanine, aspartate,

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

See similar textbooks

Similar questions

4) Phosphofructokinase (PFK) is a highly regulated enzyme in glycolysis. ADP (and also AMP - adenosine monophosphate) bind to allosteric sites on PFK's structure, causing additional active sites (fructose-6-phosphate binding sites) to open. Conversely, ATP and PEP (phosphoenolpyruvate) bind to different allosteric sites, resulting in PFK's active sites closing. a) How does an allosteric activator work? What is the allosteric activator? When would it be important for PFK to be activated? Function: Allosteric Activator(s): Importance: b) How does an allosteric inhibitor work? What is the allosteric inhibitor? When would it be important for PFK to be inhibited? Function: Allosteric Inhibitor(s): Importance: c) How does this relate to the ideas of homeostasis and why does it make sense to control this system homeostatically? Use a specific example to make your comparison.
1. Opine dehydrogenases (ODH) have evolved in invertebrate marine organisms with wide-ranging physiological roles. The first class of this family of enzymes provides an alternative pathway for the lactate dehydrogenase pathway in anaerobic energy production. The lactate dehydrogenase pathway is found in higher organisms and in mammals including humans. One class of opine dehydrogenases catalyzes the reductive coupling of pyruvate to N-a-carboxyalkyl-L-amino acids represented by the re- action below: NH₂ ི་ ODH HO R 요 OH སྨིཾནྟཱ ར པ དརཱ ཨཱཋཏྭཱ… … ཨཱསྨིཾ ཏྟཏྟིནྡནྟི ཨཱ HO NAD(P)H NAD(P)* S R₁ R₂ where R1 is the side chain of the amino acid, R2 represents the alkyl group of the a-keto acid that is coupled to the amino acid, and NAD(P)H/NAD(P)* are the reduced/oxidized forms of nicotinamide ad- enine dinucleotide phosphate, a cofactor of the enzyme that catalyzes oxidation-reduction reactions. (a). The product of the reaction has two chiral centers as shown: The Ca atom of the amino acid…
Citrate (the product of the first step of the TCA cycle) is considered to be a sign of high energy. 1. Which step of glycolysis does citrate regulate (does it activate or inhibit that step?) 2. WHY exactly is citrate considered a sign of high energy?
1. Opine dehydrogenases (ODH) have evolved in invertebrate marine organisms with wide-ranging physiological roles. The first class of this family of enzymes provides an alternative pathway for the lactate dehydrogenase pathway in anaerobic energy production. The lactate dehydrogenase pathway is found in higher organisms and in mammals including humans. One class of opine dehydrogenases catalyzes the reductive coupling of pyruvate to N-a-carboxyalkyl-L-amino acids represented by the re- action below: དང་ NH₂ ODH ས HO S མིནྟཱ ཨཱར པ 'ནཔི ཏཏྭཱ ཡཾ དསྨཱ ཨབྷིནྡནྟི ཨཱ R₂ OH NAD(P)H NAD(P)* R OH R₁ R₂ where R1 is the side chain of the amino acid, R2 represents the alkyl group of the a-keto acid that is coupled to the amino acid, and NAD(P)H/NAD(P)* are the reduced/oxidized forms of nicotinamide ad- enine dinucleotide phosphate, a cofactor of the enzyme that catalyzes oxidation-reduction reactions. (a). : The product of the reaction has two chiral centers as shown: The Ca atom of the amino acid…
1. The first step in the payoff phase of glycolysis is catalyzed by the enzyme glyceraldehyde 3-phosphate dehydrogenase, an enzyme that contains a nucleophilic cysteine playing a central role in the reaction. A) In the direction of gluconeogenesis, what reaction does this enzyme catalyze? AG° = -6.3 kcal/mol for this reaction in the direction of gluconeogenesis. Based on what you know about the substrates involved, provide two chemical reasons as to why the AGO of this reaction is negative.
1. Identify the oxidized coenzyme (letter abbreviation only) that participates in this reaction of the Kreb’s cycle. Succinate --> Fumarate 2. How many mol of NADH can be obtained upon the beta oxidation of stearic acid? 3. How many mol of ATP can be obtained upon the complete oxidation of 1 mol stearic acid? 4. How many steps in glycolysis in which ATO is converted to ADP?
26. These catalyze oxidation and reduction reactions, e.g. pyruvate dehydrogenase, catalysing the oxidation of pyruvate to acetyl coenzyme A. a. oxidoreductases b. transferases c. hydrolases d. ligases 27. These catalyze transferring of the chemical group from one to another compound. An example is a transaminase, which transfers an amino group from one molecule to another. a. oxidoreduUctases b. transferases c. hydrolases d. ligases 28. They catalyze the hydrolysis of a bond. For example, the enzyme pepsin hydrolyzes peptide bonds in proteins. a. oxidoreductases b. transferases c. hydrolases d. ligases 29. Catalyze the association of two molecules. For example, DNA ligase catalyzes the joining of two fragments of DNA by forming a phosphodiester bond. a. oxidoreductases b. transferases c. hydrolases d. ligases 30. It is the loss of electrons, gain of oxygen or loss of hydrogen. a. reduction b. temperature C. substrate concentration d. oxidation
9. The transamination of the amino acid aspartate is catalyzed by aspartate aminotransferase. A) Draw out the mechanism for aspartate aminotransferase - you don’t need to show the subsequent formation of glutamate by the transaminase. B) After transamination, write out the subsequent steps (no mechanisms) to generate a molecule of glucose from two aspartates. How many ATP equivalents would this consume? C) After the transamination, write out the subsequent steps (no mechanisms) to fully oxidize aspartate into CO2 through malate (see above). How many ATP equivalents would this produce?
3. Answer the following questions about the metabolic pathway shown below: glutamate dehydrogenase e NH3 0-C-C-cH2-CH2-C- 0-C-CH-CH2-CH2-C-O + H,O + NAD + NH + NADH + H (a) Label the correct substances as the substrate, enzyme, and co-enzyme. (b) Which of the six classes does the enzyme of this reaction belong to? Why? (c) What is the name of the first molecule in this reaction? (d) Which metabolic pathway is this reaction likely to be a part of? A. glycolysis B. deamination C. beta-oxidation D. fermentation
1. How many ATP is produced in one molecule of glucose that undergo glycolysis plus oxidation of pyruvate to acetyl CoA? 2. Galactose and fructose can also used as substrate for glycolysis. Their conversion into a substrate that can enter into the glycolytic pathway involves the use of how many ATPs? 3. How many ATPs are produced when the product of glycolysis undergoes anaerobic respiration?
1. Consider the oxidation of the fatty acid with the common name arachidic acid. a. Draw the structure of arachidic acid. b. How many turns of the fatty acid oxidation cycle is required for the complete oxidation of arachidic acid? c. How many moles of ATP are formed from one mole of arachidic acid if the acetyl CoA produced go to the citric acid cycle and oxidative phosphorylation? Assume 1 mole of NADH is equivalent to 3 moles ATP and 1 mole FADH2 is equivalent to 2 moles of ATP. Show how you arrived at your answer
1. Prostaglandins are a class of eicosanoids, fatty acid derivatives with a variety of extremely potent actions on vertebrate tissues. They are responsible for producing fever and inflammation and its associated pain. Prostaglandins are derived from the 20- carbon fatty acid arachidonic acid in a reaction catalyzed by the enzyme prostaglandin endoperoxide synthase. This enzyme, a cyclooxygenase, uses oxygen to convert arachidonic acid to PGG2, the immediate precursor of many different prostaglandins. (a) The kinetic data given below are for the reaction catalyzed by prostaglandin endoperoxide synthase. Focusing here on the first two columns, determine the Vmax and Km of the enzyme. (b) Ibuprofen is an inhibitor of prostaglandin endoperoxide synthase. By inhibiting the synthesis of prostaglandins, ibuprofen reduces inflammation and pain. Using the data in the first and third columns of the table, determine the type of inhibition that ibuprofen exerts on prostaglandin endoperoxide…