ResetHelpoxaloacetatealpha-ketoglutaratealdehydeaspartateglutamineketoneasparagineglutamateTransamination pair (1)Transamination pair (2)Not part of a transamination pair Transamination is a chemical reaction that transfers an amino group to a keto acid to form new amino acids. This pathway is responsible for the deamination ofmost amino acids. This pathway is one of the major degradation pathways that converts essential amino acids to nonessential amino acids (amino acids that canbe synthesized de novo by the organism). Transamination reactions can be regarded as anaplerotic pathways because they are reversible reactions that can yieldcitric acid cycle intermediates. Cells containing amino acids in abundance can convert them via transamination to needed intermediates. Being reversible,transaminations can be used either for amino acid synthesis or for replenishment of citric acid cycle intermediates, depending on the needs of the cell.Corresponding pairs of reactants (amino acids) and products (intermediates) are called transamination pairs.Identify the transamination pairs among the following species.Drag the appropriate species to their respective bins.Hint 1. General transamination reactionIn the reaction shown, the amino group from the species containing R1 is transferred to the keto acid containing R2:NH,NH,R,-C-co0 + R-C-co0R,-C-CoO + R-C-c0"

TRANSAMINATON PAIR 1 Glutamate/ alpha keto gluterate Tramsamination pair 2 Aspartate/ oxaloacete…

Answered: Transamination pair (1)

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Zymogen activation Covalent modification Competitive inhibition Allosteric activation Allosteric inhibition
Which of the following statements about the transamination and deamination steps of amino acid degradation is true? (A) a-ketoglutarate is always formed during a transamination between an amino acid and glutamate. (B) Transamination reactions produce glutamate that is deaminated after entering the urea cycle. (C) Free ammonia is removed from glutamate using glutamate dehydrogenase and NAD+ as an oxidizing agent. (D) The free NH4+ that is removed from glutamate during the deamination reaction is used to form glucose.(E) The carbon backbone that results from transamination enters the mitochondria to be used in the urea cycle.
The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B?(b) Genetic deficiency in animals of enzyme C would result in excessiveurinary excretion of what compound?(c) Some forms of the condition described in (b) can be successfully treatedby injection of rather massive doses of vitamin B12. What kind ofgenetic alteration in the enzyme would be consistent with this result?(d) Genetic deficiency in animals of enzyme B will result in excessive urinaryexcretion of what amino acid?
Of eight enzymes in the CAC, why is the succinate dehydrogenase complex unique? Because it is a component of the electron transport chain Because it catalyzes an oxidative reaction Because it is an integral membrane protein All of the above Only A and C
An animal cell is capable of converting alanine into serine. What is the shortest pathway using known enzymes by which this conversion could be accomplished? Show intermediates and cofactors; no enzyme names are required. (Hint: the first step is the removal of the nitrogen by transamination.)
Which of the following is NOT TRUE about fatty acid biosynthesis? A. 8 NADPH is used to produce palmitate. B. The growing fatty acid chain is elongated by the sequential addition of two-carbon units. C. The process is repeated 7 times to produce palmitate. D. The process occurs in the cytosol.
Leigh syndrome is characterized by psychomotor regression: that is, the progressive loss of mental andmovement abilities. Patients also suffer from lacticacidosis, a condition in which mitochondrial respiration is deficient, so their tissues metabolize glucoseanaerobically, leading to the buildup of lactate. Somepatients with Leigh syndrome have a mutation in themitochondrial gene MT-CO3, which encodes a subunit of the electron transport complex cytochromec oxidase. Other patients diagnosed with Leigh syndrome have a loss-of-function mutation in the nucleargene SURF1, which encodes a factor needed for theassembly of this same enzyme complex.a. How can the same symptoms result from mutationsin a mitochondrial gene and from mutations in anuclear gene?
The citric acid cycle itself, which is composed of enzymatically catalyzed steps, can be thought of essentially as a supramolecular enzyme. Explain.
Consider the following Statements: (1) Citric acid cycle intermediates are often the products from amino acid carbon skeleton degradation. (2) The net effect of transamination is to collect the amino groups from a variety of amino acids into the amino acids glutamate and aspartate. (3) All of the reactions of the urea cycle occur within mitochondria. how many is true
For each of the statements below about the dUTPase enzyme, mark whether it is true or false. If it is false, change the language to make the statement true. _______If the dUTPase enzyme is the rate determining step in a larger metabolic pathway, the reaction likely lies near to equilibrium and is irreversible. _______For the dUTPase reaction, it is not likely that DG’ = DG°’ _______ dUTPase has a higher affinity for its substrate than for its product, but both of these are higher than the affinity for the transition state _______Kinetic analysis of dUTPase using Michaelis-Menten methods assumes that the formation of the E*S complex has a large negative value for DG
Which one of the following statements is not correct for the transamination reaction that amino acid contributed? a.Pyridoxal phosphate has a crucial role in transamination reactions. b.Enzyme levels may be high in liver and muscle diseases. c.Transamination reactions are catalyzed by aminotransferases. d.Alanine aminotransferase catalyzed reactions can be given as an example for transamination reactions. e.Transamination reactions are irreversible.
Strategies for regulating the central pathways in carbohydrate metabolism vary among different cells in one organism and among organisms. Slight changes in the regulation of enzymes in central metabolism can effectively re-route metabolite traffic through these pathways, just like a small mutation in PFK-1 can convert a healthy cell into a cancerous one. For instance, Gillaspera mold uses an alternative strategy for regulation the TCA and glycolysis. Gillaspera contains a unique isocitrate dehydrogenase that has an allosteric site for citrate. High citrate inhibits isocitrate dehydrogenase in this organism. Gillaspera also lacks a citrate binding site on PFK-1, so this variant of the enzyme is not affected by citrate concentrations at all. Gillaspera lacks the enzymes ethanol dehydrogenase and lactate dehydrogenase and no carbons are lost in its unique fermentation product. Would high glucose in these organisms lead to production of carbon dioxide from glucose catabolism?…

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