(Integrates with Chapter \(22 .\) ) Write a balanced equation for the synthesis of glucose (by gluconeogenesis) from aspartate.

Short Answer

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The balanced chemical reactions representing the synthesis of glucose from aspartate via gluconeogenesis are: Step 1 - Aspartate + alpha-ketoglutarate yields Oxaloacetate + Glutamate. Step 2 - Oxaloacetate + GTP yields Phosphoenolpyruvate + GDP + CO2. Step 3 - 2 Phosphoenolpyruvate + 4 ADP + 4 Pi + 2 NADH yields Glucose + 4 ATP + 2 NAD+ + 2 H2O.

Step by step solution

01

Conversion of Aspartate to Oxaloacetate

Aspartate is first converted into oxaloacetate through a transamination reaction. Transaminase transfers an amino group from aspartate to alpha-ketoglutarate, forming oxaloacetate and glutamate. This can be written in chemical terms as: \[\mathrm{Aspartate + \alpha - ketoglutarate \rightarrow Oxaloacetate + Glutamate}\]
02

Conversion of Oxaloacetate to Phosphoenolpyruvate

Oxaloacetate is then converted into phosphoenolpyruvate (PEP). This two-step process involves the decarboxylation (removal of a carboxyl group) and phosphorylation (addition of a phosphate group) of oxaloacetate. Biochemically, this happens in the presence of GTP (guanosine triphosphate), and it can be represented like this: \[\mathrm{Oxaloacetate + GTP \rightarrow Phosphoenolpyruvate + GDP + CO_2}\]
03

Conversion of Phosphoenolpyruvate to Glucose

The final step involves multiple reactions via the gluconeogenic pathway to convert phosphoenolpyruvate into glucose. Pyruvate carboxylase and PEP carboxykinase are the key enzymes that participate in the conversion. These steps are complex and have been summarized in this reaction: \[\mathrm{2 Phosphoenolpyruvate + 4 ADP + 4 Pi + 2 NADH \rightarrow Glucose + 4 ATP + 2 NAD+ + 2 H2O}\]

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Transamination Reaction
The transamination reaction is a critical biochemical process in which an amino group from one amino acid is transferred to a keto acid. This process helps in the interconversion of amino acids and plays a vital role in the metabolism of nitrogenous compounds.

In the context of gluconeogenesis, aspartate undergoes a transamination reaction where it donates its amino group to \(\alpha-ketoglutarate\), resulting in the formation of oxaloacetate and glutamate. The enzyme that catalyzes this reaction is called a transaminase or aminotransferase. This pivotal step not only produces an important gluconeogenic intermediate, oxaloacetate, but also links amino acid catabolism with glucose synthesis.

Understanding this concept is essential because it illustrates how nitrogen from amino acids can be removed, allowing their carbon skeletons to be utilized in glucose production. The ability to interconvert molecules offers flexibility in metabolic pathways, ensuring that the body can maintain blood glucose levels during fasting periods or heavy exercise when glycogen stores are depleted.
Biochemical Pathways
Biochemical pathways are sequences of chemical reactions occurring within a cell that lead to the synthesis or breakdown of molecules. These pathways are highly regulated, and each step is typically catalyzed by a specific enzyme. In the textbook exercise, gluconeogenesis is the biochemical pathway in focus—comprising a series of reactions that convert non-carbohydrate precursors into glucose.

It's important for students to note how biochemical pathways, like gluconeogenesis, demonstrate the cell's ability to convert various substrates into needed compounds. It's not a single reaction but a carefully orchestrated sequence, where the product of one reaction becomes the substrate for the next. Each step can be influenced by cellular conditions and regulatory molecules, allowing the cell to adapt to energetic demands.

The study of these pathways shows how organisms convert food into energy, synthesize necessary cellular components, and manage waste materials. Thus, a deep understanding of metabolic pathways like gluconeogenesis helps us appreciate the complexity and efficiency of biological systems.
Oxidative Decarboxylation
Oxidative decarboxylation is a critical reaction where a carboxyl group is removed from a molecule as carbon dioxide (\(CO_2\)), and the remaining compound is oxidized. This type of reaction is significant in metabolism as it often represents a link between different metabolic pathways.

During gluconeogenesis, oxaloacetate is transformed into phosphoenolpyruvate through an oxidative decarboxylation step, which implies the loss of a \(CO_2\) molecule and the gain of a high-energy phosphate bond in the presence of GTP. This particular reaction is notable because it helps to circumvent the irreversible step in glycolysis wherein pyruvate is converted to acetyl-CoA, and thereby enables the flow of metabolites in the direction of glucose production.

A clear grasp of oxidative decarboxylation is essential for students because it highlights how energy can be conserved and redirected within a cell's metabolism. The removal of a carboxyl group often makes a molecule more reactive and primes it for subsequent steps in metabolic pathways, such as the generation of glucose in gluconeogenesis.

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Most popular questions from this chapter

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