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Chapter 24: Q24P (page 1123)

Glutamine is biosynthesised from glutamate in two steps using ATP and ammonia. Propose a mechanism for this biosynthesis.

Short Answer

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Mechanism followed as:

Step by step solution

01

Synthesis of glutamine from glutamate

The glutamine synthesis from glutamate occurs from alpha-ketoglutarate produced as an intermediate in the TCA cycle (citric acid cycle). The reaction occurs by glutamine synthase, an allosteric enzyme. The reaction occurs in the presence of ammonia, and ATP is converted to ADP.

02

Mechanism

Mechanism followed as:

  1. Glutamate is converted to Y - glutamyl phosphate as an intermediate by adding a phosphate ion.

With the conversion of ATP to ADP

  1. Glutamate synthase is added with the ammonia phosphate group and is replaced by amine and glutamine formed.

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Most popular questions from this chapter

What coenzyme is required to convert pyruvate to acetaldehyde?

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A student is trying to determine the mechanism for a reaction that uses ATP to activate a carboxylate ion, which reacts with a thiol. If the carboxylate ion attacks the gamma- phosphorous of ATP, the reaction products are the thioester, ADP, and phosphate. However, whether it attacks the alpha-phosphorous or the beta-phosphorous of ATP cannot be determined from the reaction products because the thioester, AMP, and pyrophosphate would be the products in both reactions. The mechanisms can be distinguished by a labelling experiment in which the enzyme, the carboxylate ion, ATP, and radioactively labelled pyrophosphate are incubated, and then the ATP is isolated. If the isolated ATP is radioactive, the attack occurs on the alpha-phosphorous. If it is not radioactive, an attack occurs on the beta- phosphorous. Explain these conclusions.

When pyruvate is reduced by NADH to lactate, which hydrogen in lactate comes from NADH?
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