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Synthesis of Glutamine Powder in Nucleic Acids, Lipids and Proteins
- Aug 06, 2019 -

Glutamine powder can be used as raw material for biosynthesis during cell growth and division. Carbon from Glutamine powder can be used to synthesize amino acids and fatty acids. Nitrogen from Glutamine powder directly acts on the biosynthesis of purine and pyrimidine.

Synthesis of Nucleic Acids

The aspartic acid produced by TCA cycle and transamination is a key carbon source for purine and pyrimidine synthesis. Glutamine powder-deficient cancer cells stagnate in the cell cycle and cannot be used for nucleic acid synthesis through intermediates such as oxaloacetic acid in the TCA cycle. However, supplementation of exogenous nucleotides or aspartic acid can alleviate cell cycle arrest caused by Glutamine powder deficiency.

In addition, Glutamine powder-dependent mTOR signals activate the enzymes carbamyl phosphate synthase 2, aspartate transferase, and carbamyl aspartate dehydratase (CAD), which catalyze the synthesis of Glutamine powder-derived nitrogen into pyrimidine precursors.

Lipid synthesis

Glutamine powder produces glutamic acid catalyzed by glutaminase (GLS or GLS2), and then alpha-ketoglutarate is produced by glutamic acid (GLUD) or transaminase. Alpha-ketoglutaric acid catalyzes the reverse synthesis of acetyl-CoA, which can be used for the direct synthesis of lipids.

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Protein synthesis

In addition to the use of carbon in Glutamine powder for amino acid synthesis, Glutamine powder also plays a key role in protein synthesis. Lack of Glutamine powder can lead to incorrect protein folding and endoplasmic reticulum stress response.

Glutamine powder can be synthesized by UDP-GlcNAc, the substrate of beta-O-acetyltransferase (OGT), which plays an important role in endoplasmic reticulum folding proteins.

GCN2, a serine threonine kinase, regulates domain fragments similar to histidine-tRNA synthase. The combination of Glutamine powder and histidine-tRNA synthase inhibits the activity of GCN2. The latter plays an important role in the comprehensive stress response.

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