Amino Acid Biosynthesis: Uncovering the Pathways for Synthesizing Amino Acids

The glutamate dehydrogenase reaction converts glutamate to glutamine, using ammonia as a nitrogen source.

The first step in the biosynthesis of isoleucine is the condensation of acetyl-CoA and propionyl-CoA to form α-ketobutyrate.

The aspartate aminotransferase reaction converts oxaloacetate to aspartate, using glutamate as a nitrogen source.

Serine hydroxymethyltransferase catalyzes the conversion of serine to glycine, with the release of a methylene group.

The alanine aminotransferase reaction converts pyruvate to alanine, using glutamate as a nitrogen source.

The first step in the biosynthesis of valine is the condensation of acetyl-CoA and isobutyryl-CoA to form α-ketoisovalerate.

The aspartate kinase reaction converts phosphoenolpyruvate to aspartate, using ATP as an energy source.

Threonine deaminase catalyzes the conversion of threonine to glycine, with the release of ammonia.

The glutamate synthase reaction converts α-ketoglutarate to glutamate, using ammonia and NADPH as cofactors.

The first step in the biosynthesis of leucine is the condensation of acetyl-CoA and butyryl-CoA to form α-ketoisocaproate.

The malate dehydrogenase reaction converts oxaloacetate to malate, using NADH as a cofactor.

Methionine synthase catalyzes the conversion of methionine to cysteine, using vitamin B12 as a cofactor.

The isoleucine aminotransferase reaction converts α-ketobutyrate to isoleucine, using glutamate as a nitrogen source.

The first step in the biosynthesis of lysine is the condensation of acetyl-CoA and propionyl-CoA to form α-ketoadipate.

The pyruvate kinase reaction converts phosphoenolpyruvate to pyruvate, using ADP as an energy acceptor.