Aspartate biosynthesis (Saccharomyces cerevisiae)

Jump to: navigation, search

The biosynthesis of aspartate is an interface between amino acid metabolism and carbohydrate metabolism. Aspartate is synthesized through a transamination reaction between oxaloacetate, an important Krebs cycle intermediate, and glutamate, an amino acid. Here, aspartate aminotransferase catalyzes the reversible transfer of an amino group from glutamate to oxaloacetate, forming -ketoglutarate and aspartate. Yeast aspartate aminotransferase is encoded by AAT1 and AAT2. Aat1p localizes to mitochondria and may be involved in a putative malate-aspartate shuttle, while Aat2p localizes to the cytosol and is required for growth on minimal media lacking aspartate. Aspartate, in addition to its role as a proteinogenic amino acid, is a substrate in the arginine biosynthesis pathway and a precursor to the aspartate family amino acids methionine, isoleucine, asparagine, and threonine in S. cerevisiae. Source: [YeastGenome](https://pathway.yeastgenome.org/).