L-aspartate:2-oxoglutarate aminotransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. [EC:2.6.1.1]

L-aspartate:2-oxoglutarate aminotransferase activity, also known as aspartate aminotransferase (AST) or glutamate-oxaloacetate transaminase (GOT), catalyzes the reversible transfer of an amino group from L-aspartate to 2-oxoglutarate. This reaction is crucial for several metabolic pathways, including the citric acid cycle and the urea cycle. The enzyme utilizes pyridoxal phosphate (PLP) as a cofactor, which forms a Schiff base with the amino group of the substrate. The reaction proceeds through a ping-pong mechanism, where the enzyme first forms an external aldimine with the amino group of L-aspartate. This aldimine is then converted to a ketimine, releasing oxaloacetate and forming a quinonoid intermediate. The quinonoid intermediate then reacts with 2-oxoglutarate, releasing glutamate and regenerating the enzyme. The transfer of the amino group from L-aspartate to 2-oxoglutarate is critical for maintaining the balance of amino acids and carbon skeletons in the cell. AST is a key enzyme in the interconversion of amino acids and plays a significant role in nitrogen metabolism.'
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Proteins (1)

Compounds (6)