glycine:2-oxoglutarate aminotransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: glycine + 2-oxoglutarate = glyoxylate + L-glutamate. [EC:2.6.1.4, MetaCyc:GLYCINE-AMINOTRANSFERASE-RXN]

Glycine:2-oxoglutarate aminotransferase activity, also known as GOT or AST, is a crucial enzyme involved in amino acid metabolism. It catalyzes the reversible transfer of an amino group from L-aspartate to α-ketoglutarate, generating oxaloacetate and L-glutamate. This reaction plays a pivotal role in several metabolic pathways, including the citric acid cycle, gluconeogenesis, and urea cycle.

The enzyme exhibits a high degree of specificity for its substrates, requiring both glycine and α-ketoglutarate for activity. The reaction proceeds through a ping-pong mechanism, involving the formation of a covalent intermediate with the enzyme.

First, the enzyme binds L-aspartate and removes its amino group, forming a Schiff base intermediate. This amino group is then transferred to α-ketoglutarate, generating L-glutamate and regenerating the enzyme.

The activity of glycine:2-oxoglutarate aminotransferase is essential for maintaining amino acid homeostasis and regulating the flow of carbon and nitrogen through metabolic pathways. Disruptions in the enzyme's activity can lead to various metabolic disorders, including hyperammonemia, encephalopathy, and neurodegeneration. This enzymatic function is critical for cellular energy production, detoxification, and overall metabolic balance.'
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Proteins (1)

Compounds (3)