Aminomethyltransferase (AMT)

Aminomethyltransferase is an enzyme encoded by the AMT gene, localized to the mitochondrial matrix as a component of the glycine cleavage system[1][2]. It catalyzes the transfer of a methylamine group from the glycine cleavage system's intermediate to tetrahydrofolate, linking glycine degradation with cellular one-carbon metabolism and folate-related methylation pathways[1][2]. Aminomethyltransferase is essential for the breakdown of glycine, an amino acid and neurotransmitter, thereby preventing toxic accumulation of glycine—especially in the brain[2][4]. Pathogenic mutations in AMT are responsible for 20% of cases of nonketotic hyperglycinemia, a disorder characterized by severe neurological dysfunction beginning in the neonatal or infantile period due to excessive glycine accumulation[1][2][4]. There are no direct drugs targeting aminomethyltransferase, and disease management focuses on downstream reduction of glycine or modulation of glycine neurotransmission.

Other names

glycine cleavage system protein TAMTGCEGCSTGCVTNKH

No direct clinical inhibitors or activators of AMT are in current therapeutic use. Drugs used in glycine encephalopathy act downstream to reduce glycine levels (sodium benzoate) or modulate glycine receptors (dextromethorphan)