Glycine C-acetyltransferase (GCAT)

Glycine C-acetyltransferase (GCAT) is a mitochondrial enzyme catalyzing a key reaction in amino acid metabolism: the conversion of 2-amino-3-ketobutyrate and coenzyme A into glycine and acetyl-CoA[1][2][3][5][6]. It is classified as an acyltransferase, specifically EC 2.3.1.29, and depends on pyridoxal phosphate as a cofactor[2][5][6]. GCAT is strongly expressed in tissues including heart, brain, liver, pancreas, and lung[5]. The enzyme plays an essential role in the degradation of L-threonine to glycine, forming the second step of a conserved metabolic pathway in both prokaryotic and eukaryotic cells, with implications in broader glycine, serine, and threonine metabolism[1][2][3][5][6]. Structurally, it contains specific catalytic domains and residues linked to its enzymatic mechanism involving Schiff base formation, nucleophilic attack, and intermediate stabilization[6]. Several aliases exist, reflecting its enzymological activity and mitochondrial localization. GCAT has associated disease links (e.g., cancer), but its direct role as a therapeutic target, interacting drugs, biomarkers, or specific safety concerns have not been well described or established in available literature[3].

Other names

2-amino-3-ketobutyrate coenzyme A ligaseKBLAKB ligaseAminoacetone synthaseGlycine acetyltransferase2-amino-3-ketobutyrate-CoA ligase