EC - Glycine C-acetyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
glycine C-acetyltransferase
Other names:
2-amino-3-ketobutyrate CoA ligase
2-amino-3-ketobutyrate coenzyme A ligase
2-amino-3-ketobutyrate-CoA ligase
aminoacetone synthase
glycine acetyltransferase
aminoacetone synthetase
AKB ligase
Systematic name:
acetyl-CoA:glycine C-acetyltransferase




This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC, L-threonine 3-dehydrogenase, in the degradation of threonine to form glycine [3]. This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00518
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008890
CAS Registry Number: 37257-11-7


  1. McGilvray, D. and Morris, J.G.
    Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase".
    Biochem. J. 112 : 657-671 (1969). [PMID: 5821726]
  2. Mukherjee, J.J. and Dekker, E.E.
    Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme.
    J. Biol. Chem. 262 : 14441-14447 (1987). [PMID: 3117785]
  3. Edgar, A.J. and Polak, J.M.
    Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs.
    Eur. J. Biochem. 267 : 1805-1812 (2000). [PMID: 10712613]
  4. Schmidt, A., Sivaraman, J., Li, Y., Larocque, R., Barbosa, J.A.R.G., Smith, C., Matte, A., Schrag, J.D. and Cygler, M.
    Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism.
    Biochemistry 40 : 5151-5160 (2001). [PMID: 11318637]

[EC created 1972]