| EC |
2.3.1.29 |
| Accepted name: |
glycine C-acetyltransferase |
| Reaction: |
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate |
| Other name(s): |
2-amino-3-ketobutyrate CoA ligase; 2-amino-3-ketobutyrate coenzyme A ligase; 2-amino-3-ketobutyrate-CoA ligase; glycine acetyltransferase; aminoacetone synthase; aminoacetone synthetase; KBL; AKB ligase |
| Systematic name: |
acetyl-CoA:glycine C-acetyltransferase |
| Comments: |
This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC 1.1.1.103, 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: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37257-11-7 |
| References: |
| 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 (1969) 657–671. [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 (1987) 14441–14447. [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 (2000) 1805–1812. [DOI] [PMID: 10712613] |
| 4. |
Schmidt, A., Sivaraman, J., Li, Y., Larocque, R., Barbosa, J.A., 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 (2001) 5151–5160. [DOI] [PMID: 11318637] |
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| [EC 2.3.1.29 created 1972] |
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