The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

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, 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, KEGG, MetaCyc, PDB, 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 (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. [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. [PMID: 11318637]
[EC created 1972]

Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald