glycine C-acetyltransferase;
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

Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups

acetyl-CoA:glycine C-acetyltransferase

acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate [RN:R00371]

R00371

acetyl-CoA [CPD:C00024];
glycine [CPD:C00037]

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].

1  [PMID:5821726]

McGilvray D, Morris JG.

Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase".

Biochem. J. 112 (1969) 657-71.

Arthrobacter sp.

2  [PMID:3117785]

Mukherjee JJ, Dekker EE.

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) 14441-7.

Escherichia coli [GN:eco]

3  [PMID:10712613]

Edgar AJ, Polak JM.

Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs.

Eur. J. Biochem. 267 (2000) 1805-12.

Homo sapiens [GN:hsa], Mus musculus [GN:mmu]

4  [PMID:11318637]

Schmidt A, Sivaraman J, Li Y, Larocque R, Barbosa JA, Smith C, Matte A, Schrag JD, 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) 5151-60.

Escherichia coli [GN:eco]

5

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