| glycine C-acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.29 | ||||||||
| CAS no. | 37257-11-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a glycine C-acetyltransferase (EC 2.3.1.29) is an enzyme that catalyzes the chemical reaction:
- acetyl-CoA + glycine CoA + 2-amino-3-oxobutanoate
Thus, the two substrates of this enzyme are acetyl-CoA and glycine, whereas its two products are CoA and 2-amino-3-oxobutanoate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:glycine C-acetyltransferase. Other names in common use include 2-amino-3-ketobutyrate CoA ligase, 2-amino-3-ketobutyrate coenzyme A ligase, 2-amino-3-ketobutyrate-CoA ligase, glycine acetyltransferase, and aminoacetone synthase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1FC4.
Human genes
References
- McGilvray D, Morris JG (1969). "Utilization of L-threonine by a species of Arthrobacter. A novel catabolic role for "aminoacetone synthase"". Biochem. J. 112 (5): 657–71. doi:10.1042/bj1120657. PMC 1187769. PMID 5821726.