Glycine C-acetyltransferase
| 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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1FC4.
Human genes
[edit]References
[edit]- 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.
