Glycine C-acetyltransferase
| Glycine C-acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.29 | ||||||||
| CAS no. | 37257-11-7 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Glycine C-acetyltransferase (EC 2.3.1.29) is an enzyme that catalyzes the chemical reaction:
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The two substrates of this enzyme are glycine and acetyl-CoA. Its products are (S)-2-amino-3-ketobutyric acid and coenzyme A.[1]
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 and L-threonine 3-dehydrogenase act together to degrade threonine to glycine. It employs one cofactor, pyridoxal phosphate.[2]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 1FC4.
Human genes
References