Phosphate acetyltransferase
| Phosphate acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Phosphate acetyltransferase homodimer, Methanosarcina thermophila | |||||||||
| Identifiers | |||||||||
| EC no. | 2.3.1.8 | ||||||||
| CAS no. | 9029-91-8 | ||||||||
| 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 | ||||||||
| |||||||||
Phosphate acetyltransferase (EC 2.3.1.8) is an enzyme that catalyzes the chemical reaction
The substrates of this enzyme are phosphate and acetyl-CoA. Its products are acetyl phosphate and coenzyme A.[1][2] It was characterised from Clostridium kluyveri.[3]
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:phosphate acetyltransferase. Other names in common use include phosphotransacetylase, phosphoacylase, and PTA. This enzyme participates in three metabolic pathways: taurine and hypotaurine metabolism, pyruvate metabolism, and propanoate metabolism.[4]
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1QZT, PDB: 1R5J, PDB: 1TD9, PDB: 1VMI, PDB: 1XCO, PDB: 2AF3, and PDB: 2AF4.
References
- ↑ Bergmeyer HU, Holz G, Klotzch H, Lang G (1963). "[Phosphotransacetylase from Clostridium Kluyveri. Culture of the Bacterium, Isolation, Crystallization and Properties of the Enzyme]". Biochem. Z. (in German). 338: 114–21. PMID 14087284.
- ↑ Stadtman, E.R. (1952). "The Purification and Properties of Phosphotransacetylase". Journal of Biological Chemistry. 196 (2): 527–534. doi:10.1016/S0021-9258(19)52386-9. PMID 12980995.
- ↑ Stadtman, E.R. (1955). Phosphotransacetylase from Clostridium kluyveri. Methods in Enzymology. Vol. 1. pp. 596–599. doi:10.1016/0076-6879(55)01103-8.
- ↑ Enzyme 2.3.1.8 at KEGG Pathway Database.