Phosphate acetyltransferase
| acetyl phosphate | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.8 | ||||||||
| CAS number | 9029-91-8 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a phosphate acetyltransferase (EC 2.3.1.8) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + phosphate CoA + acetyl phosphate
The substrates of this enzyme are acetyl-CoA and phosphate, whereas its two products are CoA and acetyl phosphate.
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 3 metabolic pathways: taurine and hypotaurine metabolism, pyruvate metabolism, and propanoate metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1QZT, 1R5J, 1TD9, 1VMI, 1XCO, 2AF3, and 2AF4.
References
- BERGMEYER HU, HOLZ G, KLOTZSCH H, LANG G (1963). "[PHOSPHOTRANSACETYLASE FROM CLOSTRIDIUM KLUYVERI. CULTURE OF THE BACTERIUM, ISOLATION, CRYSTALLIZATION AND PROPERTIES OF THE ENZYME.]". Biochem. Z. 338: 114–21. PMID 14087284.
- STADTMAN ER (1952). "The purification and properties of phosphotransacetylase". J. Biol. Chem. 196 (2): 527–34. PMID 12980995.
- Stadtman ER (1955). Stadtman, ER, ed. "Phosphotransacetylase from Clostridium kluyveri". Methods Enzymol. Methods in Enzymology. 1: 596–599. doi:10.1016/0076-6879(55)01103-8. ISBN 0-12-181801-2.