Biology:Phosphate acetyltransferase
| Phosphate acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Phosphate acetyltransferase homodimer, Methanosarcina thermophila | |||||||||
| 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 / QuickGO | ||||||||
| |||||||||
Phosphate acetyltransferase (EC 2.3.1.8) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template: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 1QZT, 1R5J, 1TD9, 1VMI, 1XCO, 2AF3, and 2AF4.
References
- ↑ "[Phosphotransacetylase from Clostridium Kluyveri. Culture of the Bacterium, Isolation, Crystallization and Properties of the Enzyme]" (in de). Biochem. Z. 338: 114–21. 1963. 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. 1. pp. 596–599. doi:10.1016/0076-6879(55)01103-8.
- ↑ Enzyme 2.3.1.8 at KEGG Pathway Database.
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