phosphate acetyltransferase

{{infobox enzyme

| Name = Phosphate acetyltransferase

| EC_number = 2.3.1.8

| CAS_number = 9029-91-8

| GO_code = 0008959

| image = 2af3.jpg

| width = 270

| caption = Phosphate acetyltransferase homodimer, Methanosarcina thermophila

}}

In enzymology, a phosphate acetyltransferase ({{EC number|2.3.1.8}}) is an enzyme that catalyzes the chemical reaction

:acetyl-CoA + phosphate $\rightleftharpoons$ 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 {{PDB link|1QZT}}, {{PDB link|1R5J}}, {{PDB link|1TD9}}, {{PDB link|1VMI}}, {{PDB link|1XCO}}, {{PDB link|2AF3}}, and {{PDB link|2AF4}}.

References

{{cite journal |vauthors=BERGMEYER HU, HOLZ G, KLOTZSCH H, LANG G | title = Phosphotransacetylase from Clostridium Kluyveri. Culture of the Bacterium, Isolation, Crystallization and Properties of the Enzyme | date = 1963 | journal = Biochem. Z. | volume = 338 | pages = 114–21 | pmid = 14087284 }}
{{cite journal | author = STADTMAN ER | date = 1952 | title = The purification and properties of phosphotransacetylase | journal = J. Biol. Chem. | volume = 196 | pages = 527–34 | pmid = 12980995 | issue = 2 | doi = 10.1016/S0021-9258(19)52386-9 | doi-access = free }}
{{cite book | author = Stadtman ER | date = 1955 | title = [98] Phosphotransacetylase from Clostridium kluyveri | volume = 1 | pages = [https://archive.org/details/methodsinenzymol01acad/page/n628 596]–599 | doi = 10.1016/0076-6879(55)01103-8 | series = Methods in Enzymology | editor1-last = Stadtman | editor1-first = ER | isbn = 0-12-181801-2 | url-access = registration | url = https://archive.org/details/methodsinenzymol01acad }}

Category:EC 2.3.1

Category:Enzymes of known structure