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Information on EC 2.3.1.8 - phosphate acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A9M8

for references in articles please use BRENDA:EC2.3.1.8
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     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.8 phosphate acetyltransferase
IUBMB Comments
Also acts with other short-chain acyl-CoAs.
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Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0A9M8
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphotransacetylase, phosphate acetyltransferase, pta-1, aywb-pdul, pdul1, pdul2, moth_0864, pta-2, moth_1181, phosphotransacetylase pta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyltransferase, phosphate
-
-
-
0
phosphoacylase
-
-
-
0
phosphotransacetylase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:phosphate acetyltransferase
Also acts with other short-chain acyl-CoAs.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-91-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-
-
-
r
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
-
-
-
r
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
-
-
-
-
r
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
desulfo-CoA
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyruvate
additional information
-
not significant efects: NADH, ATP, phosphoenol pyruvate and aspartate, even at concentrations as high as 10 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9 - 2.4
acetyl phosphate
0.029 - 0.058
acetyl-CoA
0.059 - 0.067
CoA
1.5 - 3
phosphate
0.312
acetyl phosphate
-
pH 7.8, 30°C
0.0095
acetyl-CoA
-
pH 7.8, 30°C
0.0327
CoA
-
pH 7.8, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 227
acetyl phosphate
0.03 - 29.6
acetyl-CoA
415
acetyl phosphate
-
pH 7.8, 30°C
120
acetyl-CoA
-
pH 7.8, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1300
acetyl phosphate
-
pH 7.8, 30°C
12600
acetyl-CoA
-
pH 7.8, 30°C
12600
CoA
-
pH 7.8, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
desulfo-CoA
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the substrate-binding site is located at the C-terminal PTA-PTB domain. The N-terminal P-loop NTPase domain is involved in expression of the maximal catalytic activity, stabilization of the hexameric native state, and phosphate acetyltransferase activity regulation by NADH, ATP, phosphoenolpyruvate, and pyruvate. The truncated protein Pta-F3 is able to complement the growth on acetate of an Escherichia coli mutant defective in acetyl-CoA synthetase and phosphate acetyltransferase activity
physiological function
-
expression of phosphate acetyltransferase eutD restOres the ability of a strain lacking phosphate acetyltransferase pta and acetate kinase to grow on acetate as sole carbon source
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77000
x * 77000, SDS-PAGE, recombinant protein
36000
-
2 * 36000, SDs-PAGE, recombinant protein
79500
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 77000, SDS-PAGE, recombinant protein
dimer
-
2 * 36000, SDs-PAGE, recombinant protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimizu, M.; Suzuki, T.; Kameda, K.Y.; Abiko, Y.
Phosphotransacetylase of Escherichia coli B, purification and properties
Biochim. Biophys. Acta
191
550-558
1969
Escherichia coli
Manually annotated by BRENDA team
Suzuki, T.
Phosphotransacetylase of Escherichia coli B, activation by pyruvate and inhibition by NADH and certain nucleotides
Biochim. Biophys. Acta
191
559-569
1969
Escherichia coli
Manually annotated by BRENDA team
Castano-Cerezo, S.; Pastor, J.; Renilla, S.; Bernal, V.; Iborra, J.; Canovas, M.
An insight into the role of phosphotransacetylase (pta) and the acetate/acetyl-CoA node in Escherichia coli
Microb. Cell Fact.
8
54
2009
Escherichia coli, Escherichia coli BW25113
Manually annotated by BRENDA team
Campos-Bermudez, V.A.; Bologna, F.P.; Andreo, C.S.; Drincovich, M.F.
Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation
FEBS J.
277
1957-1966
2010
Escherichia coli (P0A9M8), Escherichia coli
Manually annotated by BRENDA team
Bologna, F.P.; Campos-Bermudez, V.A.; Saavedra, D.D.; Andreo, C.S.; Drincovich, M.F.
Characterization of Escherichia coli EutD: a phosphotransacetylase of the ethanolamine operon
J. Microbiol.
48
629-636
2010
Escherichia coli
Manually annotated by BRENDA team
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