HOME
login
history
all enzymes
BRENDA home
History
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:EC2.3.1.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.8 phosphate acetyltransferaseIUBMB Comments
Also acts with other short-chain acyl-CoAs.
Specify your search results
Word Map
- 2.3.1.8
-
acetyl-coenzyme
-
methanosarcina
- thermophila
- formate-lyase
- acetobutylicum
-
pta-ack
- coash
-
acka-pta
- acetoin
-
acetogenic
- butyryl-coa
-
acetate-activating
- tyrobutyricum
-
2.7.2.1
- phosphoketolase
- 2,3-butanediol
-
acetate-grown
- acetylphosphate
- sulfoacetaldehyde
- synthesis
- biotechnology
- biofuel production
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphotransacetylase
PTA
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
(S)-lactate fermentation to propanoate, acetate and hydrogen, acetate and ATP formation from acetyl-CoA I, acetylene degradation (anaerobic), ethanolamine utilization, gallate degradation III (anaerobic), heterolactic fermentation, L-lysine fermentation to acetate and butanoate, methanogenesis from acetate, mixed acid fermentation, purine nucleobases degradation II (anaerobic), pyruvate fermentation to acetate II, pyruvate fermentation to acetate IV, sulfoacetaldehyde degradation I, sulfolactate degradation II, superpathway of fermentation (Chlamydomonas reinhardtii)
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:phosphate acetyltransferase
Also acts with other short-chain acyl-CoAs.
CAS REGISTRY NUMBER
COMMENTARY
9029-91-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
IMAGE
0.029
acetyl-CoA
mutant Pta-F1, pH 8.0, 30°C S0.5-value, Hill constant 2.1
0.039
acetyl-CoA
mutant Pta-F1, pH 8.0, 30°C, S0.5-value, Hill constant 1.3
0.045
acetyl-CoA
wild-type, pH 8.0, 30°C, S0.5-value, Hill constant 1.3
0.058
acetyl-CoA
mutant Pta-F1, pH 8.0, 30°C, S0.5-value, Hill constant 1.8
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of truncated mutants Pta-F1, consisting of the PTA-PTB domains, mutant Pta-F2, consisting of the PTA-PTB domains plus part of the DRTGG motif, and Pta-F3, consisting of the PTA-PTB domains plus the complete DRTGG motif. CD spectra for Pta-F1, Pta-F2 and Pta-F3 are comparable, but not identical, to the spectrum of the entire protein
additional information
-
construction of truncated mutants Pta-F1, consisting of the PTA-PTB domains, mutant Pta-F2, consisting of the PTA-PTB domains plus part of the DRTGG motif, and Pta-F3, consisting of the PTA-PTB domains plus the complete DRTGG motif. CD spectra for Pta-F1, Pta-F2 and Pta-F3 are comparable, but not identical, to the spectrum of the entire protein
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
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
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
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.3.1.8)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
