Information on EC 2.3.1.8 - phosphate acetyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.3.1.8
-
RECOMMENDED NAME
GeneOntology No.
phosphate acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + phosphate = CoA + acetyl phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetate fermentation
-
-
acetate formation from acetyl-CoA I
-
-
acetylene degradation
-
-
Carbon fixation pathways in prokaryotes
-
-
gallate degradation III (anaerobic)
-
-
heterolactic fermentation
-
-
L-lysine fermentation to acetate and butanoate
-
-
Metabolic pathways
-
-
Methane metabolism
-
-
methanogenesis from acetate
-
-
Microbial metabolism in diverse environments
-
-
mixed acid fermentation
-
-
Propanoate metabolism
-
-
purine metabolism
-
-
purine nucleobases degradation II (anaerobic)
-
-
pyruvate fermentation to acetate II
-
-
pyruvate fermentation to acetate IV
-
-
Pyruvate metabolism
-
-
sulfoacetaldehyde degradation I
-
-
sulfolactate degradation II
-
-
superpathway of fermentation (Chlamydomonas reinhardtii)
-
-
Taurine and hypotaurine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:phosphate acetyltransferase
Also acts with other short-chain acyl-CoAs.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-91-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
green alga
-
-
Manually annotated by BRENDA team
strain BW25113, wild-type, acs and pta deletion mutants
-
-
Manually annotated by BRENDA team
strain 36, IFO No. 3071
-
-
Manually annotated by BRENDA team
strain 36, IFO No. 3071
-
-
Manually annotated by BRENDA team
strain TM-1
-
-
Manually annotated by BRENDA team
DSS-3
UniProt
Manually annotated by BRENDA team
wild-type and mutant strains
-
-
Manually annotated by BRENDA team
hyperthermophilic eubacterium
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-dephospho-CoA + acetyl phosphate
acetyl-3'-dephospho-CoA + phosphate
show the reaction diagram
acetyl phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
acetyl-CoA + arsenate
CoA + acetyl arsenate
show the reaction diagram
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
-
-
?
acetyl-CoA + phosphate
acetyl Phosphate + CoA
show the reaction diagram
acetyl-CoA + phosphate
CoA + acetyl phosphate
show the reaction diagram
acetyl-phosphate + CoA
acetyl-CoA + phosphate
show the reaction diagram
arsenate + acetyl-CoA
acetyl arsenate + CoA
show the reaction diagram
butyryl-CoA + phosphate
CoA + butyryl phosphate
show the reaction diagram
CoA + acetyl phosphate
acetyl-CoA + phosphate
show the reaction diagram
propionyl-CoA + phosphate
CoA + propionyl phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
CoA + acetyl phosphate
acetyl-CoA + phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
required, Fe2+ or Mn2+, Mn2+ is 50-75% as effective as Fe2+
KCl
-
stimulates; stimulates enzyme activity 2.5-fold
Mn2+
-
required, Fe2+ or Mn2+, Mn2+ is 50-75% as effective as Fe2+
Na+
-
less effective than NH4+ and K+
phosphate
-
1 mM, weak activation
Rb+
-
stimulates
Tris
-
maximum activity with Tris buffer, with HEPES and MES catalysis is lowered by ca. 15%
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
2,2'-dipyridyl
-
-
2,3-Butanedione
-
almost complete loss of wild-type enzyme activity after 10 min at 10 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
acetyl phosphate
acetyl-CoA
AMP
-
inhibitory at 1 mM
arsenate
citrate buffer
-
0.1 M, pH 8.0
CoA
-
substrate inhibition; substrate inhibition
coenzyme A
desulfo-CoA
Diethylbarbiturate
diphosphate
iodoacetamide
-
70% inactivation after 1 min at 5 mM
iodoacetic acid
-
76% inactivation after 4 min at 5 mM
MgCl2
-
activation at low concentration, inhibition at high concentration
N-ethylmaleimide
NADH
-
inhibits by changing enzyme conformation, pyruvate counteracts the inhibitory effect of NADH; inhibits by changing the conformation of the enzyme
p-chloromercuribenzoate
palmitoyl-CoA
-
competitive
Phenylglyoxal
-
33% inhibition after preincubation with phenylglyoxal
phosphate
potassium diphosphate
-
0.1 M, pH 8.0
potassium phosphate
-
above 10 mM
S-Dimethylarsino-CoA
Tris(hydroxymethyl)aminomethane
-
weak
Tris-citrate
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-dimercaptopropanol
-
activates at 0.01 M
cysteine
-
activates at 0.01 M
hydrogen sulfide
-
activates at 0.01 M
NH4Cl
-
3fold stimulation at 40 mM. No significant increase in activity above 40 mM; maximal stimulation at 40 mM, 3fold
PPIB
-
cytoplasmic cytophilin, interaction with phosphate acetyltransferase leads to enhanced activity and alteration in Km value. PPIase activity is not essential for these interactions, as PPIB F99A active site mutant still interacts with phosphate acetyltransferase, but PPIB activity is responsible for the observed phosphate acetyltransferase activity enhancement; cytoplasmic cytophilin, interaction with phosphate acetyltransferase leads to enhanced activity and alteration in Km value. PPIase activity is not essential for these interactions, as PPIB F99A active site mutant still interacts with phosphate acetyltransferase, but PPIB activity is responsible for the observed phosphate acetyltransferase activity enhancement
-
pyruvate
thiolglycolic acid
-
activates at 0.01 M
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
0.024 - 22.5
acetyl phosphate
0.0086 - 0.6
acetyl-CoA
0.058
Butyryl-CoA
-
-
0.03 - 1.694
CoA
0.8 - 6
desulfo-CoA
0.111 - 12.3
phosphate
0.15
propionyl-CoA
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 5190
acetyl phosphate
0.03 - 4500
acetyl-CoA
0.283 - 5190
CoA
0.00467 - 4.53
desulfo-CoA
1500
phosphate
Methanosarcina thermophila
-
25C, pH 7.2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1300
acetyl phosphate
Escherichia coli
-
pH 7.8, 30C
358
12600
acetyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.2 - 12
acetyl phosphate
0.04 - 0.1
CoA
0.001 - 0.02
desulfo-CoA
1.1
NADH
-
37C, pH 7.5, wild-type enzyme; wild type enzyme
0.32 - 19
phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9100
-
after crystallization
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
maximum activity with Tris buffer, with HEPES and MES catalysis is lowered by ca. 15%
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.8
-
90% loss of activity at pH 6.5, 25% loss of activity at pH 7.8
6.6 - 8.2
-
about 50% of activity maximum at pH 6.6 pH and 8.2
6.8 - 8.6
-
pH 6.8: about 25% of activity maximum, pH 8.6: about 90% of activity maximum
7 - 8.7
-
pH 7.0: about 10% of activity maximum, pH 8.7: about 20% of activity maximum
7 - 8.5
-
pH 7.0: about 50% of maximal activity, pH 8.5: about 60% of maximal activity
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
-
both directions
37
-
activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 40
-
only small effect of temperature in this range
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
calculated from the deduced amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
effectively absent in acetate grown cells, also absent in cysteate-grown cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35200
-
calculated from amino acid sequence
35500
-
calculated from amino acid sequence
36200
-
calculated from amino acid sequence
38000 - 41000
-
ultracentrifugation
52000
-
gel filtration
54500
-
gel filtration
63000 - 75000
-
gel filtration
68000
-
gel filtration
70400
-
calculated from the deduced amino acid sequence
71300
-
calculated from hydrodynamic radius obtained from dynamic light scattering
75000 - 80000
-
gel filtration
76000
-
gel filtration
79500
-
gel filtration
88000
-
gel filtration
90000
-
gel filtration
170000
-
gel filtration
280000
-
gel filtration, SDS-PAGE
490000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
monomer
tetramer
trimer
-
wild-type enzyme is a trimer. Pta variants formmore hexamer than the wild-typ protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structures of the enzyme at 2.75 A resolution and its complex with acetyl phosphate at 2.85 A resolution
-
hanging drop vapor diffusion method
-
hanging drop vapor diffusion method. Crystal structures of phosphotransacetylase in complex with the substrate CoA reveals one CoA (CoA(1)) bound in the proposed active site cleft and an additional CoA (CoA(2)) bound at the periphery of the cleft. The crystal structures indicat that binding of CoA(1) is mediated by a series of hydrogen bonds and extensive van der Waals interactions with the enzyme and that there are fewer of these interactions between CoA(2) and the enzyme
hanging-drop vapor diffusion method
-
hanging drop vapor diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, 40C, 5 min, stable
487514
7 - 10
-
stable
487540
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
50% loss of activity within 5 min
37
-
half-life: 20 min
40
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, stable
70
-
5 min, stable up to 70C in absence of additional salts
88
-
60 min, 44% loss of activity
90
-
60% loss of activity after 120 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
(NH4)2SO4, Na2SO4, NaCl or KCl stabilizes
-
50-60% loss of activity after dialysis for 8 h against 0.05 M Tris buffer, Fe2+ and dithiothreitol stabilize
-
activity is lost upon dialysis and cannot be restored by addition of known cofactors or crude boiled extracts
-
ammonium sulfate and potassium phosphate stabilize
-
dilute solutions are instable, in frozen state stable
-
divalent cations, e.g. FeSO4, Fe(NH4)2SO4, MgCl2, MnCl2, MgSO4 or ATP increase lability
-
ethylene glycol 20% v/v stabilizes
-
increased stability is obtained by adding a reducing agent and a component of the reaction
-
labile in dilute solutions or at elevated temperatures
-
lyophilization causes almost complete loss of enzyme activity
-
MgCl2 destabilizes
-
NH4Cl sligthly stabilizes
-
repeated freezing and thawing inactivates
-
stabilized by addition of 200 mM ammonium sulfate and 2-5 mM mercaptans to the extraction buffer
-
sulfate and phosphate partially protect against heat inactivation
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to air
-
487526
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, stable for several months
-
-20C, 0.2 M phosphate or Tris-HCl, pH 8.0, several months
-
-20C, no loss of activity for several weeks
-
-24C, (NH4)2SO4, 50-70% loss of activity after some months
-
0-4C, 2.7-3.0 M ammonium sulfate, months
-
4C or -20C, protein concentration 0.5 mg/ml, several weeks
-
stable for at least 3 h when stored on ice
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, 73% pure
-
apparent homogeneity
-
enzyme is associated with the pyruvate dehydrogenase complex
-
fusion protein with beta-galactosidase
-
homogeneity, biotinylated fusion protein
-
recombinant enzyme from Escherichia coli
-
recombinant protein using His-tag
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)/pSJS1244
-
expressed as His-tag fusion protein in Escherichia coli BL21(lambdaDE3)
-
expressed in Escherichia coli
-
expressed in soluble form in Escherichia coli BL21-DE3
-
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
-
overexpressing CAT2, which encodes the major mitochondrial and peroxisomal carnitine acetyltransferase, on the formation of esters and other flavour compounds during fermentation and overexpression of a modified CAT2 that results in a protein that localizes to the cytosol. The overexpression of both forms of CAT2 resulted in a reduction in ester concentrations, especially in ethyl acetate and isoamyl acetate
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
availabity of ammonium during growth on acetate results in upregulation
-
gene is expressed during exponential growth on glucose or acetate and is downregulated in the stationary phase; gene is expressed during exponential growth on glucose or acetate and is downregulated in the stationary phase
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C159A
-
Km similar to wild-type enzyme
C159A/C277A/C312A/C325A
-
Km similar to wild-type enzyme
C159S
-
Km similar to wild-type enzyme
C277A
-
Km similar to wild-type enzyme
C277A/C312A/C325A
-
Km similar to wild-type enzyme
C312A
-
Km similar to wild-type enzyme
C325A
-
Km similar to wild-type enzyme
D316E
kcat for the reaction of acetyl phosphate and CoA is 2.4fold lower than wild-type value, Km for CoA is 1.1fold higher than wild-type value, Km for acetyl phosphate is 1.4fold lower than wild-type value
R133A
-
altered kinetic properties, increased Km for CoA
R133E
-
altered kinetic properties, increased Km for CoA
R133K
-
altered kinetic properties, increased Km for CoA
R287Q
-
decreased Km for CoA
R28Q
-
increased Km
R310A
kcat for the reaction of acetyl phosphate and CoA is 22.6fold lower than wild-type value, Km for CoA is 1.8fold higher than wild-type value, Km for acetyl phosphate is 122fold higher than wild-type value
R310K
kcat for the reaction of acetyl phosphate and CoA is 472fold lower than wild-type value, Km for CoA is 1.8fold higher than wild-type value, Km for acetyl phosphate is 2.9fold higher than wild-type value
R87A
-
altered kinetic properties, increased Km for CoA
R87E
-
altered kinetic properties, increased Km for CoA
R87K
-
altered kinetic properties, increased Km for CoA
S309A
kcat for the reaction of acetyl phosphate and CoA is 358fold lower than wild-type value, Km for CoA is nearly identical to wild-type value, Km for acetyl phosphate is 1.96fold lower than wild-type value
S309C
kcat for the reaction of acetyl phosphate and CoA is 851fold lower than wild-type value, Km for CoA is1.4 fold higher than wild-type value, Km for acetyl phosphate is 1.4fold higher than wild-type value
S309T
kcat for the reaction of acetyl phosphate and CoA is 337fold lower than wild-type value, Km for CoA is 1.8fold lower than wild-type value, Km for acetyl phosphate is nearly identical to wild-type value
G273D
-
kcat for reaction with acetyl-CoA and phosphate is 3fold higher than wild-type value, kcat for reaction with CoA and acetyl phosphate is 2.3fold higher than wild-type value. Mutant enzyme shows less aggregation than wild type enzyme; kcat/Km for CoA is 2.2fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 3.6fold higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme
M294I
-
kcat for reaction with acetyl-CoA and phosphate is 143fold lower than wild-type value, kcat for reaction with CoA and acetyl phosphate is 1.4fold lower than wild-type value. Mutant enzyme shows less aggregation than wild type enzyme; kcat/Km for CoA is 1.7fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 1.2lower higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme
R252H
-
kcat for reaction with acetyl-CoA and phosphate is 2.5fold higher than wild-type value, kcat for reaction with CoA and acetyl phosphate is 2.5fold higher than wild-type value. No inhibition by NADH. Mutant enzyme shows less aggregation than wild type enzyme; kcat/Km for CoA is 2.6fold higher than wild-type value. kcat/KM for acetoacetyl-CoA is 1.6fold higher than wild-type value. Lower proportion of large enzyme aggregates compared with wild-type enzyme
additional information
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