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Information on EC 2.3.1.8 - phosphate acetyltransferase
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EC Tree
2.3.1.8 phosphate acetyltransferaseIUBMB Comments
Also acts with other short-chain acyl-CoAs.
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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 enzyme appears in viruses and cellular organisms
Synonyms
phosphotransacetylase, phosphate acetyltransferase, pta-1, aywb-pdul, pdul1, pdul2, pta-2, moth_1181, moth_0864, phosphotransacetylase pta, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-S-CoA: orthophosphate acetyltransferase
PGN_1179
phosphate acetyltransferase
phosphotransacetylase
PTA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + phosphate = CoA + acetyl phosphate
reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
evidence against an acyl-enzyme intermediate
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
rapid equilibrium random bi-bi reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
rapid equilibrium random bi-bi reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
ternary complex kinetic echanism rather than a ping-pong kinetic mechanism. Sustrates bind to the enzyme in a random order
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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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)
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:phosphate acetyltransferase
Also acts with other short-chain acyl-CoAs.
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CAS REGISTRY NUMBER
COMMENTARY
9029-91-8
-
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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
3'-dephospho-CoA + acetyl phosphate
acetyl-3'-dephospho-CoA + phosphate
-
rate is about one tenth of the activity with CoA
-
?
3'-dephospho-CoA + acetyl phosphate
acetyl-3'-dephospho-CoA + phosphate
Limosilactobacillus fermentum DSM 20391
-
rate is about one tenth of the activity with CoA
-
?
acetyl phosphate + CoA
acetyl-CoA + phosphate
with isoform Pta-2, reaction is irreversible, no acetyl phosphate forming reaction can be detected
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
formation of acetyl-CoA is favored
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
in reverse reaction specific for CoA
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
in reverse reaction specific for CoA
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
rate of acetyl-CoA synthesis is 10times greater than rate of acetyl phosphate synthesis
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
integral role in acetate metabolism
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
enables growth on acetate as carbon and energy source, required for ethanolamine catabolism
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
rate of acetyl-CoA synthesis is 6.5times greater than rate of acetyl phosphate synthesis
-
r
acetyl-phosphate + CoA
acetyl-CoA + phosphate
-
ternary complex kinetic echanism rather than a ping-pong kinetic mechanism. Sustrates bind to the enzyme in a random order
-
r
butyryl-CoA + phosphate
CoA + butyryl phosphate
-
at a rate 0.01 as rapid as acetyl-CoA
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
involved in taurine catabolism
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities
-
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
-
at a rate 0.1 to 0.5 as rapid as acetyl-CoA
-
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
reaction of EC 2.3.1.222
-
?
additional information
?
-
-
enzymes is confirmed by total proteome analysis of glycerol-grown cells
-
?
additional information
?
-
-
physiological function in anaerobic metabolism of eukaryotic green algae rather than in aerobic acetate activation
-
?
additional information
?
-
enzyme additionally catalyzes reaction with propionyl-CoA, reaction of EC 2.3.1.222, and with butanoyl-CoA, reaction of EC 2.3.1.19
-
-
additional information
?
-
enzyme additionally catalyzes reaction with propionyl-CoA, reaction of EC 2.3.1.222, and with butanoyl-CoA, reaction of EC 2.3.1.19
-
-
additional information
?
-
-
enzyme additionally catalyzes reaction with propionyl-CoA, reaction of EC 2.3.1.222, and with butanoyl-CoA, reaction of EC 2.3.1.19
-
-
additional information
?
-
no substrates: butanoyl-CoA, acetyl phosphate
-
-
additional information
?
-
no substrates: butanoyl-CoA, acetyl phosphate
-
-
additional information
?
-
-
no substrates: butanoyl-CoA, acetyl phosphate
-
-
additional information
?
-
-
mutation of phosphotransacetylase reduces the virulence of Salmonella enterica serovar typhimurium in mice
-
?
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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
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
integral role in acetate metabolism
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
enables growth on acetate as carbon and energy source, required for ethanolamine catabolism
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities
-
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
involved in taurine catabolism
-
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities
-
-
?
additional information
?
-
-
physiological function in anaerobic metabolism of eukaryotic green algae rather than in aerobic acetate activation
-
-
?
additional information
?
-
-
mutation of phosphotransacetylase reduces the virulence of Salmonella enterica serovar typhimurium in mice
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
KCl
NH4+
Tris
-
maximum activity with Tris buffer, with HEPES and MES catalysis is lowered by ca. 15%
additional information
K+
-
enzyme is activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+
K+
-
rate of arsenolysis increases with increasing potassium or ammonium salt concentration and reaches a maximum rate at 0.02 to 0.03 M salt concentration
K+
-
enzyme is inactive in absence of K+ or NH4+, maximal activation at about 0.02 M
K+
-
K+ or NH4+ at concentration above 10 mM required for maximum activity
NH4+
-
enzyme is activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+
NH4+
-
rate of arsenolysis increases with increasing potassium or ammonium salt concentration and reaches a maximum rate at 0.02 to 0.03 M salt concentration
NH4+
-
K+ or NH4+ at concentration above 10 mM required for maximum activity, enzyme is inactive in absence of K+ or NH4+, maximal activation at about 0.02 M
additional information
-
no activity with: Fe3+, Zn2+, Mg2+, Co2+, Ni2+, Sn2+, Cu2+, Mo6+, K+, NH4+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-Butanedione
-
almost complete loss of wild-type enzyme activity after 10 min at 10 mM
2-[(1S)-1-[(N-acetyl-L-alanyl)amino]ethyl]-1,3-oxazol-5-yl diphenyl phosphate
inhibitor identified by in silico screening, dock score -191.515 kcal/mol
MgCl2
-
activation at low concentration, inhibition at high concentration
Phenylglyoxal
-
33% inhibition after preincubation with phenylglyoxal
(NH4)2SO4
-
activation at low concentration, inhibition at high concentration
acetyl phosphate
substrate inhibition; substrate inhibition
acetyl-CoA
-
competitive inhibitor versus CoA when acetyl phosphate is at subsaturating levels but it does not inhibit versus CoA when acetyl phosphate is at saturating levels. Acetyl-CoA is a competitive inhibitor versus acetyl phosphate when CoA is at subsaturating levels but it does not inhibit versus acetyl phosphate when CoA is at saturating levels
coenzyme A
-
competitive with respect to acetyl-CoA, non competitive with respect to phosphate
desulfo-CoA
-
competitive inhibitor with respect to CoA, noncompetitive inhibitor with respect to acetyl phosphate
Diethylbarbiturate
-
potassium diethylbarbiturate buffer, 0.1 M, pH 8.0
Mn2+
0.1 microM, 82% residual activity; 0.2 microM, 40% residual activity
Na+
-
acts as inhibitor in the presence of NH4+ or K+, competitive inhibition
NADH
-
inhibits by changing enzyme conformation, pyruvate counteracts the inhibitory effect of NADH; inhibits by changing the conformation of the enzyme
phosphate
-
competitive with respect to acyl phosphate, non competitive with respect to CoA
phosphate
-
competitive inhibitor versus acetyl phosphate when CoA is at saturating or subsaturating levels. Phosphate is a noncompetitive inhibitor versus CoA when acetyl phosphate is at a subsaturating level (0.15 mM), but it does not inhibit versus CoA when acetyl phosphate is at a saturating level (4 mM)
additional information
-
fructose-1,6-bisphosphate (1 mM), oxaloacetate (1 mM), 2-oxoglutarate (1.5 mM), and citrate (1.5 mM) have no effect on enzyme activity
-
additional information
in silico virtual screening of PubChem compounds with enhanced binding energies when compared with acetyl phosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
maxmimum activity in the presence of 1 mM dithiothreitol
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
-
additional information
-
not significant efects: NADH, ATP, phosphoenol pyruvate and aspartate, even at concentrations as high as 10 mM
-
NH4Cl
-
3fold stimulation at 40 mM. No significant increase in activity above 40 mM
pyruvate
-
isoform PtaII has 133% activity in the presence of 0.05 mM pyruvate
pyruvate
-
stimulates activity of wild-type enzyme 0.2fold over control, and the activity of the mutant enzyme R252H 3fold over control
pyruvate
-
stimulates wild-type activity, its effect is potentiated in the variants, being most pronounced on R252H
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.464
acetyl phosphate
pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB
0.616
acetyl phosphate
pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB
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
0.041
acetyl-CoA
pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB
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
0.13
CoA
pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB
0.219
CoA
pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB
12.3
phosphate
pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB
additional information
additional information
-
effects of monovalent kations
-
additional information
additional information
Km value of butanoyl-CoA 0.02, of propionyl-CoA 0.12 mM, respectively, pH 7.4, 55°C
-
additional information
additional information
Km value of butanoyl-CoA 0.02, of propionyl-CoA 0.12 mM, respectively, pH 7.4, 55°C
-
additional information
additional information
-
Km value of butanoyl-CoA 0.02, of propionyl-CoA 0.12 mM, respectively, pH 7.4, 55°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.73
acetyl-CoA
-
37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme
25
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme
57.9
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme
252.5
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme
403
CoA
-
37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme
574.5
CoA
-
37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme
1301
CoA
-
37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme
1480
CoA
-
37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme
additional information
additional information
kcat value of butanoyl-CoA 0.12, of propionyl-CoA 1.14 per s, respectively, pH 7.4, 55°C
-
additional information
additional information
kcat value of butanoyl-CoA 0.12, of propionyl-CoA 1.14 per s, respectively, pH 7.4, 55°C
-
additional information
additional information
-
kcat value of butanoyl-CoA 0.12, of propionyl-CoA 1.14 per s, respectively, pH 7.4, 55°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kcat/Km value of butanoyl-CoA 6.68, of propionyl-CoA 9.26 per s and mM, respectively, pH 7.4, 55°C
-
additional information
additional information
kcat/Km value of butanoyl-CoA 6.68, of propionyl-CoA 9.26 per s and mM, respectively, pH 7.4, 55°C
-
additional information
additional information
-
kcat/Km value of butanoyl-CoA 6.68, of propionyl-CoA 9.26 per s and mM, respectively, pH 7.4, 55°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0028
desulfo-CoA
-
25°C, pH 7.2, with respect to acetyl phosphate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activities of recombinant plasmids expressed in Escherichia coli and Clostridium acetobutylicum
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
7.8
additional information
-
maximum activity with Tris buffer, with HEPES and MES catalysis is lowered by ca. 15%
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.8
-
90% loss of activity at pH 6.5, 25% loss of activity at pH 7.8
6.8 - 8.6
-
pH 6.8: about 25% of activity maximum, pH 8.6: about 90% of activity maximum
7 - 8.5
-
pH 7.0: about 50% of maximal activity, pH 8.5: about 60% of maximal activity
7 - 8.7
-
pH 7.0: about 10% of activity maximum, pH 8.7: about 20% of activity maximum
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 35
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
effectively absent in acetate grown cells, also absent in cysteate-grown cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
physiological function
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
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
the phosphotransacetylase Pta and acetate kinase Ack genes are tandemly located in the genome, and are cotranscribed as an operon. Inactivation of Pta or Ack by homologous recombination is successful only when the inactivated gene is expressed in trans
physiological function
-
the phosphotransacetylase Pta and acetate kinase Ack genes are tandemly located in the genome, and are cotranscribed as an operon. Inactivation of Pta or Ack by homologous recombination is successful only when the inactivated gene is expressed in trans
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus subtilis (strain 168)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
71000
71300
-
calculated from hydrodynamic radius obtained from dynamic light scattering
76000
77000
90000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
monomer
tetramer
trimer
-
wild-type enzyme is a trimer. Pta variants formmore hexamer than the wild-typ protein
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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. 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
to 2.04 A resolution. An acetyl-CoA molecule binds to each subunit of the dimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
R133Q
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
R310Q
R87Q
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
G300A
-
the mutant of isoform PtaII shows reduced activity compared to the wild type enzyme
G300D
-
the mutant of isoform PtaII shows reduced activity compared to the wild type enzyme
D309A
complete loss of activity, mutation does not affect the dimerization
D318A
complete loss of activity, mutant displays a broad biphasic pattern in gel filtration
R135A
21% decrease in specific activity, mutation does not affect the dimerization
R312A
complete loss of activity, mutation does not affect the dimerization
R89A
58% decrease in specific activity, mutation does not affect the dimerization
S311A
complete loss of activity, mutation does not affect the dimerization
D318A
-
complete loss of activity, mutant displays a broad biphasic pattern in gel filtration
R135A
-
21% decrease in specific activity, mutation does not affect the dimerization
R312A
-
complete loss of activity, mutation does not affect the dimerization
R89A
-
58% decrease in specific activity, mutation does not affect the dimerization
S311A
-
complete loss of activity, mutation does not affect the dimerization
G273D
M294I
R252H
additional information
R310Q
kcat for the reaction of acetyl phosphate and CoA is 75.2fold lower than wild-type value, Km for CoA is 2.8fold higher than wild-type value, Km for acetyl phosphate is 4.2fold higher than 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
G273D
-
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
M294I
-
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
R252H
-
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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, 40°C, 5 min, stable
487514
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
40
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, stable
45
50
60
80
additional information
45
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, 15% loss of activity
50
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, 48% loss of activity
60
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, 98% loss of activity
60
-
pH 8.0, 50 mM Tris/HCl, complete loss of activity after 1 min
additional information
-
sulfate and phosphate partially protect against heat inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
divalent cations, e.g. FeSO4, Fe(NH4)2SO4, MgCl2, MnCl2, MgSO4 or ATP increase lability
-
increased stability is obtained by adding a reducing agent and a component of the reaction
-
lyophilization causes almost complete loss of enzyme activity
-
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
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein using His-tag
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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)
-
expression in Escherichia coli
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
-
proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
biotechnology
synthesis
biotechnology
genetic tools for use in Clostridium thermocellum that allow creation of unmarked mutations while using a replicating plasmid. The strategy employs counter-selections developed from the native Clostridium thermocellum hpt gene and the Thermoanaerobacterium saccharolyticum tdk gene and is used to delete the genes for both lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta)
biotechnology
-
genetic tools for use in Clostridium thermocellum that allow creation of unmarked mutations while using a replicating plasmid. The strategy employs counter-selections developed from the native Clostridium thermocellum hpt gene and the Thermoanaerobacterium saccharolyticum tdk gene and is used to delete the genes for both lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta)
synthesis
a lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta) deletion strain is evolved for 2,000 h, resulting in a stable strain with 40:1 ethanol selectivity and a 4.2-fold increase in ethanol yield over the wild-type strain. In a coculture of organic acid-deficient engineered strains of both Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, fermentation of 92 g/liter Avicel results in 38 g/liter ethanol, with acetic and lactic acids below detection limits, in 146 h. engineering is based on a phosphoribosyl transferase (Hpt) deletion strain, which produces acetate, lactate, and ethanol in a ratio of 1.7:1.5:1.0, similar to the 2.1:1.9:1.0 ratio produced by the wild type. The Hpt/Ldh double mutant strain does not produce significant levels of lactate and has a 1.4:1.0 ratio of acetate to ethanol. Similarly, the Hpt/Pta double mutant strain does not produce acetate and has a 1.9:1.0 ratio of lactate to ethanol. The Hpt/Ldh/Pta triple mutant strain achieves ethanol selectivity of 40:1 relative to organic acids
synthesis
-
overexpression of phosphotransacetylase in the yeast Rhodosporidium toruloides for enhanced cell growth and lipid production. Compared with the parental strain, the engineered strain shows significant improvement in glucose consumption, cell growth and lipid accumulation when cultivated under nitrogen limited conditions in an Erlenmeyer flask as well as a stirred tank bioreactor. The phosphotransacetylase enzyme has little direct effects on the enzymes of fatty acid biosynthetic pathway, but might facilitate the fatty acid precursor acetyl-CoA supply
synthesis
-
a lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta) deletion strain is evolved for 2,000 h, resulting in a stable strain with 40:1 ethanol selectivity and a 4.2-fold increase in ethanol yield over the wild-type strain. In a coculture of organic acid-deficient engineered strains of both Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, fermentation of 92 g/liter Avicel results in 38 g/liter ethanol, with acetic and lactic acids below detection limits, in 146 h. engineering is based on a phosphoribosyl transferase (Hpt) deletion strain, which produces acetate, lactate, and ethanol in a ratio of 1.7:1.5:1.0, similar to the 2.1:1.9:1.0 ratio produced by the wild type. The Hpt/Ldh double mutant strain does not produce significant levels of lactate and has a 1.4:1.0 ratio of acetate to ethanol. Similarly, the Hpt/Pta double mutant strain does not produce acetate and has a 1.9:1.0 ratio of lactate to ethanol. The Hpt/Ldh/Pta triple mutant strain achieves ethanol selectivity of 40:1 relative to organic acids
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REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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The purification and properties of phosphotransacetylase
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196
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Irreversible inhibition of phosphotransacetylase by S-dimethylarsino-CoA
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749
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Clostridium kluyveri
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-
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Evidence against an acyl-enzyme intermediate in the reaction catalyzed by clostridial phosphotransacetylase
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15
3472-3479
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Clostridium kluyveri
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Kinetic studies with phosphotransacetylase. V. The mechanism of activation by univalent cations
Biochim. Biophys. Acta
321
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1973
Clostridium kluyveri
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Kinetic studies with phosphotransacetylase. II. The acetylation of arsenate by acetyl coenzyme A
Biochim. Biophys. Acta
268
334-343
1972
Clostridium kluyveri
brenda
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Kinetic studies with phosphotransacetylase
Biochim. Biophys. Acta
242
39-54
1971
Clostridium kluyveri
brenda
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Kinetic properties of phosphotransacetylase from Veillonella alcalescens
J. Bacteriol.
111
47-55
1972
Veillonella parvula
brenda
Whiteley, H.R.; Pelroy, R.A.
Purification and properties of phosphotransacetylase from Veillonella alcalescens
J. Biol. Chem.
247
1911-1917
1972
Veillonella parvula
brenda
Drake, H.L.; Hu, S.I.; Wood, H.G.
Purification of five components from Clostridium thermoaceticum which catalyze synthesis of acetate from pyruvate and methyltetrahydrofolate. Properties of phosphotransacetylase
J. Biol. Chem.
256
11137-11144
1981
Moorella thermoacetica
brenda
Vigenschow, H.; Schwarm, H.M.; Knobloch, K.
Purification and characterization of a phosphotransacetylase from Rhodopseudomonas palustris
Biol. Chem. Hoppe-Seyler
367
957-962
1986
Rhodopseudomonas palustris
brenda
Lundie, L.L.; Ferry, J.G.
Activation of acetate by Methanosarcina thermophila. Purification and characterization of phosphotransacetylase
J. Biol. Chem.
264
18392-18396
1989
Methanosarcina thermophila
brenda
Rado, T.A.; Hoch, J.A.
Phosphotransacetylase from Bacillus subtilis: purification and physiological studies
Biochim. Biophys. Acta
321
114-125
1973
Bacillus subtilis
brenda
Robinson, J.R.; Sagers, R.D.
Phosphotransacetylase from Clostridium acidiurici
J. Bacteriol.
112
465-473
1972
Gottschalkia acidurici
brenda
Smith, L.T.; Kaplan, N.O.
Purification of phosphotransacetylase by affinity chromatography
Anal. Biochem.
95
2-7
1979
Clostridium kluyveri
brenda
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
brenda
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
brenda
Nojiri, T.; Tanaka, F.; Nakayama, I.
Purification and properties of phosphotransacetylase from Lactobacillus fermenti
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69
789-801
1971
Limosilactobacillus fermentum, Limosilactobacillus fermentum DSM 20391
brenda
Kyrtopoulos, S.A.; Satchell, D.P.N.
Kinetic studies with phosphotransacetylase. 3. The acylation of phosphate ions by acetyl coenzyme A
Biochim. Biophys. Acta
276
376-382
1972
Clostridium kluyveri
brenda
Kyrtopoulos, S.A.; Satchell, D.P.N.
Kinetic studies with phosphotransacetylase. IV. Inhibition by products
Biochim. Biophys. Acta
276
383-391
1972
Clostridium kluyveri
brenda
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Phosphotransacetylase associated with the pyruvate dehydrogenase complex from the nitrogen fixing Azotobacter vinelandii
FEBS Lett.
22
305-309
1972
Azotobacter vinelandii
brenda
Bock, A.K.; Glasemacher, J.; Schmidt, R.; Schonheit, P.
Purification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima
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181
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1999
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brenda
Boynton, Z.L.; Bennett, G.N.; Rudolph, F.B.
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62
2758-2766
1996
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brenda
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183
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2001
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brenda
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41
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Genes coding for phosphotransacetylase and acetate kinase in Sinorhizobium meliloti are in an operon that is inducible by phosphate stress and controlled by PhoB
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Expression, purification, crystallization and preliminary X-ray analysis of phosphotransacetylase from Methanosarcina thermophila
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59
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2003
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brenda
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The eutD gene of Salmonella enterica encodes a protein with phosphotransacetylase enzyme activity
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