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Enzyme Nomenclature
Information on EC 2.3.1.8 - phosphate acetyltransferase
for references in articles please use BRENDA:EC2.3.1.8
Word Map on EC 2.3.1.8
- 2.3.1.8
- methanosarcina
-
acetyl-coenzyme
- thermophila
-
formate-lyase
- acetobutylicum
-
pta-ack
-
acka-pta
- coash
- butyryl-coa
-
2.7.2.1
- acetoin
-
acetate-activating
- tyrobutyricum
-
acetate-grown
- 2,3-butanediol
- sulfoacetaldehyde
- acetylphosphate
-
acetogenic
- phosphotransbutyrylase
-
embden-meyerhof-parnas
- synthesis
- biotechnology
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Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
2.3.1.8
-
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RECOMMENDED NAME
GeneOntology No.
phosphate acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + phosphate = CoA + acetyl phosphate
rapid equilibrium random bi-bi reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
evidence against an acyl-enzyme intermediate; reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
rapid equilibrium random bi-bi reaction mechanism
-
acetyl-CoA + phosphate = CoA + acetyl phosphate
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
Acyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
-
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
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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
-
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 + 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
-
-
-
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
-
-
?
additional information
?
-
-
physiological function in anaerobic metabolism of eukaryotic green algae rather than in aerobic acetate activation
-
-
-
additional information
?
-
carnitine acetyltransferases catalyse the reversible reaction between carnitine and acetyl-CoA to form acetylcarnitine and free CoA. This reaction is important in transferring activated acetyl groups to the mitochondria and in regulating the acetyl-CoA/CoA pools within the cell
-
-
-
additional information
?
-
-
mutation of phosphotransacetylase reduces the virulence of Salmonella enterica serovar typhimurium in mice
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
-
-
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
P41790, Q8ZND6
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
Q5LMK3
involved in taurine catabolism
-
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
P41790, Q8ZND6
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
?
-
P32796
carnitine acetyltransferases catalyse the reversible reaction between carnitine and acetyl-CoA to form acetylcarnitine and free CoA. This reaction is important in transferring activated acetyl groups to the mitochondria and in regulating the acetyl-CoA/CoA pools within the cell
-
-
-
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+
NH4+
Tris
-
maximum activity with Tris buffer, with HEPES and MES catalysis is lowered by ca. 15%
additional information
K+
-
enzyme is inactive in absence of K+ or NH4+, maximal activation at about 0.02 M
K+
-
activates; 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 activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+
K+
-
K+ or NH4+ at concentration above 10 mM required for maximum activity
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
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+
-
enzyme is activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+
additional information
-
no activity with: Fe3+, Zn2+, Mg2+, Co2+, Ni2+, Sn2+, Cu2+, Mo6+, K+, NH4+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-Butanedione
-
almost complete loss of wild-type enzyme activity after 10 min at 10 mM
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-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
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
maxmimum activity in the presence of 1 mM dithiothreitol
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
-
additional information
-
not significant efects: NADH, ATP, phosphoenol pyruvate and aspartate, even at concentrations as high as 10 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; 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
0.2812
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme G273D; mutant enzyme G273D
0.2814
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme M294I; mutant enzyme M294I
0.5297
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme R252H; mutant enzyme R252H
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
-
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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; mutant enzyme M294I
252.5
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme; mutant enzyme G273D
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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 - 8.7
-
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
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
effectively absent in acetate grown cells, also absent in cysteate-grown cells
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus subtilis (strain 168);
Methanosarcina thermophila;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
71000
71300
-
calculated from hydrodynamic radius obtained from dynamic light scattering
76000
77000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
monomer
tetramer
trimer
-
wild-type enzyme is a trimer. Pta variants formmore hexamer than the wild-typ protein
?
-
x * 76000, SDS-PAGE, recombinant protein; x * 77000, SDS-PAGE, recombinant 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
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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
40
-
5 min, 1.5 mg/ml protein concentration, 0.15 M ammonium sulfate, pH 6, stable
45
50
60
80
100
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
-
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
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
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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; gene is expressed during exponential growth on glucose or acetate and is downregulated in the stationary phase
-
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ENGINEERING
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
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
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
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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)
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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
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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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