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3'-dephospho-CoA + acetyl phosphate
acetyl-3'-dephospho-CoA + phosphate
acetyl phosphate + CoA
acetyl-CoA + phosphate
acetyl-CoA + arsenate
CoA + acetyl arsenate
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
acetyl-CoA + phosphate
acetyl Phosphate + CoA
acetyl-CoA + phosphate
CoA + acetyl phosphate
acetyl-phosphate + CoA
acetyl-CoA + phosphate
arsenate + acetyl-CoA
acetyl arsenate + CoA
butyryl-CoA + phosphate
CoA + butyryl phosphate
CoA + acetyl phosphate
acetyl-CoA + phosphate
propionyl-CoA + phosphate
CoA + propionyl phosphate
additional information
?
-
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
-
-
-
?
acetyl phosphate + CoA
acetyl-CoA + phosphate
-
-
-
?
acetyl phosphate + CoA
acetyl-CoA + phosphate
with isoform Pta-2, reaction is irreversible, no acetyl phosphate forming reaction can be detected
-
-
r
acetyl phosphate + CoA
acetyl-CoA + phosphate
-
-
-
-
r
acetyl phosphate + CoA
acetyl-CoA + phosphate
-
-
-
r
acetyl-CoA + arsenate

CoA + acetyl arsenate
-
-
-
-
?
acetyl-CoA + arsenate
CoA + acetyl arsenate
-
-
-
-
?
acetyl-CoA + carnitine

CoA + O-acetylcarnitine
-
-
-
?
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
-
-
-
?
acetyl-CoA + phosphate

acetyl Phosphate + CoA
-
-
-
?
acetyl-CoA + phosphate
acetyl Phosphate + CoA
-
-
-
?
acetyl-CoA + phosphate
acetyl Phosphate + CoA
-
-
-
-
r
acetyl-CoA + phosphate
acetyl Phosphate + CoA
-
-
-
r
acetyl-CoA + phosphate

CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
formation of acetyl-CoA is favored
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
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
-
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
ir
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
ir
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
ir
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
ir
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
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
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
ir
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
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
-
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
?
acetyl-CoA + phosphate
CoA + acetyl phosphate
-
-
-
r
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
-
-
-
?
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
arsenate + acetyl-CoA

acetyl arsenate + CoA
-
-
-
-
?
arsenate + acetyl-CoA
acetyl arsenate + CoA
-
-
-
?
arsenate + acetyl-CoA
acetyl arsenate + CoA
-
-
-
?
butyryl-CoA + phosphate

CoA + butyryl phosphate
-
-
-
-
?
butyryl-CoA + phosphate
CoA + butyryl phosphate
-
at a rate 0.01 as rapid as acetyl-CoA
-
-
?
butyryl-CoA + phosphate
CoA + butyryl phosphate
-
-
-
-
?
CoA + acetyl phosphate

acetyl-CoA + phosphate
-
-
-
r
CoA + acetyl phosphate
acetyl-CoA + phosphate
involved in taurine catabolism
-
-
?
CoA + acetyl phosphate
acetyl-CoA + phosphate
-
-
-
-
r
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
-
-
-
-
?
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
-
-
-
-
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
reaction of EC 2.3.1.222
-
-
?
propionyl-CoA + phosphate
CoA + propionyl phosphate
-
-
-
-
?
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
?
-
-
arsenolysis
-
-
?
additional information
?
-
-
arsenolysis
-
-
?
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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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
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
citrate buffer
-
0.1 M, pH 8.0
CoA
substrate inhibition; substrate inhibition
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
palmitoyl-CoA
-
competitive
Phenylglyoxal
-
33% inhibition after preincubation with phenylglyoxal
potassium diphosphate
-
0.1 M, pH 8.0
potassium phosphate
-
above 10 mM
pyruvate
-
inhibitory at 0.5 mM
Tris(hydroxymethyl)aminomethane
-
weak
(NH4)2SO4

-
above 10 mM
(NH4)2SO4
-
activation at low concentration, inhibition at high concentration
acetyl phosphate

substrate inhibition; substrate inhibition
acetyl-CoA

-
competitive
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
ADP

-
inhibitory at 1 mM
ADP
-
50% inhibition at 6 mM, MgCl2 reverses inhibition
AMP

-
inhibitory at 1 mM
AMP
-
complete loss of activity at 3 mM AMP
arsenate

-
-
arsenate
-
50% inhibition at 10 mM
ATP

-
inhibitory at 1 mM
ATP
-
50% inhibition at 1.5 mM, MgCl2 reverses inhibition
Ba2+

-
15% inhibition at 1 mM, 76% inhibition at 10 mM
Ca2+

-
50% inhibition at 1 mM
coenzyme A

-
competitive
coenzyme A
-
competitive with respect to acetyl-CoA, non competitive with respect to phosphate
coenzyme A
-
strong substrate inhibition
desulfo-CoA

-
competitive
desulfo-CoA
-
strong competitive inhibitor
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
diphosphate

-
non competitive
diphosphate
-
50% inhibition at 12 mM
Li+

-
-
Mg2+

-
-
Mn2+

-
50% inhibition at 1 mM
Mn2+
0.1 microM, 82% residual activity; 0.2 microM, 40% residual activity
N-ethylmaleimide

-
-
N-ethylmaleimide
-
above 0.1 mM
Na+

-
-
Na+
-
acts as inhibitor in the presence of NH4+ or K+, competitive inhibition
NADH

-
potent inhibitor
NADH
-
inhibits by changing enzyme conformation, pyruvate counteracts the inhibitory effect of NADH; inhibits by changing the conformation of the enzyme
p-chloromercuribenzoate

-
-
p-chloromercuribenzoate
-
above 0.1 mM
phosphate

substrate inhibition; substrate inhibition
phosphate
-
inhibition of arsenolysis
phosphate
-
competitive with respect to acyl phosphate, non competitive with respect to CoA
phosphate
-
end product inhibitor
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)
S-dimethylarsino-CoA

-
-
S-dimethylarsino-CoA
-
irreversible inhibition, phosphate protects
SO42-

-
-
additional information

-
overview: product inhibition
-
additional information
-
inhibition by various buffer systems
-
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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0.024 - 22.5
acetyl phosphate
0.04 - 0.15
propionyl-CoA
additional information
additional information
-
0.024
acetyl phosphate

-
-
0.043
acetyl phosphate
-
R87Q mutant
0.073
acetyl phosphate
-
R133Q mutant
0.094
acetyl phosphate
23ưC, pH 7.2, mutant enzyme S309A
0.096
acetyl phosphate
-
25ưC, pH 7.2
0.129
acetyl phosphate
-
30ưC
0.143
acetyl phosphate
23ưC, pH 7.2, mutant enzyme D316E
0.166
acetyl phosphate
-
R287Q mutant
0.17
acetyl phosphate
-
wild tpye
0.175
acetyl phosphate
23ưC, pH 7.2, mutant enzyme S309T
0.18
acetyl phosphate
-
wild-type after expression in E. coli
0.185
acetyl phosphate
23ưC, pH 7.2, wild-type enzyme
0.186
acetyl phosphate
-
25ưC, pH 7.2
0.187
acetyl phosphate
-
C277A mutant
0.191
acetyl phosphate
-
C159S mutant
0.198
acetyl phosphate
-
C312A mutant
0.206
acetyl phosphate
-
C159A mutant
0.222
acetyl phosphate
-
C159A/C277A/C312A/C325A mutant
0.23
acetyl phosphate
-
C325A mutant
0.254
acetyl phosphate
-
C277A/C312A/C325A mutant
0.255
acetyl phosphate
23ưC, pH 7.2, mutant enzyme S309C
0.311
acetyl phosphate
-
-
0.312
acetyl phosphate
-
pH 7.8, 30ưC
0.4
acetyl phosphate
pH 7.6, 55ưC
0.464
acetyl phosphate
pH 7.2, 35ưC, presence of 10fold molar excess of activator PPIB
0.5
acetyl phosphate
pH 7.2, 35ưC
0.531
acetyl phosphate
23ưC, pH 7.2, mutant enzyme R310K
0.59
acetyl phosphate
-
-
0.616
acetyl phosphate
pH 7.2, 35ưC, presence of 10fold molar excess of activator PPIB
0.66
acetyl phosphate
-
-
0.66
acetyl phosphate
-
-
0.775
acetyl phosphate
-
R310Q mutant
0.775
acetyl phosphate
23ưC, pH 7.2, mutant enzyme R310Q
0.9
acetyl phosphate
wild-type, pH 8.0, 30ưC
1
acetyl phosphate
pH 7.2, 35ưC
1.1
acetyl phosphate
mutant Pta-F1, pH 8.0, 30ưC
1.32
acetyl phosphate
-
R28Q mutant
1.7
acetyl phosphate
mutant Pta-F1, pH 8.0, 30ưC
2.4
acetyl phosphate
mutant Pta-F1, pH 8.0, 30ưC
22.5
acetyl phosphate
23ưC, pH 7.2, mutant enzyme R310A
0.0086
acetyl-CoA

-
-
0.0095
acetyl-CoA
-
pH 7.8, 30ưC
0.029
acetyl-CoA
mutant Pta-F1, pH 8.0, 30ưC S0.5-value, Hill constant 2.1
0.039
acetyl-CoA
mutant Pta-F1, pH 8.0, 30ưC, S0.5-value, Hill constant 1.3
0.04
acetyl-CoA
pH 7.6, 55ưC
0.041
acetyl-CoA
pH 7.2, 35ưC, presence of 10fold molar excess of activator PPIB
0.045
acetyl-CoA
wild-type, pH 8.0, 30ưC, S0.5-value, Hill constant 1.3
0.05
acetyl-CoA
pH 7.2, 35ưC
0.058
acetyl-CoA
mutant Pta-F1, pH 8.0, 30ưC, S0.5-value, Hill constant 1.8
0.0638
acetyl-CoA
pH 9.0, 37ưC
0.2812
acetyl-CoA
-
37ưC, pH 7.5, mutant enzyme G273D
0.2812
acetyl-CoA
-
mutant enzyme G273D
0.2814
acetyl-CoA
-
37ưC, pH 7.5, mutant enzyme M294I
0.2814
acetyl-CoA
-
mutant enzyme M294I
0.3293
acetyl-CoA
-
wild-type enzyme
0.3293
acetyl-CoA
-
37ưC, pH 7.5, wild-type enzyme
0.49
acetyl-CoA
pH 7.6, 55ưC
0.5297
acetyl-CoA
-
37ưC, pH 7.5, mutant enzyme R252H
0.5297
acetyl-CoA
-
mutant enzyme R252H
3.36
acetyl-CoA
-
at pH 8.0 and 25ưC
5.97
acetyl-CoA
-
at pH 8.0 and 25ưC
0.03
CoA

-
-
0.0327
CoA
-
pH 7.8, 30ưC
0.037
CoA
23ưC, pH 7.2, mutant enzyme S309T
0.059
CoA
mutant Pta-F1, pH 8.0, 30ưC
0.062
CoA
mutant Pta-F1, pH 8.0, 30ưC
0.065
CoA
-
25ưC, pH 7.2
0.065
CoA
23ưC, pH 7.2, wild-type enzyme
0.066
CoA
mutant Pta-F1, pH 8.0, 30ưC, Hill-constant 1.6
0.067
CoA
23ưC, pH 7.2, mutant enzyme S309A
0.067
CoA
wild-type, pH 8.0, 30ưC, Hill-constatn 1.7
0.073
CoA
-
C159A/C277A/C312A/C325A mutant
0.074
CoA
23ưC, pH 7.2, mutant enzyme D316E
0.086
CoA
-
C277A/C312A/C325A mutant
0.089
CoA
-
wild-type after expression in E. coli
0.094
CoA
23ưC, pH 7.2, mutant enzyme S309C
0.116
CoA
23ưC, pH 7.2, mutant enzyme R310K
0.12
CoA
23ưC, pH 7.2, mutant enzyme R310A
0.13
CoA
pH 7.2, 35ưC, presence of 10fold molar excess of activator PPIB
0.1621
CoA
-
wild-type enzyme
0.1621
CoA
-
37ưC, pH 7.5, wild-type enzyme
0.163
CoA
-
37ưC, pH 7.5, mutant enzyme R252H
0.163
CoA
-
mutant enzyme R252H
0.168
CoA
-
37ưC, pH 7.5, mutant enzyme G273D
0.1683
CoA
-
mutant enzyme G273D
0.185
CoA
23ưC, pH 7.2, mutant enzyme R310Q
0.192
CoA
-
37ưC, pH 7.5, mutant enzyme M294I
0.192
CoA
-
mutant enzyme M294I
0.219
CoA
pH 7.2, 35ưC, presence of 10fold molar excess of activator PPIB
0.8
desulfo-CoA

-
R87E mutant
0.8
desulfo-CoA
-
R133K mutant
1
desulfo-CoA
-
R133E mutant
1.3
desulfo-CoA
-
R87Q mutant
1.3
desulfo-CoA
-
R133A mutant
1.4
desulfo-CoA
-
wild-type
3.9
desulfo-CoA
-
R87K mutant
4
desulfo-CoA
-
R133Q mutant
6
desulfo-CoA
-
R87A mutant
0.111
phosphate

-
-
0.742
phosphate
-
25ưC, pH 7.2
1.1
phosphate
-
37ưC, pH 7.5, mutant enzyme G273D
1.1
phosphate
-
mutant enzyme G273D
1.3
phosphate
-
37ưC, pH 7.5, mutant enzyme M294I
1.3
phosphate
-
mutant enzyme M294I
1.5
phosphate
-
wild-type enzyme
1.5
phosphate
-
37ưC, pH 7.5, wild-type enzyme
1.5
phosphate
mutant Pta-F1, pH 8.0, 30ưC
1.9
phosphate
mutant Pta-F1, pH 8.0, 30ưC
2.1
phosphate
wild-type, pH 8.0, 30ưC
2.8
phosphate
-
37ưC, pH 7.5, mutant enzyme R252H
2.8
phosphate
-
mutant enzyme R252H
3
phosphate
mutant Pta-F1, pH 8.0, 30ưC
11
phosphate
pH 7.2, 35ưC
12.3
phosphate
pH 7.2, 35ưC, presence of 10fold molar excess of activator PPIB
0.04
propionyl-CoA

pH 7.6, 55ưC
additional information
additional information

-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
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, 55ưC
-
additional information
additional information
Km value of butanoyl-CoA 0.02, of propionyl-CoA 0.12 mM, respectively, pH 7.4, 55ưC
-
additional information
additional information
-
Km value of butanoyl-CoA 0.02, of propionyl-CoA 0.12 mM, respectively, pH 7.4, 55ưC
-
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0.15 - 5190
acetyl phosphate
0.00467 - 4.53
desulfo-CoA
1500
phosphate
-
25ưC, pH 7.2
0.21
propionyl-CoA
pH 7.6, 55ưC
additional information
additional information
-
0.15
acetyl phosphate

mutant Pta-F1, pH 8.0, 30ưC
1.32
acetyl phosphate
-
C159A mutant
1.56
acetyl phosphate
mutant Pta-F1, pH 8.0, 30ưC
1.63
acetyl phosphate
-
R310Q mutant
2.16
acetyl phosphate
mutant Pta-F1, pH 8.0, 30ưC
2.65
acetyl phosphate
pH 7.6, 55ưC
3.03
acetyl phosphate
-
C159A/C277A/C312A/C325A mutant
4.93
acetyl phosphate
-
R87Q mutant
5.45
acetyl phosphate
-
mutant R287Q
12.5
acetyl phosphate
-
R133Q mutant
24.1
acetyl phosphate
-
mutant R28Q
40.6
acetyl phosphate
-
wild type
44.5
acetyl phosphate
-
C312A mutant
51.6
acetyl phosphate
-
C277A/C312A/C325A mutant
57.6
acetyl phosphate
-
C325A mutant
66.3
acetyl phosphate
-
C159S mutant
68.5
acetyl phosphate
-
wild-type after expression in E. coli
94.9
acetyl phosphate
-
C277A mutant
227
acetyl phosphate
wild-type, pH 8.0, 30ưC
403.5
acetyl phosphate
-
mutant enzyme M294I
415
acetyl phosphate
-
pH 7.8, 30ưC
574.5
acetyl phosphate
-
wild-type enzyme
1301
acetyl phosphate
-
mutant enzyme G273D
1480
acetyl phosphate
-
mutant enzyme R252H
1500
acetyl phosphate
-
25ưC, pH 7.2
1927
acetyl phosphate
-
30ưC, calculated per monomer
5190
acetyl phosphate
-
25ưC, pH 7.2
0.03
acetyl-CoA

mutant Pta-F1, pH 8.0, 30ưC
0.2
acetyl-CoA
pH 7.6, 55ưC
0.23
acetyl-CoA
mutant Pta-F1, pH 8.0, 30ưC
0.43
acetyl-CoA
mutant Pta-F1, pH 8.0, 30ưC
1.73
acetyl-CoA
-
37ưC, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme
5.18
acetyl-CoA
pH 7.6, 55ưC
25
acetyl-CoA
-
37ưC, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme
29.6
acetyl-CoA
wild-type, pH 8.0, 30ưC
57.9
acetyl-CoA
-
37ưC, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme
57.9
acetyl-CoA
-
mutant enzyme M294I
83.1
acetyl-CoA
-
wild-type enzyme
120
acetyl-CoA
-
pH 7.8, 30ưC
208.9
acetyl-CoA
-
mutant enzyme R252H
252.5
acetyl-CoA
-
37ưC, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme
252.5
acetyl-CoA
-
mutant enzyme G273D
1487
acetyl-CoA
pH 9.0, 37ưC
0.283
CoA

-
R87E mutant
3.3
CoA
-
C159A/C277A/C312A/C325A mutant
6.1
CoA
23ưC, pH 7.2, mutant enzyme S309C
11
CoA
23ưC, pH 7.2, mutant enzyme R310K
14.5
CoA
23ưC, pH 7.2, mutant enzyme S309A
15.4
CoA
23ưC, pH 7.2, mutant enzyme S309T
53.6
CoA
-
C277A/C312A/C325A mutant
69
CoA
23ưC, pH 7.2, mutant enzyme R310Q
87.5
CoA
-
wild-type after expression in E. coli
230
CoA
23ưC, pH 7.2, mutant enzyme R310A
403
CoA
-
37ưC, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme
574.5
CoA
-
37ưC, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme
1301
CoA
-
37ưC, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme
1480
CoA
-
37ưC, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme
2150
CoA
23ưC, pH 7.2, mutant enzyme D316E
5190
CoA
-
25ưC, pH 7.2
5190
CoA
23ưC, pH 7.2, wild-type enzyme
0.00467
desulfo-CoA

-
R133E mutant
0.0125
desulfo-CoA
-
R133A mutant
0.133
desulfo-CoA
-
R133K mutant
0.383
desulfo-CoA
-
R87E mutant
0.467
desulfo-CoA
-
R133Q mutant
0.683
desulfo-CoA
-
R87K mutant
1.63
desulfo-CoA
-
R87Q mutant
3.07
desulfo-CoA
-
R87A mutant
4.53
desulfo-CoA
-
wild-type
additional information
additional information

kcat value of butanoyl-CoA 0.12, of propionyl-CoA 1.14 per s, respectively, pH 7.4, 55ưC
-
additional information
additional information
kcat value of butanoyl-CoA 0.12, of propionyl-CoA 1.14 per s, respectively, pH 7.4, 55ưC
-
additional information
additional information
-
kcat value of butanoyl-CoA 0.12, of propionyl-CoA 1.14 per s, respectively, pH 7.4, 55ưC
-
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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
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
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
-
R133Q

-
altered kinetic properties, increased Km for CoA
R133Q
-
increased Km for CoA, decreased Km for acetyl phosphate
R310Q

-
decreased Km for CoA
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
R87Q

-
altered kinetic properties, increased Km for CoA
R87Q
-
increased Km for CoA, decreased Km for acetyl phosphate
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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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

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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Acetate-activating enzymes of Bradyrhizobium japonicum bacteroids
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-
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Irreversible inhibition of phosphotransacetylase by S-dimethylarsino-CoA
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Purification and properties of phosphotransacetylase from the eucaryotic green alga Chlorogonium elongatum
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-
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Kinetic studies with phosphotransacetylase
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1971
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Kinetic properties of phosphotransacetylase from Veillonella alcalescens
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Purification and properties of phosphotransacetylase from Veillonella alcalescens
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1911-1917
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