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0.024 - 22.5
acetyl phosphate
additional information
additional information
-
0.024
acetyl phosphate

-
-
0.043
acetyl phosphate
-
R87Q mutant
0.073
acetyl phosphate
-
R133Q mutant
0.094
acetyl phosphate
23°C, pH 7.2, mutant enzyme S309A
0.096
acetyl phosphate
-
25°C, pH 7.2
0.129
acetyl phosphate
-
30°C
0.143
acetyl phosphate
23°C, pH 7.2, mutant enzyme D316E
0.166
acetyl phosphate
-
R287Q mutant
0.17
acetyl phosphate
-
wild tpye
0.175
acetyl phosphate
23°C, pH 7.2, mutant enzyme S309T
0.18
acetyl phosphate
-
wild-type after expression in E. coli
0.185
acetyl phosphate
23°C, pH 7.2, wild-type enzyme
0.186
acetyl phosphate
-
25°C, 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
23°C, pH 7.2, mutant enzyme S309C
0.311
acetyl phosphate
-
-
0.312
acetyl phosphate
-
pH 7.8, 30°C
0.464
acetyl phosphate
-
pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB
0.5
acetyl phosphate
-
pH 7.2, 35°C
0.531
acetyl phosphate
23°C, pH 7.2, mutant enzyme R310K
0.59
acetyl phosphate
-
-
0.616
acetyl phosphate
-
pH 7.2, 35°C, 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
23°C, pH 7.2, mutant enzyme R310Q
0.9
acetyl phosphate
wild-type, pH 8.0, 30°C
1
acetyl phosphate
-
pH 7.2, 35°C
1.1
acetyl phosphate
mutant Pta-F1, pH 8.0, 30°C
1.32
acetyl phosphate
-
R28Q mutant
1.7
acetyl phosphate
mutant Pta-F1, pH 8.0, 30°C
2.4
acetyl phosphate
mutant Pta-F1, pH 8.0, 30°C
22.5
acetyl phosphate
23°C, pH 7.2, mutant enzyme R310A
0.0086
acetyl-CoA

-
-
0.0095
acetyl-CoA
-
pH 7.8, 30°C
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
0.05
acetyl-CoA
-
pH 7.2, 35°C
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
0.3293
acetyl-CoA
-
37°C, pH 7.5, wild-type enzyme; wild-type enzyme
0.5297
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme R252H; mutant enzyme R252H
3.36
acetyl-CoA
-
at pH 8.0 and 25°C
5.97
acetyl-CoA
-
at pH 8.0 and 25°C
0.03
CoA

-
-
0.0327
CoA
-
pH 7.8, 30°C
0.037
CoA
23°C, pH 7.2, mutant enzyme S309T
0.059
CoA
mutant Pta-F1, pH 8.0, 30°C
0.062
CoA
mutant Pta-F1, pH 8.0, 30°C
0.065
CoA
23°C, pH 7.2, wild-type enzyme
0.066
CoA
mutant Pta-F1, pH 8.0, 30°C, Hill-constant 1.6
0.067
CoA
23°C, pH 7.2, mutant enzyme S309A
0.067
CoA
wild-type, pH 8.0, 30°C, Hill-constatn 1.7
0.073
CoA
-
C159A/C277A/C312A/C325A mutant
0.074
CoA
23°C, pH 7.2, mutant enzyme D316E
0.086
CoA
-
C277A/C312A/C325A mutant
0.089
CoA
-
wild-type after expression in E. coli
0.093
CoA
-
C159A mutant; C277A mutant
0.094
CoA
23°C, pH 7.2, mutant enzyme S309C
0.116
CoA
23°C, pH 7.2, mutant enzyme R310K
0.12
CoA
23°C, pH 7.2, mutant enzyme R310A
0.13
CoA
-
pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB
0.1621
CoA
-
37°C, pH 7.5, wild-type enzyme; wild-type enzyme
0.163
CoA
-
37°C, pH 7.5, mutant enzyme R252H; mutant enzyme R252H
0.168
CoA
-
37°C, pH 7.5, mutant enzyme G273D
0.1683
CoA
-
mutant enzyme G273D
0.185
CoA
23°C, pH 7.2, mutant enzyme R310Q
0.192
CoA
-
37°C, pH 7.5, mutant enzyme M294I; mutant enzyme M294I
0.219
CoA
-
pH 7.2, 35°C, presence of 10fold molar excess of activator PPIB
0.7
CoA
-
R133E mutant; R133Q mutant
0.8
desulfo-CoA

-
R133K mutant; R87E mutant
1
desulfo-CoA
-
R133E mutant
1.3
desulfo-CoA
-
R133A mutant; R87Q 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
-
25°C, pH 7.2
1.1
phosphate
-
37°C, pH 7.5, mutant enzyme G273D; mutant enzyme G273D
1.3
phosphate
-
37°C, pH 7.5, mutant enzyme M294I; mutant enzyme M294I
1.5
phosphate
-
37°C, pH 7.5, wild-type enzyme; wild-type enzyme
1.5
phosphate
mutant Pta-F1, pH 8.0, 30°C
1.9
phosphate
mutant Pta-F1, pH 8.0, 30°C
2.1
phosphate
wild-type, pH 8.0, 30°C
2.8
phosphate
-
37°C, pH 7.5, mutant enzyme R252H; mutant enzyme R252H
3
phosphate
mutant Pta-F1, pH 8.0, 30°C
11
phosphate
-
pH 7.2, 35°C
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
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
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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
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
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
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Preston, G.G.; Zeiher, C.; Wall, J.D.; Emerich, D.W.
Acetate-activating enzymes of Bradyrhizobium japonicum bacteroids
Appl. Environ. Microbiol.
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Phosphotransacetylase from Clostridium kluyveri
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Clostridium kluyveri
-
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Phosphotransacetylase aus Clostridium kluyveri
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Clostridium kluyveri
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The purification and properties of phosphotransacetylase
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Clostridium kluyveri
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Irreversible inhibition of phosphotransacetylase by S-dimethylarsino-CoA
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84-90
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Clostridium kluyveri
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Purification and properties of phosphotransacetylase from the eucaryotic green alga Chlorogonium elongatum
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Chlorogonium elongatum
-
brenda
Henkin, J.; Abeles, R.H.
Evidence against an acyl-enzyme intermediate in the reaction catalyzed by clostridial phosphotransacetylase
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Clostridium kluyveri
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Kinetic studies with phosphotransacetylase. V. The mechanism of activation by univalent cations
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Clostridium kluyveri
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Kinetic studies with phosphotransacetylase. II. The acetylation of arsenate by acetyl coenzyme A
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1972
Clostridium kluyveri
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Kinetic studies with phosphotransacetylase
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1971
Clostridium kluyveri
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Kinetic properties of phosphotransacetylase from Veillonella alcalescens
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111
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1972
Veillonella parvula
brenda
Whiteley, H.R.; Pelroy, R.A.
Purification and properties of phosphotransacetylase from Veillonella alcalescens
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1911-1917
1972
Veillonella parvula
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Purification of five components from Clostridium thermoaceticum which catalyze synthesis of acetate from pyruvate and methyltetrahydrofolate. Properties of phosphotransacetylase
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256
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1981
Moorella thermoacetica
brenda
Vigenschow, H.; Schwarm, H.M.; Knobloch, K.
Purification and characterization of a phosphotransacetylase from Rhodopseudomonas palustris
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367
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Rhodopseudomonas palustris
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Phosphotransacetylase from Bacillus subtilis: purification and physiological studies
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Bacillus subtilis
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Phosphotransacetylase from Clostridium acidiurici
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Gottschalkia acidurici
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Purification of phosphotransacetylase by affinity chromatography
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95
2-7
1979
Clostridium kluyveri
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Phosphotransacetylase of Escherichia coli B, purification and properties
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550-558
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Escherichia coli
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Phosphotransacetylase of Escherichia coli B, activation by pyruvate and inhibition by NADH and certain nucleotides
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Purification and properties of phosphotransacetylase from Lactobacillus fermenti
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69
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Lactobacillus fermentum, Lactobacillus fermentum DSM 20391
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Purification and characterization of two extremely thermostable enzymes, phosphate acetyltransferase and acetate kinase, from the hyperthermophilic eubacterium Thermotoga maritima
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Expression, purification, crystallization and preliminary X-ray analysis of phosphotransacetylase from Methanosarcina thermophila
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The eutD gene of Salmonella enterica encodes a protein with phosphotransacetylase enzyme activity
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Crystal structure of a phosphotransacetylase from Streptococcus pyogenes
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Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila
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Mutation of phosphotransacetylase but not isocitrate lyase reduces the virulence of Salmonella enterica serovar Typhimurium in mice
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Structural and functional studies suggest a catalytic mechanism for the phosphotransacetylase from Methanosarcina thermophila
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188
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Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila
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brenda
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In vivo and in vitro analyses of single-amino acid variants of the Salmonella enterica phosphotransacetylase enzyme provide insights into the function of its N-terminal domain
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282
12629-12640
2007
Salmonella enterica
brenda
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