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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
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
0.4
acetyl phosphate
pH 7.6, 55°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
0.04
acetyl-CoA
pH 7.6, 55°C
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
0.0638
acetyl-CoA
pH 9.0, 37°C
0.2812
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme G273D
0.2812
acetyl-CoA
-
mutant enzyme G273D
0.2814
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme M294I
0.2814
acetyl-CoA
-
mutant enzyme M294I
0.3293
acetyl-CoA
-
wild-type enzyme
0.3293
acetyl-CoA
-
37°C, pH 7.5, wild-type enzyme
0.49
acetyl-CoA
pH 7.6, 55°C
0.5297
acetyl-CoA
-
37°C, pH 7.5, mutant enzyme R252H
0.5297
acetyl-CoA
-
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
0.094
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
-
wild-type enzyme
0.1621
CoA
-
37°C, pH 7.5, wild-type enzyme
0.163
CoA
-
37°C, pH 7.5, mutant enzyme R252H
0.163
CoA
-
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
0.192
CoA
-
mutant enzyme M294I
0.219
CoA
pH 7.2, 35°C, 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
-
25°C, pH 7.2
1.1
phosphate
-
37°C, pH 7.5, mutant enzyme G273D
1.1
phosphate
-
mutant enzyme G273D
1.3
phosphate
-
37°C, pH 7.5, mutant enzyme M294I
1.3
phosphate
-
mutant enzyme M294I
1.5
phosphate
-
wild-type enzyme
1.5
phosphate
-
37°C, pH 7.5, 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
2.8
phosphate
-
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
0.04
propionyl-CoA
pH 7.6, 55°C
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, 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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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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Preston, G.G.; Zeiher, C.; Wall, J.D.; Emerich, D.W.
Acetate-activating enzymes of Bradyrhizobium japonicum bacteroids
Appl. Environ. Microbiol.
55
165-170
1989
Bradyrhizobium japonicum
brenda
Stadtman, E.R.
Phosphotransacetylase from Clostridium kluyveri
Methods Enzymol.
1
596-599
1955
Clostridium kluyveri
-
brenda
Bergmeyer, H.U.; Holz, G.; Klotsch, H.; Lang, G.
Phosphotransacetylase aus Clostridium kluyveri
Biochem. Z.
338
114-121
1963
Clostridium kluyveri
brenda
Stadtman, E.R.
The purification and properties of phosphotransacetylase
J. Biol. Chem.
196
527-534
1952
Clostridium kluyveri
brenda
Duhr, E.F.; Owens, M.S.; Barden, R.E.
Irreversible inhibition of phosphotransacetylase by S-dimethylarsino-CoA
Biochim. Biophys. Acta
749
84-90
1983
Clostridium kluyveri
brenda
Kreuzberg, K.; Umlauf, H.; Blaschkowski, H.P.
Purification and properties of phosphotransacetylase from the eucaryotic green alga Chlorogonium elongatum
Biochim. Biophys. Acta
842
22-29
1985
Chlorogonium elongatum
-
brenda
Henkin, J.; Abeles, R.H.
Evidence against an acyl-enzyme intermediate in the reaction catalyzed by clostridial phosphotransacetylase
Biochemistry
15
3472-3479
1976
Clostridium kluyveri
brenda
Kyrtopoulos, S.A.; Satchell, D.P.N.
Kinetic studies with phosphotransacetylase. V. The mechanism of activation by univalent cations
Biochim. Biophys. Acta
321
126-142
1973
Clostridium kluyveri
brenda
Kyrtopoulos, S.A.; Satchell, D.P.N.
Kinetic studies with phosphotransacetylase. II. The acetylation of arsenate by acetyl coenzyme A
Biochim. Biophys. Acta
268
334-343
1972
Clostridium kluyveri
brenda
Hibbert, F.; Kyrtopoulos, S.A.; Satchell, D.P.N.
Kinetic studies with phosphotransacetylase
Biochim. Biophys. Acta
242
39-54
1971
Clostridium kluyveri
brenda
Pelroy, R.A.; Whiteley, H.R.
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
J. Biochem.
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
Bresters, T.W.; Krul, J.; Scheepens, P.C.; Veeger, C.
Phosphotransacetylase associated with the pyruvate dehydrogenase complex from the nitrogen fixing Azotobacter vinelandii
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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
J. Bacteriol.
181
1861-1867
1999
Thermotoga maritima
brenda
Boynton, Z.L.; Bennett, G.N.; Rudolph, F.B.
Cloning, sequencing, and expression of genes encoding phosphotransacetylase and acetate kinase from Clostridium acetobutylicum ATCC 824
Appl. Environ. Microbiol.
62
2758-2766
1996
Clostridium acetobutylicum
brenda
Iyer, P.P.; Ferry, J.G.
Role of arginines in coenzyme A binding and catalysis by the phosphotransacetylase from Methanosarcina thermophila
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183
4244-4250
2001
Methanosarcina thermophila
brenda
Knorr, R.; Ehrmann, M.A.; Vogel, R.F.
Cloning of the phosphotransacetylase gene from Lactobacillus sanfranciscensis and characterization of its gene product
J. Basic Microbiol.
41
339-349
2001
Fructilactobacillus sanfranciscensis
brenda
Latimer, M.T.; Ferry, J.G.
Cloning, sequence analysis, and hyperexpression of the genes encoding phosphotransacetylase and acetate kinase from Methanosarcina thermophila
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175
6822-6829
1993
Methanosarcina thermophila, Methanosarcina thermophila TM-1
brenda
Rasche, M.E.; Smith, K.S.; Ferry, J.G.
Identification of cysteine and arginine residues essential for the phosphotransacetylase from Methanosarcina thermophila
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179
7712-7717
1997
Methanosarcina thermophila
brenda
Shin, B.S.; Choi, S.K.; Park, S.H.
Regulation of the Bacillus subtilis phosphotransacetylase gene
J. Biochem.
126
333-339
1999
Bacillus subtilis
brenda
Summers, M.L.; Denton, M.C.; McDermott, T.R.
Genes coding for phosphotransacetylase and acetate kinase in Sinorhizobium meliloti are in an operon that is inducible by phosphate stress and controlled by PhoB
J. Bacteriol.
181
2217-2224
1999
Sinorhizobium meliloti
brenda
Iyer, P.P.; Lawrence, S.H.; Yennawar, H.P.; Ferry, J.G.
Expression, purification, crystallization and preliminary X-ray analysis of phosphotransacetylase from Methanosarcina thermophila
Acta Crystallogr. Sect. D
59
1517-1520
2003
Methanosarcina thermophila
brenda
Brinsmade, S.R.; Escalante-Semerena, J.C.
The eutD gene of Salmonella enterica encodes a protein with phosphotransacetylase enzyme activity
J. Bacteriol.
186
1890-1892
2004
Salmonella enterica
brenda
Xu, Q.S.; Shin, D.H.; Pufan, R.; Yokota, H.; Kim, R.; Kim, S.H.
Crystal structure of a phosphotransacetylase from Streptococcus pyogenes
Proteins
55
479-481
2004
Streptococcus pyogenes
brenda
Iyer, P.P.; Lawrence, S.H.; Luther, K.B.; Rajashankar, K.R.; Yennawar, H.P.; Ferry, J.G.; Schindelin, H.
Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila
Structure
12
559-567
2004
Methanosarcina thermophila
brenda
Kim, Y.R.; Brinsmade, S.R.; Yang, Z.; Escalante-Semerena, J.; Fierer, J.
Mutation of phosphotransacetylase but not isocitrate lyase reduces the virulence of Salmonella enterica serovar Typhimurium in mice
Infect. Immun.
74
2498-2502
2006
Salmonella enterica
brenda
Lawrence, S.H.; Luther, K.B.; Schindelin, H.; Ferry, J.G.
Structural and functional studies suggest a catalytic mechanism for the phosphotransacetylase from Methanosarcina thermophila
J. Bacteriol.
188
1143-1154
2006
Methanosarcina thermophila (P38503), Methanosarcina thermophila
brenda
Lawrence, S.H.; Ferry, J.G.
Steady-state kinetic analysis of phosphotransacetylase from Methanosarcina thermophila
J. Bacteriol.
188
1155-1158
2006
Methanosarcina thermophila
brenda
Brinsmade, S.R.; Escalante-Semerena, J.C.
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
J. Biol. Chem.
282
12629-12640
2007
Salmonella enterica
brenda
Xu, Q.S.; Jancarik, J.; Lou, Y.; Kuznetsova, K.; Yakunin, A.F.; Yokota, H.; Adams, P.; Kim, R.; Kim, S.H.
Crystal structures of a phosphotransacetylase from Bacillus subtilis and its complex with acetyl phosphate
J. Struct. Funct. Genomics
6
269-279
2005
Bacillus subtilis
brenda
Starai, V.J.; Garrity, J.; Escalante-Semerena, J.C.
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
Microbiology
151
3793-3801
2005
Salmonella enterica (P41790), Salmonella enterica (Q8ZND6), Salmonella enterica
brenda
Gorzynska, A.K.; Denger, K.; Cook, A.M.; Smits, T.H.
Inducible transcription of genes involved in taurine uptake and dissimilation by Silicibacter pomeroyi DSS-3T
Arch. Microbiol.
185
402-406
2006
Ruegeria pomeroyi (Q5LMK3)
brenda
Veit, A.; Rittmann, D.; Georgi, T.; Youn, J.W.; Eikmanns, B.J.; Wendisch, V.F.
Pathway identification combining metabolic flux and functional genomics analyses: acetate and propionate activation by Corynebacterium glutamicum
J. Biotechnol.
140
75-83
2009
Corynebacterium glutamicum
brenda
Castano-Cerezo, S.; Pastor, J.; Renilla, S.; Bernal, V.; Iborra, J.; Canovas, M.
An insight into the role of phosphotransacetylase (pta) and the acetate/acetyl-CoA node in Escherichia coli
Microb. Cell Fact.
8
54
2009
Escherichia coli, Escherichia coli BW25113
brenda
Nemeti, B.; Gregus, Z.
Mechanism of thiol-supported arsenate reduction mediated by phosphorolytic-arsenolytic enzymes: I. The role of arsenolysis
Toxicol. Sci.
110
270-281
2009
Clostridium kluyveri, Methanosarcina thermophila
brenda
Gregus, Z.; Roos, G.; Geerlings, P.; Nemeti, B.
Mechanism of thiol-supported arsenate reduction mediated by phosphorolytic-arsenolytic enzymes: II. Enzymatic formation of arsenylated products susceptible for reduction to arsenite by thiols
Toxicol. Sci.
110
282-292
2009
Methanosarcina thermophila
brenda
Campos-Bermudez, V.A.; Bologna, F.P.; Andreo, C.S.; Drincovich, M.F.
Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation
FEBS J.
277
1957-1966
2010
Escherichia coli (P0A9M8), Escherichia coli
brenda
Bologna, F.P.; Campos-Bermudez, V.A.; Saavedra, D.D.; Andreo, C.S.; Drincovich, M.F.
Characterization of Escherichia coli EutD: a phosphotransacetylase of the ethanolamine operon
J. Microbiol.
48
629-636
2010
Escherichia coli
brenda
Dimou, M.; Venieraki, A.; Liakopoulos, G.; Katinakis, P.
Cloning, characterization and transcriptional analysis of two phosphate acetyltransferase isoforms from Azotobacter vinelandii
Mol. Biol. Rep.
38
3653-3663
2011
Azotobacter vinelandii (C1DER7), Azotobacter vinelandii (C1DQG8), Azotobacter vinelandii
brenda
Dimou, M.; Venieraki, A.; Zografou, C.; Katinakis, P.
The cytoplasmic cyclophilin from Azotobacter vinelandii interacts with phosphate acetyltransferase isoforms enhancing their in vitro activity
Mol. Biol. Rep.
39
4135-4143
2012
Azotobacter vinelandii (C1DER7), Azotobacter vinelandii (C1DQG8), Azotobacter vinelandii
brenda
Kushkevych, I.V.
Activity and kinetic properties of phosphotransacetylase from intestinal sulfate-reducing bacteria
Acta Biochim. Pol.
62
103-108
2015
Desulfovibrio piger, Desulfomicrobium sp., Desulfomicrobium sp. Rod-9, Desulfovibrio piger Vib-7
brenda
Argyros, D.A.; Tripathi, S.A.; Barrett, T.F.; Rogers, S.R.; Feinberg, L.F.; Olson, D.G.; Foden, J.M.; Miller, B.B.; Lynd, L.R.; Hogsett, D.A.; Caiazza, N.C.
High ethanol titers from cellulose by using metabolically engineered thermophilic, anaerobic microbes
Appl. Environ. Microbiol.
77
8288-8294
2011
Acetivibrio thermocellus (O52593), Acetivibrio thermocellus, Acetivibrio thermocellus DSM 1237 (O52593)
brenda
Taylor, T.; Ingram-Smith, C.; Smith, K.S.
Biochemical and Kinetic Characterization of the eukaryotic phosphotransacetylase class IIa enzyme from Phytophthora ramorum
Eukaryot. Cell
14
652-660
2015
Phytophthora ramorum
brenda
Saigo, M.; Golic, A.; Alvarez, C.E.; Andreo, C.S.; Hogenhout, S.A.; Mussi, M.A.; Drincovich, M.F.
Metabolic regulation of phytoplasma malic enzyme and phosphotransacetylase supports the use of malate as an energy source in these plant pathogens
Microbiology
160
2794-2806
2014
Candidatus Phytoplasma
brenda
Patil, Y.; Junghare, M.; Mller, N.
Fermentation of glycerol by Anaerobium acetethylicum and its potential use in biofuel production
Microb. Biotechnol.
10
203-217
2017
Anaerobium acetethylicum
brenda
Breitkopf, R.; Uhlig, R.; Drenckhan, T.; Fischer, R.J.
Two propanediol utilization-like proteins of Moorella thermoacetica with phosphotransacetylase activity
Extremophiles
20
653-661
2016
Moorella thermoacetica (Q2RJ94), Moorella thermoacetica (Q2RK58), Moorella thermoacetica
brenda
Varma, P.; Adimulam, Y.; Subrahmanyam, K.
In silico virtual screening of PubChem compounds against phosphotransacetylase, a putative drug target for Staphylococcus aureus
Int. J. Comput. Biol. Drug Des.
10
39-48
2017
Staphylococcus aureus (Q6GJ80), Staphylococcus aureus MRSA 252 (Q6GJ80)
-
brenda
Yoshida, Y.; Sato, M.; Nonaka, T.; Hasegawa, Y.; Kezuka, Y.
Characterization of the phosphotransacetylase-acetate kinase pathway for ATP production in Porphyromonas gingivalis
J. Oral Microbiol.
11
1588086
2019
Porphyromonas gingivalis (B2RK03), Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277 (B2RK03)
brenda
Yang, X.; Sun, W.; Shen, H.; Zhang, S.; Jiao, X.; Zhao, Z.
Expression of phosphotransacetylase in Rhodosporidium toruloides leading to improved cell growth and lipid production
RSC Adv.
8
24673-24678
2018
Bacillus subtilis
-
brenda