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Literature summary extracted from

  • 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 (2010), FEBS J., 277, 1957-1966.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.8 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 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.8 0.029
-
 acetyl-CoA mutant Pta-F1, pH 8.0, 30°C S0.5-value, Hill constant 2.1 Escherichia coli
2.3.1.8 0.039
-
 acetyl-CoA mutant Pta-F1, pH 8.0, 30°C, S0.5-value, Hill constant 1.3 Escherichia coli
2.3.1.8 0.045
-
 acetyl-CoA wild-type, pH 8.0, 30°C, S0.5-value, Hill constant 1.3 Escherichia coli
2.3.1.8 0.058
-
 acetyl-CoA mutant Pta-F1, pH 8.0, 30°C, S0.5-value, Hill constant 1.8 Escherichia coli
2.3.1.8 0.059
-
 CoA mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 0.062
-
 CoA mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 0.066
-
 CoA mutant Pta-F1, pH 8.0, 30°C, Hill-constant 1.6 Escherichia coli
2.3.1.8 0.067
-
 CoA wild-type, pH 8.0, 30°C, Hill-constatn 1.7 Escherichia coli
2.3.1.8 0.9
-
 acetyl phosphate wild-type, pH 8.0, 30°C Escherichia coli
2.3.1.8 1.1
-
 acetyl phosphate mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 1.5
-
 phosphate mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 1.7
-
 acetyl phosphate mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 1.9
-
 phosphate mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 2.1
-
 phosphate wild-type, pH 8.0, 30°C Escherichia coli
2.3.1.8 2.4
-
 acetyl phosphate mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 3
-
 phosphate mutant Pta-F1, pH 8.0, 30°C Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.8 77000
-
 x * 77000, SDS-PAGE, recombinant protein Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.8 Escherichia coli P0A9M8
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.8 acetyl phosphate + CoA
-
 Escherichia coli acetyl-CoA + phosphate
-
 r
2.3.1.8 acetyl-CoA + phosphate
-
 Escherichia coli acetyl Phosphate + CoA
-
 r

Subunits

EC Number Subunits Comment Organism
2.3.1.8 ? x * 77000, SDS-PAGE, recombinant protein Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.3.1.8 PTA
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.8 0.03
-
 acetyl-CoA mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 0.15
-
 acetyl phosphate mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 0.23
-
 acetyl-CoA mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 0.43
-
 acetyl-CoA mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 1.56
-
 acetyl phosphate mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 2.16
-
 acetyl phosphate mutant Pta-F1, pH 8.0, 30°C Escherichia coli
2.3.1.8 29.6
-
 acetyl-CoA wild-type, pH 8.0, 30°C Escherichia coli
2.3.1.8 227
-
 acetyl phosphate wild-type, pH 8.0, 30°C Escherichia coli

General Information

EC Number General Information Comment Organism
2.3.1.8 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 Escherichia coli