Protein Variants | Comment | Organism |
---|---|---|
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.029 | - |
acetyl-CoA | mutant Pta-F1, pH 8.0, 30°C S0.5-value, Hill constant 2.1 | Escherichia coli | |
0.039 | - |
acetyl-CoA | mutant Pta-F1, pH 8.0, 30°C, S0.5-value, Hill constant 1.3 | Escherichia coli | |
0.045 | - |
acetyl-CoA | wild-type, pH 8.0, 30°C, S0.5-value, Hill constant 1.3 | Escherichia coli | |
0.058 | - |
acetyl-CoA | mutant Pta-F1, pH 8.0, 30°C, S0.5-value, Hill constant 1.8 | Escherichia coli | |
0.059 | - |
CoA | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
0.062 | - |
CoA | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
0.066 | - |
CoA | mutant Pta-F1, pH 8.0, 30°C, Hill-constant 1.6 | Escherichia coli | |
0.067 | - |
CoA | wild-type, pH 8.0, 30°C, Hill-constatn 1.7 | Escherichia coli | |
0.9 | - |
acetyl phosphate | wild-type, pH 8.0, 30°C | Escherichia coli | |
1.1 | - |
acetyl phosphate | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
1.5 | - |
phosphate | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
1.7 | - |
acetyl phosphate | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
1.9 | - |
phosphate | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
2.1 | - |
phosphate | wild-type, pH 8.0, 30°C | Escherichia coli | |
2.4 | - |
acetyl phosphate | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
3 | - |
phosphate | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
77000 | - |
x * 77000, SDS-PAGE, recombinant protein | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A9M8 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl phosphate + CoA | - |
Escherichia coli | acetyl-CoA + phosphate | - |
r | |
acetyl-CoA + phosphate | - |
Escherichia coli | acetyl Phosphate + CoA | - |
r |
Subunits | Comment | Organism |
---|---|---|
? | x * 77000, SDS-PAGE, recombinant protein | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
PTA | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.03 | - |
acetyl-CoA | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
0.15 | - |
acetyl phosphate | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
0.23 | - |
acetyl-CoA | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
0.43 | - |
acetyl-CoA | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
1.56 | - |
acetyl phosphate | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
2.16 | - |
acetyl phosphate | mutant Pta-F1, pH 8.0, 30°C | Escherichia coli | |
29.6 | - |
acetyl-CoA | wild-type, pH 8.0, 30°C | Escherichia coli | |
227 | - |
acetyl phosphate | wild-type, pH 8.0, 30°C | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
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 |