Activating Compound | Comment | Organism | Structure |
---|---|---|---|
NH4Cl | maximal stimulation at 40 mM, 3fold | Salmonella enterica | |
NH4Cl | 3fold stimulation at 40 mM. No significant increase in activity above 40 mM | Salmonella enterica | |
pyruvate | stimulates activity of wild-type enzyme 0.2fold over control, and the activity of the mutant enzyme R252H 3fold over control | Salmonella enterica | |
pyruvate | stimulates wild-type activity, its effect is potentiated in the variants, being most pronounced on R252H | Salmonella enterica |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Salmonella enterica |
Protein Variants | Comment | Organism |
---|---|---|
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 | Salmonella enterica |
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 | Salmonella enterica |
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 | Salmonella enterica |
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 | Salmonella enterica |
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 | Salmonella enterica |
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 | Salmonella enterica |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NADH | inhibits by changing enzyme conformation, pyruvate counteracts the inhibitory effect of NADH; inhibits by changing the conformation of the enzyme | Salmonella enterica |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.1621 | - |
CoA | wild-type enzyme | Salmonella enterica | |
0.1621 | - |
CoA | 37°C, pH 7.5, wild-type enzyme | Salmonella enterica | |
0.163 | - |
CoA | 37°C, pH 7.5, mutant enzyme R252H | Salmonella enterica | |
0.163 | - |
CoA | mutant enzyme R252H | Salmonella enterica | |
0.168 | - |
CoA | 37°C, pH 7.5, mutant enzyme G273D | Salmonella enterica | |
0.1683 | - |
CoA | mutant enzyme G273D | Salmonella enterica | |
0.192 | - |
CoA | 37°C, pH 7.5, mutant enzyme M294I | Salmonella enterica | |
0.192 | - |
CoA | mutant enzyme M294I | Salmonella enterica | |
0.2812 | - |
acetyl-CoA | 37°C, pH 7.5, mutant enzyme G273D | Salmonella enterica | |
0.2812 | - |
acetyl-CoA | mutant enzyme G273D | Salmonella enterica | |
0.2814 | - |
acetyl-CoA | 37°C, pH 7.5, mutant enzyme M294I | Salmonella enterica | |
0.2814 | - |
acetyl-CoA | mutant enzyme M294I | Salmonella enterica | |
0.3293 | - |
acetyl-CoA | wild-type enzyme | Salmonella enterica | |
0.3293 | - |
acetyl-CoA | 37°C, pH 7.5, wild-type enzyme | Salmonella enterica | |
0.5297 | - |
acetyl-CoA | 37°C, pH 7.5, mutant enzyme R252H | Salmonella enterica | |
0.5297 | - |
acetyl-CoA | mutant enzyme R252H | Salmonella enterica | |
1.1 | - |
phosphate | 37°C, pH 7.5, mutant enzyme G273D | Salmonella enterica | |
1.1 | - |
phosphate | mutant enzyme G273D | Salmonella enterica | |
1.3 | - |
phosphate | 37°C, pH 7.5, mutant enzyme M294I | Salmonella enterica | |
1.3 | - |
phosphate | mutant enzyme M294I | Salmonella enterica | |
1.5 | - |
phosphate | wild-type enzyme | Salmonella enterica | |
1.5 | - |
phosphate | 37°C, pH 7.5, wild-type enzyme | Salmonella enterica | |
2.8 | - |
phosphate | 37°C, pH 7.5, mutant enzyme R252H | Salmonella enterica | |
2.8 | - |
phosphate | mutant enzyme R252H | Salmonella enterica |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
KCl | stimulates | Salmonella enterica | |
KCl | stimulates enzyme activity 2.5-fold | Salmonella enterica |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
490000 | - |
gel filtration | Salmonella enterica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Salmonella enterica | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + phosphate | - |
Salmonella enterica | CoA + acetyl phosphate | - |
? | |
CoA + acetyl phosphate | - |
Salmonella enterica | acetyl-CoA + phosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
hexamer | it is possible that native Pta is a dimer of trimers | Salmonella enterica |
trimer | wild-type enzyme is a trimer. Pta variants formmore hexamer than the wild-typ protein | Salmonella enterica |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.73 | - |
acetyl-CoA | 37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme | Salmonella enterica | |
25 | - |
acetyl-CoA | 37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme | Salmonella enterica | |
57.9 | - |
acetyl-CoA | 37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme | Salmonella enterica | |
57.9 | - |
acetyl-CoA | mutant enzyme M294I | Salmonella enterica | |
83.1 | - |
acetyl-CoA | wild-type enzyme | Salmonella enterica | |
208.9 | - |
acetyl-CoA | mutant enzyme R252H | Salmonella enterica | |
252.5 | - |
acetyl-CoA | 37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme | Salmonella enterica | |
252.5 | - |
acetyl-CoA | mutant enzyme G273D | Salmonella enterica | |
403 | - |
CoA | 37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme | Salmonella enterica | |
403.5 | - |
acetyl phosphate | mutant enzyme M294I | Salmonella enterica | |
574.5 | - |
acetyl phosphate | wild-type enzyme | Salmonella enterica | |
574.5 | - |
CoA | 37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme | Salmonella enterica | |
1301 | - |
CoA | 37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme | Salmonella enterica | |
1301 | - |
acetyl phosphate | mutant enzyme G273D | Salmonella enterica | |
1480 | - |
CoA | 37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme | Salmonella enterica | |
1480 | - |
acetyl phosphate | mutant enzyme R252H | Salmonella enterica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Salmonella enterica |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | 8.5 | pH 7.0: about 50% of maximal activity, pH 8.5: about 60% of maximal activity | Salmonella enterica |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
1.1 | - |
NADH | wild type enzyme | Salmonella enterica | |
1.1 | - |
NADH | 37°C, pH 7.5, wild-type enzyme | Salmonella enterica |