EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.1.3.2 | ATP | holoenzyme, catalytic subunits alone are inhibited | Sulfolobus acidocaldarius | |
2.1.3.2 | CTP | holoenzyme, catalytic subunits alone are inhibited | Sulfolobus acidocaldarius | |
2.1.3.2 | GTP | holoenzyme, catalytic subunits alone are inhibited | Sulfolobus acidocaldarius | |
2.1.3.2 | UTP | holoenzyme, catalytic subunits alone are inhibited | Sulfolobus acidocaldarius |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.3.2 | - |
Sulfolobus acidocaldarius |
2.1.3.2 | expression in Escherichia coli | Sulfolobus acidocaldarius |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.1.3.2 | ATP | inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated | Sulfolobus acidocaldarius | |
2.1.3.2 | CTP | inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated | Sulfolobus acidocaldarius | |
2.1.3.2 | GTP | inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated | Sulfolobus acidocaldarius | |
2.1.3.2 | UTP | inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated | Sulfolobus acidocaldarius |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.3.2 | additional information | - |
additional information | sigmoidal saturation curve for aspartate | Sulfolobus acidocaldarius | |
2.1.3.2 | 0.2 | - |
Carbamoyl phosphate | holoenzyme | Sulfolobus acidocaldarius | |
2.1.3.2 | 0.6 | - |
Carbamoyl phosphate | catalytic subunits | Sulfolobus acidocaldarius |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.1.3.2 | 18000 | - |
6 * 36500 + 6 * 18000, SDS-PAGE | Sulfolobus acidocaldarius |
2.1.3.2 | 36500 | - |
6 * 36500 + 6 * 18000, SDS-PAGE | Sulfolobus acidocaldarius |
2.1.3.2 | 340000 | - |
gel filtration | Sulfolobus acidocaldarius |
2.1.3.2 | 340000 | - |
holoenzyme, gel filtration | Sulfolobus acidocaldarius |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.3.2 | carbamoylphosphate + L-aspartate | Sulfolobus acidocaldarius | - |
phosphate + N-carbamoyl-L-aspartate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.3.2 | Sulfolobus acidocaldarius | - |
- |
- |
2.1.3.2 | Sulfolobus acidocaldarius | Q55338 | catalytic subunit PyrB | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.1.3.2 | - |
Sulfolobus acidocaldarius |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.1.3.2 | 29.95 | - |
at 55°C | Sulfolobus acidocaldarius |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.3.2 | carbamoyl phosphate + L-aspartate | - |
Sulfolobus acidocaldarius | phosphate + N-carbamoyl-L-aspartate | - |
? | |
2.1.3.2 | carbamoylphosphate + L-aspartate | - |
Sulfolobus acidocaldarius | phosphate + N-carbamoyl-L-aspartate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.3.2 | dodecamer | 6 * 36500 + 6 * 18000, SDS-PAGE | Sulfolobus acidocaldarius |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.3.2 | 85 | - |
no loss of activity after 15 min | Sulfolobus acidocaldarius |
2.1.3.2 | 90 | - |
native and recombinant enzyme, loss of less than 10% activity after 40 min | Sulfolobus acidocaldarius |