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Literature summary for 2.1.3.2 extracted from
- Cooperativity and high pressure: stabilization of the R conformation of the allosteric aspartate transcarbamylase under the influence of pressure (2004), Cell. Mol. Biol., 50, 347-352.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | study of enzyme kinetics under high pressure, in presence of low concentration of L-aspartate, pressure promotes the transition to R-state | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate | significant role of protein-solvent interactions in regulatory conformational changes | Escherichia coli |
apH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
presence of low concentration of L-aspartate | Escherichia coli |
| 8.2 | - |
presence of high concentration of L-aspartate | Escherichia coli |
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Release 2023.1 (January 2023)
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