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Literature summary for 1.5.1.2 extracted from
- Purification, characterization and crystallization of pyrroline-5-carboxylate reductase from the hyperthermophilic archeon Sulfolobus Solfataricus (2009), Protein Expr. Purif., 64, 125-130.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Saccharolobus solfataricus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| diffraction to 3.5 A resolution | Saccharolobus solfataricus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | - |
Saccharolobus solfataricus | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 30000 | - |
x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes | Saccharolobus solfataricus |
| 320000 | - |
gel filtration | Saccharolobus solfataricus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | Q97ZT3 | - |
- |
| Saccharolobus solfataricus P2 | Q97ZT3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Saccharolobus solfataricus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-pyrroline-5-carboxylate + NAD(P)H | - |
Saccharolobus solfataricus | L-proline + NAD(P)+ | - |
r |  |
| 1-pyrroline-5-carboxylate + NAD(P)H | - |
Saccharolobus solfataricus P2 | L-proline + NAD(P)+ | - |
r | |
| L-proline + NAD(P)+ | - |
Saccharolobus solfataricus | 1-pyrroline-5-carboxylate + NAD(P)H | - |
r | |
| L-proline + NAD(P)+ | - |
Saccharolobus solfataricus P2 | 1-pyrroline-5-carboxylate + NAD(P)H | - |
r | |
| L-thioproline + NAD(P)+ | - |
Saccharolobus solfataricus | 1-pyrroline-3-thio-5-carboxylate + NAD(P)H | - |
r | |
| L-thioproline + NAD(P)+ | - |
Saccharolobus solfataricus P2 | 1-pyrroline-3-thio-5-carboxylate + NAD(P)H | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| multimer | x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes | Saccharolobus solfataricus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
stable for at least 30 min | Saccharolobus solfataricus |
| 80 | - |
half-life 30 min | Saccharolobus solfataricus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
reaction rate at pH 9.0 is nearly 3fold higher than at pH 7.0 | Saccharolobus solfataricus |
| 9 | - |
reaction rate is nearly 3fold higher than at pH 7.0 | Saccharolobus solfataricus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | 2fold preference for NADP+ with apparent KM 0.172 mM over NAD+ with apparent KM 0.3896 mM | Saccharolobus solfataricus | |
| NADH | - |
Saccharolobus solfataricus | |
| NADP+ | 2fold preference for NADP+ with apparent KM 0.172 mM over NAD+ with apparent KM 0.3896 mM | Saccharolobus solfataricus | |
| NADPH | - |
Saccharolobus solfataricus | |
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Release 2023.1 (January 2023)
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