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Literature summary for 1.5.5.2 extracted from
- Gene and primary structures of dye-linked L-proline dehydrogenase from the hyperthermophilic archaeon Thermococcus profundus show the presence of a novel heterotetrameric amino acid dehydrogenase complex (2004), Extremophiles, 8, 99-108.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Thermococcus profundus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.5 | - |
L-proline | - |
Thermococcus profundus |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | the alpha-subunit contains the [2Fe-2S] iron-sulfur flavoprotein. The gamma subunit is a typical [8Fe-8S] ferredoxin | Thermococcus profundus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 8000 | - |
alphabetagammadelta, 1 * 54000 + 1 * 43000 + 1 * 19000 + 1 * 8000, the beta-subunit catalyzes the dye-linked L-proline dehydrogenase reaction by itself, the alpha-subunit exhibts dye-linked NADH dehydrogenase activity, SDS-PAGE | Thermococcus profundus |
| 19000 | - |
alphabetagammadelta, 1 * 54000 + 1 * 43000 + 1 * 19000 + 1 * 8000, the beta-subunit catalyzes the dye-linked L-proline dehydrogenase reaction by itself, the alpha-subunit exhibts dye-linked NADH dehydrogenase activity, SDS-PAGE | Thermococcus profundus |
| 43000 | - |
alphabetagammadelta, 1 * 54000 + 1 * 43000 + 1 * 19000 + 1 * 8000, the beta-subunit catalyzes the dye-linked L-proline dehydrogenase reaction by itself, the alpha-subunit exhibts dye-linked NADH dehydrogenase activity, SDS-PAGE | Thermococcus profundus |
| 54000 | - |
alphabetagammadelta, 1 * 54000 + 1 * 43000 + 1 * 19000 + 1 * 8000, the beta-subunit catalyzes the dye-linked L-proline dehydrogenase reaction by itself, the alpha-subunit exhibts dye-linked NADH dehydrogenase activity, SDS-PAGE | Thermococcus profundus |
| 120000 | - |
bifunctional dye-linked L-proline/NADH dehydrogenase complex, gel filtration | Thermococcus profundus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus profundus | Q76M73 | dye-L-proDH beta | - |
| Thermococcus profundus | Q76M76 | dye-L-proDH alpha | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermococcus profundus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.68 | - |
bifunctional dye-linked L-proline/NADH dehydrogenase complex | Thermococcus profundus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-proline + 2,6-dichlorophenolindophenol + H2O | - |
Thermococcus profundus | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| L-proline + ferricyanide + H2O | - |
Thermococcus profundus | (S)-1-pyrroline-5-carboxylate + ferrocyanide | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | alphabetagammadelta, 1 * 54000 + 1 * 43000 + 1 * 19000 + 1 * 8000, the beta-subunit catalyzes the dye-linked L-proline dehydrogenase reaction by itself, the alpha-subunit exhibts dye-linked NADH dehydrogenase activity, SDS-PAGE | Thermococcus profundus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bifunctional dye-linked L-proline/NADH dehydrogenase complex | - |
Thermococcus profundus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
- |
Thermococcus profundus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
10 min, about 90% of the activity remains | Thermococcus profundus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Thermococcus profundus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | 9 | stable | Thermococcus profundus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | 1.96 mol per mol of enzyme complex | Thermococcus profundus | |
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