Any feedback?
Literature summary for 1.5.5.2 extracted from
- High yields of active Thermus thermophilus proline dehydrogenase are obtained using maltose-binding protein as a solubility tag (2015), Biotechnol. J., 10, 395-403 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | ProDH is of interest for practical applications because the proline imino acid can serve as a building block for a wide range of peptides and antibiotics | Thermus thermophilus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene TT_C1214, recombinant expression of functional and soluble MBP-tagged enzyme in Escherichia coli TOP10 cells. The MBP tag inhibits the self-association of TtProDH, preventing to a large extent the formation of insoluble protein aggregates | Thermus thermophilus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| GuHCl | enzyme unfolding at 1 M, 0.5 M is not enough for proper unfolding. The fusion protein forms visible aggregates due to unfolding of MBP | Thermus thermophilus |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrial membrane | a membrane-associated protein | Thermus thermophilus | 31966 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the MBP tag inhibits the self-association of TtProDH, preventing to a large extent the formation of insoluble protein aggregates | Thermus thermophilus |
| 78675 | - |
recombinant MBP-tagged enzyme, sequence calculation | Thermus thermophilus |
| 78677 | - |
recombinant MBP-tagged enzyme, mass spectrometry | Thermus thermophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-proline + a quinone | Thermus thermophilus | - |
(S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
| L-proline + a quinone | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | - |
(S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | Q72IB8 | - |
- |
| Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | Q72IB8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant MBP-tagged enzyme from Escherichia coli, gel filtration, and tag cleavage by trypsin, followed by ultrafiltration | Thermus thermophilus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 4 | - |
purified recombinant MBP-tagged enzyme, pH 8.0, 25°C | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-proline + 2,6-dichlorphenol-indophenol | - |
Thermus thermophilus | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
| L-proline + 2,6-dichlorphenol-indophenol | - |
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
| L-proline + a quinone | - |
Thermus thermophilus | (S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
| L-proline + a quinone | a FAD-dependent reaction | Thermus thermophilus | (S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
| L-proline + a quinone | - |
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | (S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
| L-proline + a quinone | a FAD-dependent reaction | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | (S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping | Thermus thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PRODH | - |
Thermus thermophilus |
| TtProDH | - |
Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Thermus thermophilus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
enzyme unfolding experiments using recombinant MBP-tagged enzyme in 20 mM Hepes, pH 8.0, at 60-95°C, the MBP-tagged enzyme unfolds at lower temperature around 56°C due to unfolding of the MBP tag | Thermus thermophilus |
| 90 | - |
with the native enzyme, rapid loss of activity only occurs at temperatures above 90°C | Thermus thermophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Thermus thermophilus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | enzyme-bound, dependent on. Addition of excess FAD hardly improves the enzyme activity, confirming that the enzyme is fully saturated with FAD | Thermus thermophilus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | proline dehydrogenase (ProDH) catalyzes the FAD-dependent oxidation of proline to DELTA1-pyrroline-5-carboxylate, the first step of proline catabolism in many organisms | Thermus thermophilus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
