EC Number | Application | Comment | Organism |
---|---|---|---|
1.5.5.2 | 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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.5.2 | 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 |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.5.5.2 | 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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.5.5.2 | mitochondrial membrane | a membrane-associated protein | Thermus thermophilus | 31966 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | additional information | - |
the MBP tag inhibits the self-association of TtProDH, preventing to a large extent the formation of insoluble protein aggregates | Thermus thermophilus |
1.5.5.2 | 78675 | - |
recombinant MBP-tagged enzyme, sequence calculation | Thermus thermophilus |
1.5.5.2 | 78677 | - |
recombinant MBP-tagged enzyme, mass spectrometry | Thermus thermophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.5.2 | L-proline + a quinone | Thermus thermophilus | - |
(S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
1.5.5.2 | L-proline + a quinone | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | - |
(S)-1-pyrroline-5-carboxylate + a quinol | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.5.2 | Thermus thermophilus | Q72IB8 | - |
- |
1.5.5.2 | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | Q72IB8 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.5.2 | recombinant MBP-tagged enzyme from Escherichia coli, gel filtration, and tag cleavage by trypsin, followed by ultrafiltration | Thermus thermophilus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 4 | - |
purified recombinant MBP-tagged enzyme, pH 8.0, 25°C | Thermus thermophilus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Thermus thermophilus | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + a quinone | - |
Thermus thermophilus | (S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
1.5.5.2 | L-proline + a quinone | a FAD-dependent reaction | Thermus thermophilus | (S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
1.5.5.2 | L-proline + a quinone | - |
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | (S)-1-pyrroline-5-carboxylate + a quinol | - |
? | |
1.5.5.2 | L-proline + a quinone | a FAD-dependent reaction | Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 | (S)-1-pyrroline-5-carboxylate + a quinol | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.5.2 | More | recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping | Thermus thermophilus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.5.2 | PRODH | - |
Thermus thermophilus |
1.5.5.2 | TtProDH | - |
Thermus thermophilus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 25 | - |
assay at | Thermus thermophilus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 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 |
1.5.5.2 | 90 | - |
with the native enzyme, rapid loss of activity only occurs at temperatures above 90°C | Thermus thermophilus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 8 | - |
assay at | Thermus thermophilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.5.2 | 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 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.5.2 | 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 |