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Literature summary extracted from
- Molecular cloning, biochemical and biophysical studies of dihydrodipicolinate reductase of Pseudomonas aeruginosa PAO1 (2011), Int. J. Integr. Biol., 11, 145-152.
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.17.1.8 | expressed in Escherichia coli BL21(DE3) cells | Pseudomonas aeruginosa |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.17.1.8 | 0.05 | - |
NADPH | in 50 mM Tris-HCl, pH 8.0, at 37°C | Pseudomonas aeruginosa |  |
| 1.17.1.8 | 0.065 | - |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate | in 50 mM Tris-HCl, pH 8.0, at 37°C | Pseudomonas aeruginosa | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.17.1.8 | 28000 | - |
4 * 28000, calculated from amino acid sequence | Pseudomonas aeruginosa |
| 1.17.1.8 | 30000 | - |
4 * 30000, His-tagged enzyme, SDS-PAGE | Pseudomonas aeruginosa |
| 1.17.1.8 | 120000 | - |
gel filtration | Pseudomonas aeruginosa |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.17.1.8 | Pseudomonas aeruginosa | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.17.1.8 | Ni-NTA agarose column chromatography | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.1.8 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H+ | - |
Pseudomonas aeruginosa | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD+ + H2O | - |
ir | |
| 1.17.1.8 | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H+ | - |
Pseudomonas aeruginosa | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NADP+ + H2O | - |
ir | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.17.1.8 | homotetramer | 4 * 28000, calculated from amino acid sequence | Pseudomonas aeruginosa |
| 1.17.1.8 | homotetramer | 4 * 30000, His-tagged enzyme, SDS-PAGE | Pseudomonas aeruginosa |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.17.1.8 | DapB | - |
Pseudomonas aeruginosa |
| 1.17.1.8 | DHDPR | - |
Pseudomonas aeruginosa |
| 1.17.1.8 | dihydrodipicolinate reductase | - |
Pseudomonas aeruginosa |
| 1.17.1.8 | EC 1.3.1.26 | formerly | Pseudomonas aeruginosa |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.17.1.8 | 40 | - |
- |
Pseudomonas aeruginosa |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.17.1.8 | 30 | 50 | at 30°C and 50°C, approximately 57% and 85% of the enzymatic activity is retained. Between 50 and 60°C a fast decrease in activity is observed with increasing temperature. Complete loss of activity occurs above 60°C | Pseudomonas aeruginosa |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.17.1.8 | 8 | - |
- |
Pseudomonas aeruginosa |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.17.1.8 | 7 | 9 | at pH 7.0 and 9.0, approyimately 75% and 90% of the enzymatic activity is retained. Below pH 7.0 and above pH 9.0 a significant drop in activity is observed. At pH 11.0 an almost complete loss of activity is observed | Pseudomonas aeruginosa |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.1.8 | NADH | - |
Pseudomonas aeruginosa | |
| 1.17.1.8 | NADPH | - |
Pseudomonas aeruginosa | |
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