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Literature summary for 1.3.7.7 extracted from
- Overexpression and characterization of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus (2005), Biochim. Biophys. Acta, 1708, 229-237.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Rhodobacter capsulatus mutant DB176 cells | Rhodobacter capsulatus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0106 | - |
protochlorophyllide | in 100 mM HEPES-KOH (pH 7.4), 5 mM MgCl2, 5 mM dithiothreitol, at 34°C | Rhodobacter capsulatus |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 36000 | - |
2 * 36000, S-tag subunit BchL, SDS-PAGE | Rhodobacter capsulatus |
| 36046 | - |
2 * 36046, subunit BchL calculated from amino acid sequence | Rhodobacter capsulatus |
| 48671 | - |
2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence | Rhodobacter capsulatus |
| 52000 | - |
2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE | Rhodobacter capsulatus |
| 57191 | - |
2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence | Rhodobacter capsulatus |
| 60000 | - |
2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE | Rhodobacter capsulatus |
| 67000 | - |
S-tag subunit BchL, gel filtration | Rhodobacter capsulatus |
| 200000 | - |
NB-protein complex, gel filtration | Rhodobacter capsulatus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodobacter capsulatus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| S-protein agarose column chromatography | Rhodobacter capsulatus |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, NB- and L-protein subunits of the crude extract when maintained anaerobically, more than 6 months, remain stable with no significant loss of activity | Rhodobacter capsulatus |
| 4°C, NB- and L-protein subunits of the purified extract when maintained anaerobically, both activities of the components are rapidly lost during purification procedures such as affinity chromatography with S-protein agarose | Rhodobacter capsulatus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protochlorophyllide + oxidized ferredoxin + ADP + phosphate | - |
Rhodobacter capsulatus | chlorophyllide a + reduced ferredoxin + ATP | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterotetramer | 2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence | Rhodobacter capsulatus |
| heterotetramer | 2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE | Rhodobacter capsulatus |
| homodimer | 2 * 36000, S-tag subunit BchL, SDS-PAGE | Rhodobacter capsulatus |
| homodimer | 2 * 36046, subunit BchL calculated from amino acid sequence | Rhodobacter capsulatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dark-operative protochlorophyllide reductase | - |
Rhodobacter capsulatus |
| DPOR | - |
Rhodobacter capsulatus |
| light-independent Pchlide oxidoreductase | - |
Rhodobacter capsulatus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ADP | - |
Rhodobacter capsulatus | |
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Release 2023.1 (January 2023)
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