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Literature summary for 1.17.2.2 extracted from
- The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida (2003), Biochim. Biophys. Acta, 1647, 110-115.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli, the haemoprotein is present in amorphous inclusion bodies that are isolatable with the cell membranes, followed by centrifugation of the lysed cells | Pseudomonas sp. |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00087 | - |
sparteine | - |
Pseudomonas sp. |  |
| 0.0036 | - |
lupanine | - |
Pseudomonas sp. | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | - |
Pseudomonas sp. | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ba2+ | reactivation requires addition of pyrroloquinoline quinone and is dependent on Ca2+. Sr2+ and Ba2+ are equally competent at reactivating the enzyme in conjunction with pyrroloquinoline quinone. Mg2 + is much less effective | Pseudomonas sp. | |
| Ca2+ | reactivation requires addition of pyrroloquinoline quinone and is dependent on Ca2+. Sr2+ and Ba2+ are equally competent at reactivating the enzyme in conjunction with pyrroloquinoline quinone. Mg2 + is much less effective | Pseudomonas sp. | |
| Sr2+ | reactivation requires addition of pyrroloquinoline quinone and is dependent on Ca2+. Sr2+ and Ba2+ are equally competent at reactivating the enzyme in conjunction with pyrroloquinoline quinone. Mg2 + is much less effective | Pseudomonas sp. | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 66000 | - |
ultracentrifugation studies | Pseudomonas sp. |
| 72000 | - |
1 * 72000, SDS-PAGE | Pseudomonas sp. |
| 72256 | - |
1 * 72256, calculated from sequence | Pseudomonas sp. |
| 74000 | - |
gel filtration | Pseudomonas sp. |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lupanine + pyrroloquinoline quinone + H2O | Pseudomonas sp. | the quinohaemoprotein, contains one covalently bound haem per molecule, the C-terminal domain contains characteristics of a cytochrome c. The haem accepts only one electron, for the two-electron dehydrogenase reaction, a second electron acceptor must be present (pyrroloquinoline quinone) | 17-hydroxylupanine + pyrroloquinoline quinol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas sp. | Q934G0 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | protein sequence has a 26 amino acid signal sequence at the N-terminal for translocation of the protein to the periplasm | Pseudomonas sp. |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pseudomonas sp. |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| expressed in Escherichia coli, procedure is developed to renature and reactivate the enzyme, which is associated with the inclusion bodies. Reactivation requires addition of pyrroloquinoline quinone and is dependent on Ca2+ | Pseudomonas sp. |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| lupanine + pyrroloquinoline quinone + H2O | the quinohaemoprotein, contains one covalently bound haem per molecule, the C-terminal domain contains characteristics of a cytochrome c. The haem accepts only one electron, for the two-electron dehydrogenase reaction, a second electron acceptor must be present (pyrroloquinoline quinone) | Pseudomonas sp. | 17-hydroxylupanine + pyrroloquinoline quinol | - |
? | |
| sparteine + pyrroloquinoline quinone + H2O | - |
Pseudomonas sp. | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 72000, SDS-PAGE | Pseudomonas sp. |
| monomer | 1 * 72256, calculated from sequence | Pseudomonas sp. |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lupanine hydroxylase | - |
Pseudomonas sp. |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 11.8 | - |
sparteine | - |
Pseudomonas sp. | |
| 217 | - |
lupanine | - |
Pseudomonas sp. | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome c | a quinohaemoprotein, contains one covalently bound haem per molecule, the C-terminal domain contains characteristics of a cytochrome c. The heme accepts only one electron, for the two-electron dehydrogenase reaction, a second electron acceptor must be present (pyrroloquinoline quinone) | Pseudomonas sp. | |
| pyrroloquinoline quinone | quinohaemoprotein, contains a molecule of pyrroloquinoline quinone. The heme accepts only one electron, for the two-electron dehydrogenase reaction, a second electron acceptor must be present (pyrroloquinoline quinone) | Pseudomonas sp. | |
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