Cloned (Comment) | Organism |
---|---|
to enable functional assessment of the two-component monooxygenase system in Baeyer-Villiger oxidations, a recombinant plasmid expressing Fred (FMN reductase (NADH)) in tandem with 2,5-DKCMO-encoding gene in Escherichia coli is constructed | Pseudomonas putida |
to enable functional assessment of the two-component monooxygenase system in Baeyer-Villiger oxidations, recombinant plasmids expressing Fred (FMN reductase (NADH)) in tandem with the respective 2,5-DKCMO- and 3,6-DKCMO-encoding genes in Escherichia coli are constructed | Pseudomonas putida |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
40574 | - |
calculated from sequence | Pseudomonas putida |
40702 | - |
calculated from sequence | Pseudomonas putida |
41000 | - |
SDS-PAGE | Pseudomonas putida |
60000 | - |
gel filtration | Pseudomonas putida |
64000 | - |
gel filtration | Pseudomonas putida |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(+)-bornane-2,5-dione + FMNH2 + O2 | Pseudomonas putida | the enzyme is involved in the degradation of (-)-camphor | (+)-5-oxo-1,2-campholide + FMN + H2O | - |
? | |
(+)-bornane-2,5-dione + FMNH2 + O2 | Pseudomonas putida ATCC 17453 | the enzyme is involved in the degradation of (-)-camphor | (+)-5-oxo-1,2-campholide + FMN + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | M5AWY0 | - |
- |
Pseudomonas putida | Q6STM1 | - |
- |
Pseudomonas putida ATCC 17453 | M5AWY0 | - |
- |
Pseudomonas putida ATCC 17453 | Q6STM1 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Pseudomonas putida |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(+)-bornane-2,5-dione + FMNH2 + O2 | the enzyme is involved in the degradation of (-)-camphor | Pseudomonas putida | (+)-5-oxo-1,2-campholide + FMN + H2O | - |
? | |
(+)-bornane-2,5-dione + FMNH2 + O2 | the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system | Pseudomonas putida | (+)-5-oxo-1,2-campholide + FMN + H2O | - |
? | |
(+)-bornane-2,5-dione + FMNH2 + O2 | the enzyme is involved in the degradation of (-)-camphor | Pseudomonas putida ATCC 17453 | (+)-5-oxo-1,2-campholide + FMN + H2O | - |
? | |
(+)-bornane-2,5-dione + FMNH2 + O2 | the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system | Pseudomonas putida ATCC 17453 | (+)-5-oxo-1,2-campholide + FMN + H2O | - |
? | |
(+)-camphor + FMNH2 + O2 | conversion to lactone, no concersion of (-)-camphor | Pseudomonas putida | ? | - |
? | |
(+)-camphor + FMNH2 + O2 | conversion to lactone, no concersion of (-)-camphor | Pseudomonas putida ATCC 17453 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 41000, SDS-PAGE | Pseudomonas putida |
Synonyms | Comment | Organism |
---|---|---|
2,5-diketocamphane monooxygenase | - |
Pseudomonas putida |
2,5-DKCMO-1 | - |
Pseudomonas putida |
2,5-DKCMO-2 | - |
Pseudomonas putida |
camE25-1 | gene name, two isofunctional 2,5-DKCMO genes (camE25-1 for 2,5-DKCMO-1 and camE25-2 for 2,5-DKCMO-2) | Pseudomonas putida |
camE25-2 | gene name, two isofunctional 2,5-DKCMO genes (camE25-1 for 2,5-DKCMO-1 and camE25-2 for 2,5-DKCMO-2) | Pseudomonas putida |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
56 | - |
Tm-value | Pseudomonas putida |
63 | - |
Tm-value | Pseudomonas putida |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Pseudomonas putida |
8 | - |
- |
Pseudomonas putida |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in the degradation of (-)-camphor | Pseudomonas putida |