Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | required, can be substituted by Fe3+ | Pseudomonas putida | |
Fe3+ | activates and is essential for flavin reductase activity | Pseudomonas putida |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
analysis of flavin reductases in Pseudomonas putida NCIMB 10007, overview | Pseudomonas putida |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(+)-camphor + FMNH2 + O2 | Pseudomonas putida | - |
? + FMN + H2O | - |
? | |
(+)-camphor + FMNH2 + O2 | Pseudomonas putida NCIMB 10007 | - |
? + FMN + H2O | - |
? | |
3,6-diketocamphane + FMNH2 + O2 | Pseudomonas putida | - |
? + NAD+ + H2O | - |
? | |
3,6-diketocamphane + FMNH2 + O2 | Pseudomonas putida NCIMB 10007 | - |
? + NAD+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | - |
- |
- |
Pseudomonas putida NCIMB 10007 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
biooxygenating subunits of both enantiospecific DKCMO isoenzymes to homogeneity by a preparative process involving anion exchange chromatography and ultrafiltration, purification and detection of FMN-reductase activities | Pseudomonas putida |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture condition:camphor-grown cell | growth on (+)-, (-)- and (rac)-camphor. The two DKCMO isoenzymes, 2,5- and 3,6-diketocamphane monooxygenase, are highly selective towards their respective antipodes when serving as substrates for biooxygenation, nevertheless a small but significant cross-inducibility of the enantiomerically redundant DKCMO isoenzyme by both camphor antipodes exists | Pseudomonas putida | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(+)-camphor + FMNH2 + O2 | - |
Pseudomonas putida | ? + FMN + H2O | - |
? | |
(+)-camphor + FMNH2 + O2 | - |
Pseudomonas putida NCIMB 10007 | ? + FMN + H2O | - |
? | |
3,6-diketocamphane + FMNH2 + O2 | - |
Pseudomonas putida | ? + NAD+ + H2O | - |
? | |
3,6-diketocamphane + FMNH2 + O2 | - |
Pseudomonas putida NCIMB 10007 | ? + NAD+ + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 17000-18000, native flavin reductase subunit of the enzyme and flavin reductase FRED, SDS-PAGE | Pseudomonas putida |
Synonyms | Comment | Organism |
---|---|---|
3,6-diketocamphane monooxygenase | - |
Pseudomonas putida |
DKCMO | - |
Pseudomonas putida |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Pseudomonas putida |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Pseudomonas putida |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | dependent on | Pseudomonas putida |
General Information | Comment | Organism |
---|---|---|
evolution | type 2 Baeyer-Villiger monooxygenases (type 2 BVMOs) are a subgroup of the NAD(P)H:FMN-dependent two-component monooxygenases (TCMOs). They can alternatively be classed as a subgroup of the NAD(P)H:FMN-dependent class C flavoprotein monooxygenases | Pseudomonas putida |
physiological function | 2,5- and 3,6-diketocamphane monooxygenase (DKCMO) are two enantiocomplementary isoenzymes that catalyse a key lactone-forming step in the degradation of the (+)- and (-)-camphor antipodes, respectively, in Pseudomonas putida NCIMB 10007. Enzyme 3,6-diketocamphane monooxygenase distributes the flavin nucleotide- and nicotinamide nucleotide-dependent tasks between a homodimeric monooxygenase component and a separate flavin reductase (FR) with unbound FMN, the flavin thus effectively serving as a second substrate to transfer reducing power between the functionally distinct subunits. Various flavin reductases function effectively as sources of the requisite FMNH2 to 3,6-diketocamphane monooxygenase at different times throughout growth on camphor, significant subsequent contribution throughout the mid- to late-exponential phases of growth is also made by the camphor-induced homodimeric 37.0 kDa flavin reductase Fred, possible involvement of camphor-induced putidaredoxin reductase as a contributory activity. Analysis of flavin reductases in Pseudomonas putida NCIMB 10007, overview | Pseudomonas putida |