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Literature summary extracted from
- Multiple native flavin reductases in camphor-metabolizing Pseudomonas putida NCIMB 10007 Functional interaction with two-component diketocamphane monooxygenase isoenzymes (2014), Microbiology, 160, 1783-1794 .
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.155 | Fe2+ | required, can be substituted by Fe3+ | Pseudomonas putida |  |
| 1.14.14.155 | Fe3+ | activates and is essential for flavin reductase activity | Pseudomonas putida | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.155 | additional information | - |
analysis of flavin reductases in Pseudomonas putida NCIMB 10007, overview | Pseudomonas putida |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.155 | (+)-camphor + FMNH2 + O2 | Pseudomonas putida | - |
? + FMN + H2O | - |
? | |
| 1.14.14.155 | (+)-camphor + FMNH2 + O2 | Pseudomonas putida NCIMB 10007 | - |
? + FMN + H2O | - |
? | |
| 1.14.14.155 | 3,6-diketocamphane + FMNH2 + O2 | Pseudomonas putida | - |
? + NAD+ + H2O | - |
? | |
| 1.14.14.155 | 3,6-diketocamphane + FMNH2 + O2 | Pseudomonas putida NCIMB 10007 | - |
? + NAD+ + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.155 | Pseudomonas putida | - |
- |
- |
| 1.14.14.155 | Pseudomonas putida NCIMB 10007 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.155 | 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
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.14.155 | 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 and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.155 | (+)-camphor + FMNH2 + O2 | - |
Pseudomonas putida | ? + FMN + H2O | - |
? | |
| 1.14.14.155 | (+)-camphor + FMNH2 + O2 | - |
Pseudomonas putida NCIMB 10007 | ? + FMN + H2O | - |
? | |
| 1.14.14.155 | 3,6-diketocamphane + FMNH2 + O2 | - |
Pseudomonas putida | ? + NAD+ + H2O | - |
? | |
| 1.14.14.155 | 3,6-diketocamphane + FMNH2 + O2 | - |
Pseudomonas putida NCIMB 10007 | ? + NAD+ + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.14.155 | ? | x * 17000-18000, native flavin reductase subunit of the enzyme and flavin reductase FRED, SDS-PAGE | Pseudomonas putida |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.155 | 3,6-diketocamphane monooxygenase | - |
Pseudomonas putida |
| 1.14.14.155 | DKCMO | - |
Pseudomonas putida |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.155 | 25 | - |
assay at | Pseudomonas putida |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.155 | 7.6 | - |
assay at | Pseudomonas putida |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.155 | FMN | dependent on | Pseudomonas putida | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.14.155 | 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 |
| 1.14.14.155 | 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 |
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