EC Number   |
General Information |
Reference |
|---|
    1.14.14.155 | evolution |
the orientation of the isoalloxazine ring of the FMN cofactor in the active site of the TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a beta-bulge at the C-terminus of beta-strand 3, which is a feature observed in many proteins of this superfamily. Both the 2,5-DKMO and 3,6-DKMO oxygenating components have sequence similarity to bacterial luciferases and bear little similarity to type I Baeyer-Villiger monooxygenase, type I BVMOs |
-, 743943 |
| 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 |
-, 745722 |
| 1.14.14.155 | metabolism |
the enzyme is involved in the camphor-degradation pathway, overview |
-, 743943 |
| 1.14.14.155 | metabolism |
the enzyme is involved in the degradation of (-)-camphor |
-, 746821 |
| 1.14.14.155 | more |
the enzyme is a type II Baeyer-Villiger monooxygenase, enzyme structure modeling, active site structure, overview |
-, 743943 |
| 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 |
-, 745722 |
