EC Number   |
Subunits |
Reference |
|---|
    1.14.13.9 | ? |
x * 50000, recombinant enzyme, SDS-PAGE |
-, 676975 |
| 1.14.13.9 | ? |
x * 54000, recombinant soluble enzyme not counting the His-tag, SDS-PAGE |
-, 658919 |
| 1.14.13.9 | ? |
x * 60000, recombinant enzyme, SDS-PAGE |
658918 |
| 1.14.13.9 | dimer |
2 * 160000 in 0.2% Triton-X100, SDS-PAGE |
348516 |
| 1.14.13.9 | homodimer |
- |
765266 |
| 1.14.13.9 | homodimer |
ligand docking and human KMO model construction, overview |
764520 |
| 1.14.13.9 | homodimer |
the rat KMO monomer consists of three domains: alpha + beta flavin adenine dinucleotide (FAD)-binding domain I, FPMO enzyme-conserved domain II containing six-stranded beta-sheets, and C-terminal domain III, which is predicted to be comprising two transmembrane domains, although the exact topology remains ambiguous. The C-terminal region is comprising only one transmembrane domain, with the other predicted transmembrane helix lying laterally along the membrane, this helix displays hydrophobic residues on the outer side |
764520 |
| 1.14.13.9 | More |
structural analysis |
658918 |
| 1.14.13.9 | More |
the C-terminal region is required for the enzymatic activity and functions as a mitochondrial targeting signal |
712322 |
| 1.14.13.9 | More |
the structure of KMO can be realized as three domains: the first domain is where FAD is buried within beta-sheets and alpha-helices, one of which is the long alpha-helix that leads to the C-terminal domain. This helix and a loop that stands above the isoalloxazine rings of FAD define the borders of the active site in this region. The second region contains the residues of alpha-helices and beta-sheets whose side chains set the final border to the active site. Therefore, the active site is contained at the interface of the first and second regions. The third region of PfKMO consists of four alpha-helices while in scKMO and hKMO there are only the two alpha-helices of the transmembrane domain |
765242 |
