EC Number   |
Cofactor |
Reference |
|---|
    1.14.13.9 | FAD |
- |
702221, 712322, 726040, 763915, 764027, 764296, 764298, 764520, 764641, 764695, 764728, 764752, 765242, 765266, 765436, 765487, 765643, 765669 |
| 1.14.13.9 | FAD |
4 mol of FAD per subunit |
348516 |
| 1.14.13.9 | FAD |
binding domain at the N-terminus comprising residues 23-166 |
658918 |
| 1.14.13.9 | FAD |
cofactor flavin adenine dinucleotide (FAD) binds to KMO at a 1:1 ratio |
764034 |
| 1.14.13.9 | FAD |
consensus domain sequence, probably FAD-containing |
658919 |
| 1.14.13.9 | FAD |
flavoenzyme |
742082, 742349 |
| 1.14.13.9 | FAD |
flavoprotein |
348514, 348515, 348516, 676975, 743342, 743358 |
| 1.14.13.9 | FAD |
one molecule non-covalently bound FAD per molecule of enzyme |
348531 |
| 1.14.13.9 | more |
KMO has an FAD cofactor, utilizes either NADPH or NADH, releases NADP+ /NAD+ after flavin reduction, and has one dinucleotide-binding domain. Rossmann fold simply characterizes a secondary structure with an alternating motif of beta sheets and alpha helices, and is of importance because this domain non-covalently binds the FAD cofactor and also contains the active site of the enzyme for KMO |
765436 |
| 1.14.13.9 | NADH |
- |
348516, 712322, 765436 |
