EC Number |
Cofactor |
Reference |
---|
1.13.11.52 | FMNH2 |
4-5-fold higher activity than acitivity with methylene blue as the electron donor |
663820 |
1.13.11.52 | heme |
- |
395463, 395487, 395491, 395501, 671714, 671990, 672196, 672226, 676893, 684391, 685240, 687116, 687283, 687590, 688457, 695525, 696143, 696151, 696219, 696734, 696944, 698485, 698662, 698952, 699424, 699438, 699473, 699980, 700018, 700604, 710824, 711165, 711218, 711229, 711247, 711422, 711580, 711776, 711952, 712112, 712152, 712172, 712173, 712243, 712250, 712647, 712694, 712821, 712906, 712945, 712947, 713412, 713484, 713591, 723923, 724301, 726383, 741581, 742005, 742073, 742442, 742634, 743005, 743064, 743296, 743716, 765226 |
1.13.11.52 | heme |
0.8 mol of protoheme IX per mol of enzyme |
395459, 395461, 395462 |
1.13.11.52 | heme |
1 mol of heme per mol of monomer |
395478 |
1.13.11.52 | heme |
1.12 mol of heme per mol of enzyme |
395492 |
1.13.11.52 | heme |
2 mol of heme per tetramer |
395478, 395486, 395487 |
1.13.11.52 | heme |
2 molecules of protoheme IV per tetramer |
395498 |
1.13.11.52 | heme |
Ag-HisTDO is purified in its heme-ferric form. The prosthetic group can be fully converted into the heme-ferrous form by treatment with sodium dithionite |
687095 |
1.13.11.52 | heme |
characterization of the heme environment, strong proximal Fe-His bond and strond H-bonding and/or steric interactions between L-Trp and dioxygen in the distal pocket are likely crucial for the enzymatic activity of the recombinant enzyme |
395475 |
1.13.11.52 | heme |
contains 1 mol or more of heme per mol of enzyme |
395455 |