EC Number   |
Cofactor |
Reference |
|---|
    1.11.1.21 | heme |
- |
439784, 655626, 685401, 686777, 688196, 696108, 698985, 713946, 713949, 714013, 714015, 714115, 714144, 714283, 714289, 714328, 714389, 714890, 715014, 715326, 715337, 715357, 715665, 715812, 715817, 715897, 716245, 716246, 716867, 724571, 725487, 741528, 741761, 741909, 742247, 743032, 743145, 743784, 764804, 764806, 765229, 765406, 765867, 765868 |
| 1.11.1.21 | heme |
1.1 hemes per subunit for wild type KatG |
715806 |
| 1.11.1.21 | heme |
1.2-1.5 hemes per enzyme dimer |
654206 |
| 1.11.1.21 | heme |
a heme-dependent enzyme |
715469 |
| 1.11.1.21 | heme |
binding pocket distal side: triad residues P151, D152, and N153 are important for stability, they interact with the binding pocket proximal side residues W341, D402, and H290 |
654755 |
| 1.11.1.21 | heme |
catalase-peroxidase contains 2 heme molecules per tetramer |
715423 |
| 1.11.1.21 | heme |
determination and analysis of the structure of the heme environment of wild-type KatG and KatG bound to isoniazid, overview. The inactivated pro-drug added to the sample is not perturbing the heme site |
765846 |
| 1.11.1.21 | heme |
docking study with wild-type and mutant enzymes, molecular dynamics, overview |
765180 |
| 1.11.1.21 | heme |
ferric and ferrous KatG show predominant five-coordinate high-spin heme. However, the ferric form shows also small amounts of both six-coordinate high-spin and six-coordinate low-spin, and the ferrous form also exhibits a 6-coordinate low-spin heme |
715812 |
| 1.11.1.21 | heme |
ferric KatP possesses a mixture of pentacoordinate and hexacoordinate high-spin heme iron |
654365 |
