EC Number   |
Cofactor |
Reference |
|---|
   1.4.9.1 | heme c |
two heme c cofactors mediate the transfer of the substrate-derived electrons from cysteine tryptophylquinone to an external electron acceptor |
654676 |
| 1.4.9.1 | pyrroloquinoline quinone |
covalently bound |
396571 |
| 1.4.9.1 | quinoid cofactor |
alpha subunit contains unknown quinoid cofactor |
396585 |
| 1.4.9.1 | quinone |
contains a quinone similar to but not identical with the prosthetic group of EC 1.1.99.8 |
396579 |
| 1.4.9.1 | tryptophan tryptophylquinone |
- |
396584, 654628, 674171, 685218, 685296, 686104, 688702, 713510, 723880, 724308, 725020 |
| 1.4.9.1 | tryptophan tryptophylquinone |
a two-electron redox cofactor, each beta subunit of the heterotetrameric enzyme NADH possesses a tryptophan tryptophylquinone, TTQ, protein-derived cofactor. TTQ is formed by post-translational modification of two tryptophan residues of the preMADH polypeptide chain through the diheme enzyme MauG. This six-electron oxidation of preMADH requires long-range electron transfer as the structure of the MauG-preMADH complex reveals that the shortest distance between the modified residues of preMADH and the nearest heme of MauG is 14.0 A, overview |
711254 |
| 1.4.9.1 | tryptophan tryptophylquinone |
contains a tryptophan tryptophylquinone prosthetic group |
396581 |
| 1.4.9.1 | tryptophan tryptophylquinone |
each beta-subunit possesses a prosthetic group |
654866 |
| 1.4.9.1 | tryptophan tryptophylquinone |
MauG is a diheme enzyme that catalyzes the final steps in the biosynthesis of the cofactor tryptophan tryptophylquinone in the enzyme |
724352 |
| 1.4.9.1 | tryptophan tryptophylquinone |
TTQ |
742302 |
