EC Number   |
Cofactor |
Reference |
|---|
    4.1.1.1 | CoA |
desulfocoenzyme A can substitute for CoA showing that the cofactor plays a structural rather than a catalytic role |
723667 |
| 4.1.1.1 | CoA |
Km value 0.0031 mM |
736379 |
| 4.1.1.1 | CoA |
pyruvate ferredoxin oxidoreductase activity is strictly CoA-dependent, desulfo-CoA does not serve as cofactor. The pyruvate decarboxylase activity accepts desulfo-CoA, Km value for CoA is 0.0014 mM |
736379 |
| 4.1.1.1 | NAD+ |
- |
736748 |
| 4.1.1.1 | thiamine diphosphate |
- |
649510, 650079, 650447, 665422, 666806, 678843, 679569, 679914, 679923, 679924, 682443, 683005, 686477, 690431, 690432, 690937, 691427, 691428, 691435, 691441, 691443, 692402, 692733, 693587, 693703, 694588, 694835, 695198, 702341, 704470, 706270, 714005, 714220, 726785, 727473, 735039, 744966, 746673, 746776, 746864, 746951 |
| 4.1.1.1 | thiamine diphosphate |
0.1 mM, required for activity |
691578 |
| 4.1.1.1 | thiamine diphosphate |
1.5 mM, required for activity |
694790 |
| 4.1.1.1 | thiamine diphosphate |
bound in the V conformation in the active sites of the enzyme, side chains of residues Glu51, Glu477, Asp28, His114, and His 115 potentially participate in proton transfer steps |
727679 |
| 4.1.1.1 | thiamine diphosphate |
bound to the active site located at the interface of the alpha and gamma domains |
678162 |
| 4.1.1.1 | thiamine diphosphate |
bound with high affinity at slightly acidic pH |
653155 |
