EC Number |
Cofactor |
Reference |
---|
3.7.1.11 | FAD |
- |
699603 |
3.7.1.11 | FAD |
1.0 FAD molecule per enzyme monomer, 2fold Rossmann fold for FAD binding at the C-terminal end |
719735 |
3.7.1.11 | FAD |
flavoenzyme, the redox-active cofactor FAD seems not to participate in catalysis, one FAD molecule per enzyme monomer. The FAD cofactor is bound in an extended conformation at the C-terminal end of the six-stranded betab-sheet of the domain beta |
719464 |
3.7.1.11 | FAD |
noncovalently bound, one FAD per monomer |
733657 |
3.7.1.11 | more |
no cofactor: 2,6-dichlorophenol-indophenol |
695911 |
3.7.1.11 | more |
the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer |
733657 |
3.7.1.11 | NAD+ |
- |
695911 |
3.7.1.11 | thiamine diphosphate |
- |
699603 |
3.7.1.11 | thiamine diphosphate |
dependent on |
733089, 733660, 735301 |
3.7.1.11 | thiamine diphosphate |
dependent on, 0.8 ThDP per enzyme monomer, ThDP binding motif, overview |
719735 |