EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.5.1.30 | in NAD(P)(+)-free, NAD(+)-bound, and NADP(+)-bound states. The nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer | Sulfurisphaera tokodaii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.30 | Sulfurisphaera tokodaii | - |
stain 7 | - |
1.5.1.30 | Sulfurisphaera tokodaii 7 | - |
stain 7 | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ | the nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer | Sulfurisphaera tokodaii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.1.30 | HpaC | - |
Sulfurisphaera tokodaii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.30 | FMN | one molecule per monomer of enzyme. FMN is preferred over FAD | Sulfurisphaera tokodaii | |
1.5.1.30 | NADP+ | - |
Sulfurisphaera tokodaii |