EC Number | General Stability | Organism |
---|---|---|
1.18.1.2 | persistence of a native folded structure is detected in up to 6 M urea, with 38% residual activity, the high stability might be due to robust interactions between the FAD and the NADP+ domains of the protein | Leptospira interrogans |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.18.1.2 | Leptospira interrogans | Q8EY89 | - |
- |
1.18.1.2 | Leptospira interrogans 56601 | Q8EY89 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.18.1.2 | 2 reduced ferredoxin + NADP+ | source of ferredoxin: Leptospira LB107 | Leptospira interrogans | 2 oxidized ferredoxin + NADPH + H+ | - |
? | |
1.18.1.2 | 2 reduced ferredoxin + NADP+ | source of ferredoxin: Leptospira LB107 | Leptospira interrogans 56601 | 2 oxidized ferredoxin + NADPH + H+ | - |
? | |
1.18.1.2 | additional information | enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase | Leptospira interrogans | ? | - |
? | |
1.18.1.2 | additional information | enzyme additionally displays high diaphorase activity using artificial acceptors and functions as a ferric reductase | Leptospira interrogans 56601 | ? | - |
? |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.18.1.2 | 68.1 | - |
melting temperature | Leptospira interrogans |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.18.1.2 | 6.5 | - |
- |
Leptospira interrogans |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.18.1.2 | FAD | the high stability of the enzyme might be due to robust interactions between the FAD and the NADP+ domains of the protein | Leptospira interrogans | |
1.18.1.2 | NADPH | - |
Leptospira interrogans |