EC Number   |
Reaction |
Reference |
|---|
    1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
- |
- |
| 1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
hydride ion transfer reaction of the pro-S-hydrogen of NADPH to N5 of FAD, redox potentials |
394792 |
| 1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
mechanistic reaction scheme, structure-function relation |
394779, 394805 |
| 1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
mechanistic scheme for NAD(P)H:disulfide oxidoreductases |
394775 |
| 1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
molecular modeling of inhibitor binding using X-ray data |
394803 |
| 1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
neither the alpha-carboxy nor the alpha-amino function of the L-gamma-glutamyl group is essential for activity, can be replaced by uncharged benzyloxycarbonyl or tert-butyloxycarbonyl groups |
394802 |
| 1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
reducing catalytic site CVNVGC |
658318 |
| 1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
substrate binding mechanism, complex structure analysis, protease-like catalytic triade and electronic induced fit |
394793 |
| 1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
substrate binding structure, structural model |
394802 |
| 1.8.1.12 | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ |
trypanothione disulfide is the oxidized form of N1,N8-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. The enzyme from Crithidia fasciculata is a flavoprotein (FAD), whose activity is dependent on a redox-active cystine at the active centre. |
- |
