EC Number   |
Reaction |
Reference |
|---|
    1.1.1.21 | alditol + NAD(P)+ = aldose + NAD(P)H + H+ |
after the catalytic event, a rearrangement of a bound ligand can trigger the opening of the safety-belt loop of G213-S226, initiating the release of the oxidized cofactor |
684142 |
| 1.1.1.21 | alditol + NAD(P)+ = aldose + NAD(P)H + H+ |
after the hydride donation step, the positive charge in the nicotinamide head stabilizes the neutral bridge between residues D43 and L77, allowing the relaxation of the tyrosine geometry toward the substrate head and the subsequent proton donation. After this last step, Y48 recoils to a locked geometry where the D43-L77 salt bridge is formed again and completes a tight four-charge sandwich involving the D(-), L(+), Y(-), and nicotinamide(+) head |
689796 |
| 1.1.1.21 | alditol + NAD(P)+ = aldose + NAD(P)H + H+ |
mechanism, proton is donated by Tyr48 hydroxyl to the substrate |
654101 |
| 1.1.1.21 | alditol + NAD(P)+ = aldose + NAD(P)H + H+ |
reaction mechanism |
286254, 286258, 286260, 286264 |
| 1.1.1.21 | alditol + NAD(P)+ = aldose + NAD(P)H + H+ |
reaction mechanism, catalytic residues are Tyr48, Lys77, and His110, C-terminal loop residues Ala299, Leu300, Leu301, Ser302, Cys303 are involved in substrate and inhibitor binding |
669874 |
| 1.1.1.21 | alditol + NAD(P)+ = aldose + NAD(P)H + H+ |
the ordered bi-bi kinetic mechanism is controlled by hinges and latches of enzyme structure, residues R268, G213, and S226 are involved |
667807 |
