EC Number   |
Reaction |
Reference |
|---|
    1.17.4.4 | phylloquinol + a protein with a disulfide bond = phylloquinone + a protein with reduced L-cysteine residues |
(2) |
- |
| 1.17.4.4 | phylloquinone + a protein with a disulfide bond + H2O = 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues |
(1) |
- |
| 1.17.4.4 | phylloquinone + a protein with a disulfide bond + H2O = 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues |
analysis of the reaction mechanism by quantum mechanical methods, modeling, the geometries of proposed model intermediates in the mechanisms are energy optimized |
674074 |
| 1.17.4.4 | phylloquinone + a protein with a disulfide bond + H2O = 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues |
bi bi ping-pong mechanism for VKORC1, kinetic modeling |
724460 |
| 1.17.4.4 | phylloquinone + a protein with a disulfide bond + H2O = 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues |
ping-pong mechanism |
287710 |
| 1.17.4.4 | phylloquinone + a protein with a disulfide bond + H2O = 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues |
protein structure and catalytic mechanism, the enzyme activity is rate-limiting for the following gamma-carboxylation step |
671387 |
| 1.17.4.4 | phylloquinone + a protein with a disulfide bond + H2O = 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues |
quantum chemical study on mechanism and transition states. Once a key dissulfide is broken, the reaction proceeds largely downhill. The initial protonation of the epoxide oxygen is an important step, with the proton originating from a free mercapto group rather than a water molecule |
688461 |
