EC Number   |
Cofactor |
Reference |
|---|
    2.1.1.148 | FAD |
- |
637235, 657899, 671555, 680675, 681375, 681384, 691759, 692837, 694812, 718969, 719663, 720985 |
| 2.1.1.148 | FAD |
even though FAD is very well bound to three subunits, FAD interactions are not an absolute requirement for tetramer stabilization |
637235 |
| 2.1.1.148 | FAD |
FAD/NAPDH couple |
691285 |
| 2.1.1.148 | FAD |
noncovalently bound |
659429 |
| 2.1.1.148 | FAD |
presence of FAD additionally stabilizes the protein against thermal denaturation by 10 degrees. The assembly of thymidylate synthase with FAD is governed by a large enthalpy change opposed by an unfavorable entropy change resulting in a relatively strong nanomolar binding |
756968 |
| 2.1.1.148 | FAD |
presence of FAD additionally stabilizes the protein against thermal denaturation by 4.9 degrees. Binding of dUMP to FAD-loaded proteins stabilizes further. ThyX binds FAD with a low micromolar binding affinity in a process characterized by a favorable entropy change |
756968 |
| 2.1.1.148 | FAD |
the enzyme is bound to 4 FAD molecules |
720992 |
| 2.1.1.148 | FAD |
the flavin is oxidized after dUMP reacts with 5,10-methylenetetrahydrofolate |
658992 |
| 2.1.1.148 | FAD |
the pro-R hydride of NADPH and not the R6 hydride of the tetrahydropterin is the reducing agent. The stereospecificity for the pro-R NADPH oxidation is not absolute. The hydride is transferred to FAD, which is the rate-limiting step of the catalytic cascade |
658015 |
| 2.1.1.148 | FAD |
tightly bound, four molecules per tetramer |
637234, 637235 |
