EC Number   |
Reaction |
Reference |
|---|
    1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ |
- |
- |
| 1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ |
bi-bi ternary mechanism, i.e. both FMN and NADPH must bind to the active site before catalysis can occur |
672184 |
| 1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ |
binding of FMN by apoenzyme is noncooperative, exothermic and primarily enthalpy driven with significant conformational changes in enzyme upon binding. The kinetically deduced ping-pong mechanism is supported by measurement of binding affinities of the oxidized and reduced FMN cofoactors |
672105 |
| 1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ |
catalytic mechanism |
660061 |
| 1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ |
FRP:luciferase coupled reaction can utilize reduced flavin by both free diffusion and direct transfer |
671610 |
| 1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ |
ping-pong mechanism |
689388 |
| 1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ |
single-enzyme kinetic assay, SsuE follows ordered sequential mechanism with NADPH as the first substrate to bind and NADP+ as the last product to leave. In presence of monooxygenase SsuD and octanesulfonate mechanism is altered to rapid equilibrium ordered mechanism, and Km-value for FMN increases 10fold |
657786 |
| 1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ |
the enzyme catalysis obeys the ping-pong Bi-Bi kinetic mechanism with substrate FMN as well as substrate nitrofurazone, but upon coupling with the bioluminescent reaction of luciferase, it changes to the sequential mechanism |
-, 742109 |
| 1.5.1.30 | reduced riboflavin + NADP+ = riboflavin + NADPH + H+ |
the nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer |
-, 678187 |
