EC Number   |
Cofactor |
Reference  |
|---|
   1.14.14.21 | more |
the flavin reductase, EC 1.5.1.36, from Rhodococcus erythropolis strain D-1 grown in a medium containing dibenzothiophene as the sole source of sulfur is essential for the reactions of the two monooxygenases DszC and DszA in vivo. The purified flavin reductase contains no chromogenic cofactors and has a molecular mass of 86 kDa and four identical 22-kDa subunits. The enzyme catalyzes NADH-dependent reduction of flavin mononucleotide, FMN. The flavin reductase does not catalyze reduction of any nitroaromatic compound |
392304 |
| 1.14.14.21 | more |
FAD and lumiflavin have only weak activity as reducing agents |
735526 |
| 1.14.14.21 | more |
FMN oxidoreductase TdsD, a NADH-dependent FMN oxidoreductase, absolutely required for TdsC activity, maximum activity is obtained at a TdsD/TdsC molar ratio of 0.5, no activity in the absence of TdsD |
735526 |
| 1.14.14.21 | NADPH |
can substitute for NADH to some extent |
735526 |
| 1.14.14.21 | FMNH2 |
the reduced form of flavin serves as a substrate of DszC |
735584 |
| 1.14.14.21 | more |
no direct activity with NAD(P)H |
735584 |
| 1.14.14.21 | FADH2 |
- |
735785 |
| 1.14.14.21 | more |
the recombinant enzyme is able to utilize either FMNH2 or FADH2 when coupled with a flavin reductase that reduces either FMN or FAD |
735785 |
| 1.14.14.21 | FMNH2 |
enzyme DszC-FMN crystal structure analysis, FMN-binding site, binding structure and mechanism, modeling, overview |
736092 |
| 1.14.14.21 | FMNH2 |
the enzyme binds one flavin mononucleotide or reduced flavin mononucleotide (FMNH2) per 90,200-Da homodimer, and FMNH2 is an essential cosubstrate for its activity |
736340 |
