EC Number |
Cofactor |
Reference |
---|
5.3.3.2 | FMN |
- |
660902, 662026, 704638, 746921, 747106 |
5.3.3.2 | FMN |
a mechanism is proposed where the reduced flavin cofactor acts as a general acid/base catalyst and helps stabilize the carbocationic intermediate formed by protonation |
728667 |
5.3.3.2 | FMN |
bound only with very moderate affinity and is therefore completely lost during purification. However, the enzyme can be reconstituted in the crystals by soaking with FMN |
652916 |
5.3.3.2 | FMN |
FMN must be in reduced state to be catalytically active |
678309 |
5.3.3.2 | FMN |
IDI-2 requires reduced flavin |
714202 |
5.3.3.2 | FMN |
maximal activity with 10 microM FMN |
661357 |
5.3.3.2 | FMN |
nearly no activity with the flavin analogue 5-deazaFMN |
660882 |
5.3.3.2 | FMN |
reduced flavin is required. The neutral semiquinone state of the flavin is stabilized thermodynamically relative to free FMN in solution. Kd value is 0.0047 mM at pH 7.0, 37°C |
678278 |
5.3.3.2 | FMN |
required under aerobic and anaerobic conditions |
661638 |
5.3.3.2 | FMN |
required, IDI-2 reconstituted with cofactor analogues such as 5-deaza-FMN show no activity |
713655 |