EC Number |
Cofactor |
Reference |
---|
1.14.14.11 | FAD |
- |
744072 |
1.14.14.11 | FAD |
dependent on |
727028 |
1.14.14.11 | FAD |
incorporation of reduced FAD into StyA enzymes is attended with significant conformational rearrangements |
743994 |
1.14.14.11 | FAD |
the enzyme favors FAD and FMN over riboflavin |
726766 |
1.14.14.11 | FADH2 |
- |
726776, 727526, 728003, 728070 |
1.14.14.11 | FADH2 |
direct electrochemical regeneration of FADH2 to substitute for the complex native regeneration cycle including StyB and NADH |
715248 |
1.14.14.11 | FADH2 |
flavin binding and redox equilibria are tightly coupled such that reduced FAD binds apo NSMOA about 8000times more tightly than the oxidized coenzyme |
714187 |
1.14.14.11 | FADH2 |
no epoxidation activity is observed for the StyAB system when FAD is replaced by FMN or riboflavin. At a FAD concentration exceeding 0.015 mM, the styrene oxide formation rate decreases |
715353 |
1.14.14.11 | FADH2 |
NSMOA binds tightly to reduced FAD. FAD C(4a)-peroxide is the oxygen atom donor |
714256 |
1.14.14.11 | FADH2 |
StyA1 is not active with free FADH2 and recognizes StyA2B as its natural partner. FADH2-induced activation of StyA1 requires interprotein communication with StyA2B. StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity |
712306 |