EC Number   |
Cofactor |
Reference |
|---|
   1.6.5.5 | FMN |
- |
764164 |
| 1.6.5.5 | FMN |
in silico structural model of ArsH reconstituted with FMN, overview |
724333 |
| 1.6.5.5 | FMN |
prosthetic group involved in the reaction |
741786 |
| 1.6.5.5 | more |
no cofactor: NADH. Sequence does not contain a flavin-binding motif |
716132 |
| 1.6.5.5 | NADH |
the enzyme can be reduced with NADPH or NADH with a marked preference for NADPH |
764164 |
| 1.6.5.5 | NADPH |
- |
14081, 671365, 697701, 701074, 716132, 724703, 741786 |
| 1.6.5.5 | NADPH |
completely specific for NADPH as cofactor |
697208 |
| 1.6.5.5 | NADPH |
interference of NADPH on Zta1p binding to RNA is much lower than that of NADPH on human zeta-crystallin, consistent with a weaker binding of NADPH to the yeast enzyme |
697278 |
| 1.6.5.5 | NADPH |
NADPH binding causes conformational changes in the structure of the enzyme |
696058 |
| 1.6.5.5 | NADPH |
NADPH is located in the cleft between domains I and II. The adenine ring is sandwiched between the main chains of Ala220 and Glu221 and the side chain of Arg292. Ala220 and Glu221 are disordered in apo-QOR |
655855 |
