EC Number   |
Substrates |
Products |
Reversibility |
|---|
   1.1.1.315 | 11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+ |
in presence of excess NADH, wild-type catalyzes the reduction of 11-cis-retinal |
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+ |
- |
r |
| 1.1.1.315 | 11-cis-retinol + NAD+ |
- |
11-cis-retinal + NADH |
- |
? |
| 1.1.1.315 | 11-cis-retinol + NAD+ |
Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism. Substrate specificity and expression locus of Rdh5 suggest that it could serve as both an 11-cis-retinol dehydrogenase in the RPE and a 9-cis-retinol dehydrogenase and/or an androgen dehydrogenase outside of the retinal pigment epithelium |
11-cis-retinal + NADH |
- |
? |
| 1.1.1.315 | 11-cis-retinol + NAD+ |
- |
11-cis-retinal + NADH + H+ |
- |
? |
| 1.1.1.315 | 11-cis-retinol + NAD+ |
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity. RDH10 may function in the RPE retinoid visual cycle as an 11-cis-retinol dehydrogenase, and thereby partially compensate for the loss of RDH5 function in human patients with fundus albipunctatus |
11-cis-retinal + NADH + H+ |
- |
? |
| 1.1.1.315 | 11-cis-retinol + NAD+ |
activity with NAD+ is about 10fold higher than with NADP+ |
11-cis-retinal + NADH + H+ |
- |
? |
| 1.1.1.315 | 11-cis-retinol + NAD+ |
little preference between 9-cis-retinol and 11-cis-retinol. Uses NAD+ as its preferred cofactor |
11-cis-retinal + NADH + H+ |
- |
? |
| 1.1.1.315 | 11-cis-retinol + NAD+ |
microsomal preparations of RDH10 are not active in presence of NADP+ |
11-cis-retinal + NADH + H+ |
- |
r |
| 1.1.1.315 | 11-cis-retinol + NAD+ |
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity |
11-cis-retinal + NADH + H+ |
- |
? |
| 1.1.1.315 | 11-cis-retinol + NADP+ |
- |
11-cis-retinal + NADPH |
- |
? |
