EC Number   |
Natural Substrates |
|---|
   1.1.1.105 | 13-cis-retinol + NAD+ |
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol |
| 1.1.1.105 | all-trans-retinal + NAD(P)H + H+ |
RDH5 has only a minor in vivo all-trans RDH activity |
| 1.1.1.105 | all-trans-retinal + NADH + H+ |
- |
| 1.1.1.105 | all-trans-retinol + NAD+ |
RoDH-4 is capable of contributing to the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in the cellular context |
| 1.1.1.105 | all-trans-retinol + NAD+ |
- |
| 1.1.1.105 | all-trans-retinol + NAD+ |
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes |
| 1.1.1.105 | all-trans-retinol + NAD+ |
RDH1 functions in a path of all-trans-retinoic acid biosynthesis starting early during embryogenesis |
| 1.1.1.105 | all-trans-retinol + NAD+ |
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol |
| 1.1.1.105 | all-trans-retinol-[cellular-retinol-binding-protein] + NAD+ |
- |
| 1.1.1.105 | more |
the enzyme is expressed predominantly in the differentiating spinous layers and is under positive, feed-forward regulation by retinoic acid |
