EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.105 | expressed in Sf9 insect cells and in HEK-293 cells | Homo sapiens |
1.1.1.105 | RDH-E2 is expressed in Sf9 insect cells as a fusion to the C-terminal His6-tag | Homo sapiens |
EC Number | General Stability | Organism |
---|---|---|
1.1.1.105 | gel-filtration of RDH-E2 preparation to remove imidazole results in significant loss of activity (about 90%) despite nearly complete recovery of the protein suggesting that RDH-E2 is sensitive to desalting | Homo sapiens |
1.1.1.105 | the enzyme is sensitive to desalting | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.105 | imidazole | increasing the amount of imidazole in the reaction mixture with purified RDH-E2 from 25 to 225mM significantly decreases RDH-E2 activity | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.1.105 | endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
1.1.1.105 | endoplasmic reticulum | RDH-E2 protein exhibits a punctuate localization pattern, surrounding the nucleus suggesting that RDH-E2 is associated with endoplasmic reticulum | Homo sapiens | 5783 | - |
1.1.1.105 | membrane | of endoplasmic reticulum | Homo sapiens | 16020 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.105 | all-trans-retinol + NAD+ | Homo sapiens | 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 | all-trans-retinal + NADH + H+ | - |
r | |
1.1.1.105 | additional information | Homo sapiens | RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.105 | Homo sapiens | Q8N3Y7 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.105 | Ni2+-NTA resin column chromatography | Homo sapiens |
1.1.1.105 | recombinant enzyme | Homo sapiens |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.1.1.105 | epidermis | retinal dehydrogenase 2 is significantly elevated in psoriatic skin | Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.105 | all-trans-retinal + NADH + H+ | - |
Homo sapiens | all-trans-retinol + NAD+ | - |
? | |
1.1.1.105 | all-trans-retinaldehyde + NADH + H+ | - |
Homo sapiens | ? | - |
? | |
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 | Homo sapiens | all-trans-retinal + NADH + H+ | - |
r | |
1.1.1.105 | all-trans-retinol + NAD+ | exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+ | Homo sapiens | all-trans-retinal + NADH + H+ | - |
r | |
1.1.1.105 | all-trans-retinol + NADP+ | exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+ | Homo sapiens | all-trans-retinal + NADPH + H+ | - |
r | |
1.1.1.105 | additional information | no activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH | Homo sapiens | ? | - |
? | |
1.1.1.105 | additional information | RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation | Homo sapiens | ? | - |
? | |
1.1.1.105 | additional information | no activity is detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.105 | epidermal retinol dehydrogenase 2 | - |
Homo sapiens |
1.1.1.105 | RDH-E2 | - |
Homo sapiens |
1.1.1.105 | retinol dehydrogenase 2 | - |
Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.105 | NAD+ | exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+ | Homo sapiens | |
1.1.1.105 | NADH | exhibits a strong preference for NAD+/NADH as cofactors | Homo sapiens | |
1.1.1.105 | NADP+ | exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+ | Homo sapiens |