EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.105 | retinoic acid-inducible dehydrogenase reductase 3 | - |
Homo sapiens |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.105 | expressed in HEK-293 cells and Sf9 insect cells | Homo sapiens |
1.1.1.105 | expression in Sf9 cells, HepG2 and HEK293 cells | Homo sapiens |
1.1.1.300 | - |
Mus musculus |
1.1.1.300 | expression in Sf9 cells, HepG2 and HEK293 cells | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.105 | 0.000039 | - |
all-trans-retinol | pH and temperature not specified in the publication | Homo sapiens | |
1.1.1.105 | 0.000039 | - |
all-trans-retinol | pH not specified in the publication, temperature not specified in the publication | Homo sapiens | |
1.1.1.105 | 0.00006 | - |
11-cis-retinol | pH and temperature not specified in the publication | Homo sapiens | |
1.1.1.105 | 0.00046 | - |
all-trans-retinaldehyde | pH and temperature not specified in the publication | Homo sapiens | |
1.1.1.105 | 0.00046 | - |
all-trans retinal | pH not specified in the publication, temperature not specified in the publication | Homo sapiens | |
1.1.1.105 | 0.011 | - |
NADH | pH and temperature not specified in the publication | Homo sapiens | |
1.1.1.105 | 0.011 | - |
NADH | pH not specified in the publication, temperature not specified in the publication | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.1.105 | microsome | - |
Homo sapiens | - |
- |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.105 | Homo sapiens | - |
- |
- |
1.1.1.105 | Homo sapiens | Q8IZV5 | - |
- |
1.1.1.300 | Homo sapiens | O75911 | - |
- |
1.1.1.300 | Mus musculus | O88876 | - |
- |
1.1.1.300 | Mus musculus | Q8VCH7 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.105 | 11-cis-retinol + NAD+ | - |
Homo sapiens | ? | - |
? | |
1.1.1.105 | all-trans retinal + NADH + H+ | - |
Homo sapiens | all-trans-retinol + NAD+ | - |
r | |
1.1.1.105 | all-trans-retinaldehyde + NADH + H+ | - |
Homo sapiens | all-trans-retinol + NAD+ | - |
r | |
1.1.1.105 | all-trans-retinol + NAD+ | - |
Homo sapiens | all-trans-retinal + NADH + H+ | - |
r | |
1.1.1.105 | all-trans-retinol + NAD+ | - |
Homo sapiens | all-trans-retinaldehyde + NADH + H+ | - |
r | |
1.1.1.105 | additional information | the enzyme is not active with NADP+ or NADPH as cofactors | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.105 | RDH10 | - |
Homo sapiens |
1.1.1.105 | retinol dehydrogenase 10 | - |
Homo sapiens |
1.1.1.300 | DHRS3 | - |
Homo sapiens |
1.1.1.300 | DHRS3 | - |
Mus musculus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.105 | NAD+ | - |
Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.105 | physiological function | the retinol dehydrogenase activity of RDH10 is activated by retinaldehyde reductase DHRS3. In turn, DHRS3 requires the presence of retinol dehydrogenase RDH10 to display its full catalytic activity. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other | Homo sapiens |
1.1.1.300 | physiological function | DHRS3 activity requires the presence of retinol dehydrogenase RDH10 to display its full catalytic activity. The retinol dehydrogenase activity of RDH10 is reciprocally activated by retinaldehyde reductase DHRS3. At E13.5, DHRS3-null embryos have 4fold lower levels of retinol and retinyl esters, but only slightly elevated levels of retinoic acid. The membrane-associated retinaldehyde reductase and retinol dehydrogenase activities are decreased by 4- and 2fold, respectively, in Dhrs3-/- embryos, and Dhrs3-/- mouse embryonic fibroblasts exhibit reduced metabolism of both retinaldehyde andretinol. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other | Mus musculus |
1.1.1.300 | physiological function | the retinol dehydrogenase activity of RDH10 is activated by retinaldehyde reductase DHRS3. In turn, DHRS3 requires the presence of retinol dehydrogenase RDH10 to display its full catalytic activity. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other | Homo sapiens |
1.1.1.300 | physiological function | the retinol dehydrogenase activity of RDH10 is reciprocally activated by retinaldehyde reductase DHRS3. At E13.5, DHRS3-null embryos have 4fold lower levels of retinol and retinyl esters, but only slightly elevated levels of retinoic acid. The membrane-associated retinaldehyde reductase and retinol dehydrogenase activities are decreased by 4- and 2fold, respectively, in Dhrs3-/- embryos, and Dhrs3-/- mouse embryonic fibroblasts exhibit reduced metabolism of both retinaldehyde andretinol. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other | Mus musculus |