Search results for RDH10
Showing 5 results out of 5
Protein (1 results from a total of 1)
Identifier: R-HSA-2454090
Species:
Homo sapiens
Compartment:
endoplasmic reticulum membrane
Primary external reference: UniProt: RDH10:
Q8IZV5
Set (2 results from a total of 2)
Identifier: R-HSA-2454066
Species:
Homo sapiens
Compartment:
endoplasmic reticulum membrane
Identifier: R-HSA-5615661
Species:
Homo sapiens
Compartment:
endoplasmic reticulum membrane
Reaction (2 results from a total of 2)
Identifier: R-HSA-74872
Species:
Homo sapiens
Compartment:
endoplasmic reticulum membrane,
cytosol
Using NADP+ as cofactor, several members of the short-chain dehydrogenases/reductases (SDR) family can (reversibly) catalyse the oxidation of 11-cis-retinol (11cROL) to 11-cis-retinal (11cRAL) in retinal pigment epithelium (RPE) cells. Retinol dehydrogenases 10 and 11 (RDH10 and 11) are two such members utilizing the cofactor NADP+ (Wu et al. 2002, Kedishvili et al. 2002 respectively). Cellular retinaldehyde-binding protein (RLBP1), the protein bound to 11cRAL in RPE, is not present in photoreceptor cells.
Identifier: R-HSA-5362518
Species:
Homo sapiens
Compartment:
cytosol,
endoplasmic reticulum membrane
Multiple retinol dehydrogenases (RDH), members of the short-chain dehydrogenase/reductase (SDR) gene family, are candidates for catalysing conversion of retinol into retinal under physiological conditions (Napoli 2012). These include RDH16 (aka RoDH-4, RDH-E, Rdh1), RDH10, DHRS9 (aka retSDR8) and RDHE2. Two of these, Rdh1 (human ortholog RDH16) and Rdh10 (human ortholog RDH10), have been knocked out in mice and display RA-associated phenotypes. Both are membrane bound oxidoreductases that reversibly catalyse the first and rate limiting step in retinoic acid biosynthesis, and use NAD+ as cofactor to the corresponding aldehyde all trans retinal (atRAL) (Gough et al. 1998, Jurukovski et al. 1999, Pecozzi et al. 2003). The other RDH are currently under study, but have not been ablated in mice.
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