RDH10

{{Infobox enzyme

| name = Retinol dehydrogenase 10

| AltNames = NAD⁺-retinol dehydrogenase

| image =

| image_size =

| caption =

| EC_number = 1.1.1.105

| CAS_number =

| GO_code = 0052650

}}

RDH10 is a membrane-bound NAD⁺-dependent retinol dehydrogenase which belongs to the superfamily of short-chain dehydrogenases. RDH10 catalyzes the first oxidative step in retinoic acid biosynthesis:

:all-trans-retinol+ NAD⁺ $\backslash rightleftharpoons$ all-trans-retinal + NADH + H⁺

Due to its preference for NAD⁺ rather than NADP⁺ as a cofactor, RDH10 functions near-exclusively in the oxidative direction under physiological conditions to increase levels of retinal and retinoic acid.

RDH10 has also been shown to act on 11-cis-retinol via interactions with CRALBP and RPE65.

RDH10 plays an essential role in organ, limb, and craniofacial development during embryogenesis.

RDH10 loss of function mutations in mice are embryonically lethal.

Despite its similarity to other retinol dehydrogenases, RDH10 is not associated with any known human retinal disease. RDH10 may partially compensate for loss of RDH5 function in fundus albipunctatus.

RDH10 overexpression is associated with brain and spinal cord glioma progression. Serum levels of RDH10 may serve as a biomarker for type 2 diabetes or metabolic dysfunction–associated steatotic liver disease.

{{reflist|refs=

{{cite journal | vauthors = Belyaeva OV, Johnson MP, Kedishvili NY | title = Kinetic analysis of human enzyme RDH10 defines the characteristics of a physiologically relevant retinol dehydrogenase | journal = Journal of Biological Chemistry | volume = 283 | issue = 29 | pages = 20299–20308 | date = 2008-07-18 | pmid = 18502750 | pmc = 2459273 | doi = 10.1074/jbc.M800019200 | doi-access = free }}

{{cite journal | vauthors = Farjo KM, Moiseyev G, Takahashi Y, Crouch RK, Ma JX | title = The 11-cis-retinol dehydrogenase activity of RDH10 and its interaction with visual cycle proteins | journal = Investigative Ophthalmology & Visual Science | volume = 50 | issue = 11 | pages = 5089–5097 | date = 2009-11-01 | pmid = 19458327 | doi = 10.1167/iovs.09-3797 }}

{{cite journal | vauthors = Farjo KM, Moiseyev G, Nikolaeva O, Sandell LL, Trainor PA, Ma JX | title = RDH10 is the primary enzyme responsible for the first step of embryonic Vitamin A metabolism and retinoic acid synthesis | journal = Developmental Biology | volume = 357 | issue = 2 | pages = 347–355 | date = 2011-09-15 | pmid = 21782811 | pmc = 3164597 | doi = 10.1016/j.ydbio.2011.07.011 }}

{{cite journal | vauthors = Kiser PD, Palczewski K | title = Retinoids and Retinal Diseases | journal = Annual Review of Vision Science | volume = 2 | pages = 197–234 | date = 2016-06-18 | pmid = 27917399 | pmc = 5132409 | doi = 10.1146/annurev-vision-111815-114407 }}

{{cite journal | vauthors = Li F, Li R, Deng H | title = Identification of retinol dehydrogenase 10 as a shared biomarker for metabolic dysfunction-associated steatotic liver disease and type 2 diabetes mellitus | journal = Frontiers in Pharmacology | volume = 16 | pages = 1521416 | date = 2025 | pmid = 39925846 | pmc = 11802817 | doi = 10.3389/fphar.2025.1521416 | doi-access = free }}

{{cite journal | vauthors = Sandell LL, Sanderson BW, Moiseyev G, Johnson T, Mushegian A, Young K, Rey JP, Ma JX, Staehling-Hampton K, Trainor PA | title = RDH10 is essential for synthesis of embryonic retinoic acid and is required for limb, craniofacial, and organ development | journal = Genes & Development | volume = 21 | issue = 9 | pages = 1113–1124 | date = 2007-05-01 | pmid = 17473173 | pmc = 1855236 | doi = 10.1101/gad.1533407 }}

{{cite journal | vauthors = Sandell LL, Lynn ML, Inman KE, McDowell W, Trainor PA | title = RDH10 oxidation of Vitamin A is a critical control step in synthesis of retinoic acid during mouse embryogenesis | journal = PLOS ONE | volume = 7 | issue = 2 | pages = e30698 | date = 2022-02-02 | pmid = 22319578 | pmc = 3271098 | doi = 10.1371/journal.pone.0030698 | doi-access = free }}

{{cite journal | vauthors = Wu BX, Chen Y, Chen Y, Fan J, Rohrer B, Crouch RK, Ma JX | title = Cloning and characterization of a novel all-trans retinol short-chain dehydrogenase/reductase from the RPE | journal = Investigative Ophthalmology & Visual Science | volume = 43 | issue = 11 | pages = 3365–3372 | date = 2002-11-01 | pmid = 12407145 }}

{{cite journal | vauthors = Zhao Z, Song Z, Wang Z, Zhang F, Ding Z, Zhao Z, Liu L, Fan T | title = Retinol dehydrogenase 10 promotes epithelial-mesenchymal transition in spinal cord gliomas via PI3K/AKT pathway | journal = International Journal of Immunopathology and Pharmacology | volume = 38 | pages = 3946320241276336 | date = 2024-08-24 | pmid = 39180753 | pmc = 11344904 | doi = 10.1177/03946320241276336 }}

}}

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Category:NADH-dependent enzymes