RDH10,16,DHRS9,RDHE2 oxidise atROL to atRAL

Stable Identifier
R-HSA-5362518
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
Multiple RDHs convert atROL into atRAL
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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.

Literature References
PubMed ID Title Journal Year
14596915 Genomic organization and transcription of the human retinol dehydrogenase 10 (RDH10) gene

Picozzi, P, Marozzi, A, Fornasari, D, Benfante, R, Barisani, D, Meneveri, R, Ginelli, E

FEBS Lett. 2003
21621639 Physiological insights into all-trans-retinoic acid biosynthesis

Napoli, JL

Biochim. Biophys. Acta 2012
10329026 Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes

Jurukovski, V, Markova, NG, Karaman-Jurukovska, N, Randolph, RK, Su, J, Napoli, JL, Simon, M

Mol. Genet. Metab. 1999
9677409 cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids

Gough, WH, VanOoteghem, S, Sint, T, Kedishvili, NY

J. Biol. Chem. 1998
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
retinol dehydrogenase activity of RDH10,16,DHRS9,RDHE2 [endoplasmic reticulum membrane]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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