Reactome | RDH10,16,DHRS9,RDHE2 oxidise atROL to atRAL

RDH10,16,DHRS9,RDHE2 oxidise atROL to atRAL

Stable Identifier

R-HSA-5362518

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, endoplasmic reticulum membrane

Synonyms

Multiple RDHs convert atROL into atRAL

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

RDH10,16,DHRS9,RDHE2 oxidise atROL to atRAL

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
21621639	Physiological insights into all-trans-retinoic acid biosynthesis Napoli, JL	Biochim. Biophys. Acta	2012
14596915	Genomic organization and transcription of the human retinol dehydrogenase 10 (RDH10) gene Fornasari, D, Meneveri, R, Benfante, R, Picozzi, P, Marozzi, A, Ginelli, E, Barisani, D	FEBS Lett.	2003
10329026	Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes Su, J, Karaman-Jurukovska, N, Randolph, RK, Napoli, JL, Markova, NG, Simon, M, Jurukovski, V	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 Kedishvili, NY, VanOoteghem, S, Gough, WH, Sint, T	J. Biol. Chem.	1998