RGD Reference Report - Identification of all-trans-retinol:all-trans-13,14-dihydroretinol saturase. - Rat Genome Database

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Identification of all-trans-retinol:all-trans-13,14-dihydroretinol saturase.

Authors: Moise, AR  Kuksa, V  Imanishi, Y  Palczewski, K 
Citation: Moise AR, etal., J Biol Chem. 2004 Nov 26;279(48):50230-42. Epub 2004 Sep 9.
RGD ID: 8553455
Pubmed: PMID:15358783   (View Abstract at PubMed)
PMCID: PMC2665716   (View Article at PubMed Central)
DOI: DOI:10.1074/jbc.M409130200   (Journal Full-text)

Retinoids carry out essential functions in vertebrate development and vision. Many of the retinoid processing enzymes remain to be identified at the molecular level. To expand the knowledge of retinoid biochemistry in vertebrates, we studied the enzymes involved in plant metabolism of carotenoids, a related group of compounds. We identified a family of vertebrate enzymes that share significant similarity and a putative phytoene desaturase domain with a recently described plant carotenoid isomerase (CRTISO), which isomerizes prolycopene to all-trans-lycopene. Comparison of heterologously expressed mouse and plant enzymes indicates that unlike plant CRTISO, the CRTISO-related mouse enzyme is inactive toward prolycopene. Instead, the CRTISO-related mouse enzyme is a retinol saturase carrying out the saturation of the 13-14 double bond of all-trans-retinol to produce all-trans-13,14-dihydroretinol. The product of mouse retinol saturase (RetSat) has a shifted UV absorbance maximum, lambda(max) = 290 nm, compared with the parent compound, all-trans-retinol (lambda(max) = 325 nm), and its MS analysis (m/z = 288) indicates saturation of a double bond. The product was further identified as all-trans-13,14-dihydroretinol, since its characteristics were identical to those of a synthetic standard. Mouse RetSat is membrane-associated and expressed in many tissues, with the highest levels in liver, kidney, and intestine. All-trans-13,14-dihydroretinol was also detected in several tissues of animals maintained on a normal diet. Thus, saturation of all-trans-retinol to all-trans-13,14-dihydroretinol by RetSat produces a new metabolite of yet unknown biological function.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
retinol metabolic process involved_inISSUniProtKB:Q64FW28553455PMID:15358783HGNC-UCL 

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
endoplasmic reticulum membrane located_inISSUniProtKB:Q64FW28553455PMID:15358783HGNC-UCL 
nuclear membrane located_inISSUniProtKB:Q64FW28553455PMID:15358783HGNC-UCL 
nuclear outer membrane located_inISSUniProtKB:Q64FW28553455PMID:15358783HGNC-UCL 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
all-trans-retinol 13,14-reductase activity enablesISSUniProtKB:Q64FW28553455PMID:15358783HGNC-UCL 

Objects Annotated

Genes (Rattus norvegicus)
Retsat  (retinol saturase)

Additional Information