Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 130, Issue 4, Pages 1154-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja710487q
Keywords
-
Categories
Funding
- NEI NIH HHS [R01 EY009339-19S1, R01 EY009339] Funding Source: Medline
- NIDDK NIH HHS [R01 DK049780, R01 DK49780] Funding Source: Medline
- PHS HHS [R01 R0109339] Funding Source: Medline
Ask authors/readers for more resources
Retinol saturase carries out a stereospecific saturation of the C13-C14 double bond of all-trans-retinol to generate (13R)-all-trans-13,14-dihydroretinol. This compound is found in cells expressing mouse or zebrafish retinol saturase and in the livers of mice fed retinyl palmitate. All-trans-13,14-dihydroretinol is oxidized in vivo to all-trans-13,14-dihydroretinoic acid, a highly selective agonist of the retinoic acid receptor. The naturally occurring (13R)-all-trans-13,14-dihydroretinoic acid is a weaker agonist than the (13S) enantiomer, indicating enantioselective recognition by the ligand-binding pocket of this receptor. Consequently the (13S) enantiomer, acting through the retinoic acid receptor, also inhibits adipose differentiation more potently than the (13R) enantiomer.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available