RPE65 isomero-hydrolyses atREs to 11cROL

Stable Identifier
Reaction [transition]
Homo sapiens
Retinoid isomerohydrolase isomero-hydrolyses retinyl esters to 11-cis-retinol
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All-trans-retinol esters (atREs) serve as substrates for retinoid isomerohydrolase (RPE65), located in retinal pigment epithelium (RPE) cells. RPE65 hydrolyses atREs to 11-cis-retinol (11cROL), thus performing an isomerase activity as well as hydrolysis. RPE65 is membrane-bound, this being dependent on the palmitylation of the residue Cys-112 (Takahashi et al. 2009). RPE65 normally undergoes a light-dependent translocation to become more concentrated in the central region of RPE cells. This translocation requires Unconventional myosin-VIIa (MYO7A or USH1B) (Lopes et al. 2011).

Literature References
PubMed ID Title Journal Year
19049981 Identification of a novel palmitylation site essential for membrane association and isomerohydrolase activity of RPE65

Ma, JX, Takahashi, Y, Ablonczy, Z, Moiseyev, G, Chen, Y, Crouch, RK

J. Biol. Chem. 2009
21493626 The Usher 1B protein, MYO7A, is required for normal localization and function of the visual retinoid cycle enzyme, RPE65

Welch, DL, Radu, RA, Aleman, TS, Gibbs, D, Williams, DS, Jacobson, SG, Lopes, VS, Steel, KP, Libby, RT, Lillo, C

Hum. Mol. Genet. 2011
Catalyst Activity

all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity of RPE65 [plasma membrane]

This event is regulated
Positively by