The Enzyme Database

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Accepted name: retinoid isomerohydrolase
Reaction: an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid
For diagram of retinal and derivatives biosynthesis, click here
Other name(s): all-trans-retinyl-palmitate hydrolase (ambiguous); retinol isomerase (ambiguous); all-trans-retinol isomerase:hydrolase (ambiguous); all-trans-retinylester 11-cis isomerohydrolase; RPE65 (gene name)
Systematic name: all-trans-retinyl ester acylhydrolase, 11-cis retinol forming
Comments: This enzyme, which operates in the retinal pigment epithelium (RPE), catalyses the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol, a key step in the regeneration of the visual chromophore in the vertebrate visual cycle [4]. Interaction of the enzyme with the membrane is critical for its enzymic activity [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 106389-24-6
1.  Blaner, W.S., Das, S.R., Gouras, P. and Flood, M.T. Hydrolysis of 11-cis- and all-trans-retinyl palmitate by homogenates of human retinal epithelial cells. J. Biol. Chem. 262 (1987) 53–58. [PMID: 3793734]
2.  Bernstein, P.S., Law, W.C. and Rando, R.R. Isomerization of all-trans-retinoids to 11-cis-retinoids in vitro. Proc. Natl. Acad. Sci. USA 84 (1987) 1849–1853. [PMID: 3494246]
3.  Bridges, C.D. and Alvarez, R.A. The visual cycle operates via an isomerase acting on all-trans retinol in the pigment epithelium. Science 236 (1987) 1678–1680. [PMID: 3603006]
4.  Moiseyev, G., Chen, Y., Takahashi, Y., Wu, B.X. and Ma, J.X. RPE65 is the isomerohydrolase in the retinoid visual cycle. Proc. Natl. Acad. Sci. USA 102 (2005) 12413–12418. [PMID: 16116091]
5.  Nikolaeva, O., Takahashi, Y., Moiseyev, G. and Ma, J.X. Purified RPE65 shows isomerohydrolase activity after reassociation with a phospholipid membrane. FEBS J. 276 (2009) 3020–3030. [PMID: 19490105]
6.  Golczak, M., Kiser, P.D., Lodowski, D.T., Maeda, A. and Palczewski, K. Importance of membrane structural integrity for RPE65 retinoid isomerization activity. J. Biol. Chem. 285 (2010) 9667–9682. [PMID: 20100834]
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