Target type: molecularfunction
Catalysis of the reaction: all-trans-retinol = 11-cis-retinol. [GOC:pde, RHEA:19141]
Retinol isomerase activity catalyzes the interconversion of all-trans-retinol to 11-cis-retinol. This isomerization is crucial for the visual cycle, as 11-cis-retinol is the precursor to 11-cis-retinal, the chromophore that absorbs light in rhodopsin. The reaction mechanism typically involves the formation of a Schiff base intermediate between the enzyme and the retinol substrate. This intermediate undergoes a series of conformational changes, driven by the enzyme's active site, leading to the isomerization. The isomerase activity is highly specific for all-trans-retinol and 11-cis-retinol, and is essential for maintaining the proper levels of these isomers in the retina. Retinol isomerase activity is found in a variety of organisms, including humans, animals, and bacteria. In humans, it is primarily located in the retinal pigment epithelium, where it plays a critical role in the visual cycle.'
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Protein | Definition | Taxonomy |
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Retinoid isomerohydrolase | A retinal pigment epithelium-specific 65 kDa protein that is encoded in the genome of chicken. [PRO:DNx] | Gallus gallus (chicken) |
Compound | Definition | Classes | Roles |
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phenyl-n-tert-butylnitrone | phenyl-N-tert-butylnitrone: a spin-trapping agent |