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• W2090539847 startingPage "11715" @default.
• W2090539847 abstract "Vertebrate retinas contain two types of light-detecting cells. Rods subserve vision in dim light, while cones provide color vision in bright light. Both contain light-sensitive proteins called opsins. The light-absorbing chromophore in most opsins is 11-cis-retinaldehyde, which is isomerized to all-trans-retinaldehyde by absorption of a photon. Restoration of light sensitivity requires chemical re-isomerization of retinaldehyde by an enzymatic pathway called the visual cycle in the retinal pigment epithelium. The isomerase in this pathway uses all-trans-retinyl esters synthesized by lecithin retinol acyl transferase (LRAT) as the substrate. Several lines of evidence suggest that cone opsins regenerate by a different mechanism. Here we demonstrate the existence of two catalytic activities in chicken retinas. The first is an isomerase activity that effects interconversion of all-trans-retinol and 11-cis-retinol. The second is an ester synthase that effects palmitoyl coenzyme A-dependent synthesis of all-trans- and 11-cis-retinyl esters. Kinetic analysis of these two activities suggests that they act in concert to drive the formation of 11-cis-retinoids in chicken retinas. These activities may be part of a new visual cycle for the regeneration of chromophores in cones." @default.
• W2090539847 created "2016-06-24" @default.
• W2090539847 creator A5013703942 @default.
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• W2090539847 creator A5083445941 @default.
• W2090539847 creator A5087002017 @default.
• W2090539847 date "2005-08-09" @default.
• W2090539847 modified "2023-09-26" @default.
• W2090539847 title "Chicken Retinas Contain a Retinoid Isomerase Activity that Catalyzes the Direct Conversion of all-<i>trans-</i>Retinol to 11-<i>cis-</i>Retinol" @default.
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• W2090539847 doi "https://doi.org/10.1021/bi050942m" @default.
• W2090539847 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2851629" @default.
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