4.5 Article

Membrane-binding and enzymatic properties of RPE65

Journal

PROGRESS IN RETINAL AND EYE RESEARCH
Volume 29, Issue 5, Pages 428-442

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.preteyeres.2010.03.002

Keywords

Retinoid isomerase; RPE65; Membrane protein; Metalloenzyme; Retinal pigment epithelium; Leber congenital amaurosis

Categories

Funding

  1. NIH [R01-EY009339]
  2. Visual Sciences Training Program [T32-EY007157]

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Regeneration of visual pigments is essential for sustained visual function. Although the requirement for non-photochemical regeneration of the visual chromophore, 11-cis-retinal, was recognized early on, it was only recently that the trans to cis retinoid isomerase activity required for this process was assigned to a specific protein, a microsomal membrane enzyme called RPE65. In this review, we outline progress that has been made in the functional characterization of RPE65. We then discuss general concepts related to protein-membrane interactions and the mechanism of the retinoid isomerization reaction and describe some of the important biochemical and structural features of RPE65 with respect to its membrane-binding and enzymatic properties. (C) 2010 Elsevier Ltd. All rights reserved.

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