Membrane-binding and enzymatic properties of RPE65

被引：53

作者：

Kiser, Philip D. ^{[1
]}

Palczewski, Krzysztof ^{[1
]}

机构：

[1] Case Western Reserve Univ, Sch Med, Dept Pharmacol, Cleveland, OH 44106 USA

来源：

PROGRESS IN RETINAL AND EYE RESEARCH | 2010年 / 29卷 / 05期

关键词：

Retinoid isomerase; RPE65; Membrane protein; Metalloenzyme; Retinal pigment epithelium; Leber congenital amaurosis; RETINAL-PIGMENT EPITHELIUM; ALL-TRANS-RETINOL; 11-CIS-RETINOL DEHYDROGENASE GENE; LEBER CONGENITAL AMAUROSIS; ABSCISIC-ACID BIOSYNTHESIS; VISUAL CYCLE; ISOMEROHYDROLASE ACTIVITY; VITAMIN-A; PARTIAL-PURIFICATION; MICROSOMAL PROTEIN;

D O I：

10.1016/j.preteyeres.2010.03.002

中图分类号：

R77 [眼科学];

学科分类号：

100212 [眼科学];

摘要：

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.

引用

页码：428 / 442

页数：15

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