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填补维生素A研究的空白。一种将β-胡萝卜素裂解为视黄醛的酶的分子鉴定。

Filling the gap in vitamin A research. Molecular identification of an enzyme cleaving beta-carotene to retinal.

作者信息

von Lintig J, Vogt K

机构信息

Albert-Ludwig Universität Freiburg, Institut für Biologie I, Neurobiologie und Tierphysiologie, D-79104 Freiburg, Germany.

出版信息

J Biol Chem. 2000 Apr 21;275(16):11915-20. doi: 10.1074/jbc.275.16.11915.

Abstract

Vitamin A and its derivatives (retinoids) are essential components in vision; they contribute to pattern formation during development and exert multiple effects on cell differentiation with important clinical implications. It has been known for 50 years that the key step in the formation of vitamin A is the oxidative cleavage of beta-carotene; however, this enzymatic step has resisted molecular analysis. A novel approach enabled us to clone and identify a beta-carotene dioxygenase from Drosophila melanogaster, expressing it into the background of a beta-carotene (provitamin A)-synthesizing and -accumulating Escherichia coli strain. The carotene-cleaving enzyme, identified here for the first time on the molecular level, is the basis of the numerous branches of vitamin A action and links plant and animal carotene metabolism.

摘要

维生素A及其衍生物(类视黄醇)是视觉的重要组成部分;它们在发育过程中有助于模式形成,并对细胞分化产生多种影响,具有重要的临床意义。五十年来人们一直知道,维生素A形成的关键步骤是β-胡萝卜素的氧化裂解;然而,这一酶促步骤一直难以进行分子分析。一种新方法使我们能够从黑腹果蝇中克隆并鉴定出一种β-胡萝卜素双加氧酶,并将其表达于一种合成并积累β-胡萝卜素(维生素A原)的大肠杆菌菌株的背景中。这种首次在分子水平上鉴定出的胡萝卜素裂解酶,是维生素A作用众多分支的基础,它连接了植物和动物的胡萝卜素代谢。

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