[Advances in phytoene dehydrogenase - A review].

微生物学报 Pub Date : 2016-11-04
Chunji Li, Bingxue Li, Xiaori Han
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Abstract

Carotenoids, as a group of over 700 valuable unsaturated terpene compounds classified as carotene and xanthophyll family, are endowed with powerful nutritional value. Phytoene dehydrogenase is the key rate-limiting enzyme in carotenoids biosynthesis pathway, involved in catalyzing the conversion from colorless hydrocarbon phytoene to other pigmented carotenoids, and plays an essential central regulation role. The function of phytoene dehydrogenases from different organisms exist diversity. CrtP, CrtQ and isomerase CrtH are essential for the formation of lycopene in most Cyanobacteria, whereas PDS, ZDS and isomerase Z-ISO, CrtISO are in charge of producing lycopene in most algae and plants. Nevertheless, there is only one CrtI-type for the formation of neurosporene, lycopene or dehydrolycopene in most bacteria and fungi. In this review, isolation, characterization, functional diversity, transcription regulatory mechanisms and phylogenetic analysis of phytoene dehydrogenase from different organisms are illustrated. This paper will provide insights into phytoene dehydrogenase and may facilitate the optimization of carotenoids production in genetic engineering strategy.

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[植物烯脱氢酶研究进展]。
类胡萝卜素是一组700多种有价值的不饱和萜化合物,属于胡萝卜素和叶黄素家族,具有强大的营养价值。植物烯脱氢酶是类胡萝卜素生物合成途径中关键的限速酶,参与催化无色烃类植物烯向其他色素类胡萝卜素转化,起着重要的中心调控作用。植物烯脱氢酶在不同生物体内的功能存在差异。在大多数蓝藻中,CrtP、CrtQ和异构酶CrtH对番茄红素的形成至关重要,而在大多数藻类和植物中,PDS、ZDS和异构酶Z-ISO、CrtISO负责番茄红素的产生。然而,在大多数细菌和真菌中,只有一种crti类型形成神经红素,番茄红素或脱氢番茄红素。本文综述了植物烯脱氢酶的分离、鉴定、功能多样性、转录调控机制和系统发育分析。本文将为植物烯脱氢酶的研究提供新的见解,并有助于优化类胡萝卜素的基因工程生产策略。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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期刊介绍: Acta Microbiologica Sinica(AMS) is a peer-reviewed monthly (one volume per year)international journal,founded in 1953.It covers a wide range of topics in the areas of general and applied microbiology.The journal publishes original papers,reviews in microbiological science,and short communications describing unusual observations. Acta Microbiologica Sinica has been indexed in Index Copernicus (IC),Chemical Abstract (CA),Excerpt Medica Database (EMBASE),AJ of Viniti (Russia),Biological Abstracts (BA),Chinese Science Citation Database (CSCD),China National Knowledge Infrastructure(CNKI),Institute of Scientific and Technical Information of China(ISTIC),Chinese Journal Citation Report(CJCR),Chinese Biological Abstracts,Chinese Pharmaceutical Abstracts,Chinese Medical Abstracts and Chinese Science Abstracts.
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