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嗜热有机磷水解酶/内酯酶在环境和人类健康中的应用。

Hyperthermophilic phosphotriesterases/lactonases for the environment and human health.

机构信息

Institute of Protein Biochemistry (IBP), National Research Council (CNR), Naples, Italy.

出版信息

Environ Technol. 2010 Sep;31(10):1115-27. doi: 10.1080/09593331003789529.

DOI:10.1080/09593331003789529
PMID:20718294
Abstract

In the last decades the idea to use enzymes for environmental bioremediation has been more and more proposed and, in the light of this, new solutions have been suggested and detailed studies on some classes of enzymes have been performed. In particular, our attention in the last few years has been focused on the enzymes belonging to the amidohydrolase superfamily. Several members of this superfamily are endowed with promiscuous activities. The term 'catalytic promiscuity' describes the capability of an enzyme to catalyse different chemical reactions, called secondary activities, at the active site responsible for the main activity. Recently, a new family of microbial lactonases with promiscuous phosphotriesterase activity, dubbed PTE-Like Lactonase (PLL), has been ascribed to the amidohydrolase superfamily. Among members of this family are enzymes found in the archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius, which show high thermophilicity and thermal resistance. Enzymes showing phosphotriesterase activity are attractive from a biotechnological point of view because they are capable of hydrolysing the organophosphate phosphotriesters (OPs), a class of synthetic compounds employed worldwide both as insecticides and chemical warfare agents. Furthermore, from a basic point of view, studies of catalytic promiscuity offer clues to understand natural evolution of enzymes and to translate this into in vitro adaptation of enzymes to specific human needs. Thermostable enzymes able to hydrolyse OPs are considered good candidates for the set-up of efficient detoxification tools.

摘要

在过去的几十年里,人们越来越多地提出利用酶进行环境生物修复的想法,因此,人们提出了新的解决方案,并对某些类别的酶进行了详细研究。特别是,在过去几年中,我们的注意力一直集中在属于酰胺水解酶超家族的酶上。该超家族的几个成员具有混杂的活性。“催化混杂”一词描述了一种酶在负责主要活性的活性部位催化不同化学反应(称为次要活性)的能力。最近,一种新的具有混杂磷酸三酯酶活性的微生物内酯酶家族,被称为 PTE-Like Lactonase(PLL),被归入酰胺水解酶超家族。在这个家族的成员中,有在古菌 Sulfolobus solfataricus 和 Sulfolobus acidocaldarius 中发现的酶,它们表现出高热稳定性和耐热性。具有磷酸三酯酶活性的酶从生物技术的角度来看很有吸引力,因为它们能够水解有机磷酸酯磷酸三酯(OPs),这是一类在全球范围内用作杀虫剂和化学战剂的合成化合物。此外,从基础的角度来看,对催化混杂的研究为理解酶的自然进化提供了线索,并将其转化为酶在体外适应特定人类需求的能力。能够水解 OPs 的热稳定酶被认为是建立高效解毒工具的良好候选物。

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Environ Technol. 2010 Sep;31(10):1115-27. doi: 10.1080/09593331003789529.
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