Hyperthermophilic(Phosphotri)esterases/lactonases:structure,functionandpossibleapplications

发布时间 :2012-10-22  阅读次数 :573

 

报告题目: Hyperthermophilic (Phosphotri)esterases/lactonases: structure, function and possible applications
报 告 人:Prof. Giuseppe Manco
Institute of Protein Biochemistry
National Research Council of Italy,
报告时间: 2012.10.23(星期二)  上午9:30
报告地点: 生命学院3-105会议室
联系人:  杨广宇
摘要:

Recently, we have discovered, dubbed PTE-Like Lactonases (PLL) and ascribed to the amidohydrolase superfamily. a new family of microbial lactonases with promiscuous phosphotriesterase activity. Among members of this family are enzymes found in the Archaea: Sulfolobus solfataricus and Sulfolobus acidocaldarius, which show high thermophilicity and thermal resistance. From a biotechnological point of view enzymes endowed with phosphotriesterase activity are attractive objects of study because are capable to hydrolyse the organophosphate phosphotriesters (OPs), a class of worldwide used synthetic compounds employed both as insecticides and chemical warfare agents. From the viewpoint of basic research, studies of catalytic promiscuity offer clues to understand the natural evolution of enzymes and to translate this knowledge into in vitro adaptation of catalysts to specific human needs. Thermostable enzymes able to hydrolyse natural lactones and promiscuously OPs are currently considered good candidates for the set-up of efficient anti-microbial and detoxification tools. We will report on our attempts to follow these two paths.

报告人简介:

Dr Giuseppe Manco is senior Researcher (Primo Ricercatore) and Group Leader at the Institute of Protein Biochemistry, CNR, Naples, Italy.

Its main research line is the study of the structure-function relationship in enzymes from the viewpoint of understanding the determinants that underlay (thermal)stability and the molecular processes which control the substrate recognition, enzyme inhibition and enzyme catalysis. The tasks are approached mainly by studying enzymes from (hyper)thermophilic sources, and are also performed by comparison with mesophilic, homologous counterparts, which allow tracing back evolution of enzyme activity by looking at sequence/structure hallmarks and promiscuous activities. Furthermore, the potential uses of these enzymes in the industry, for the environment and for human health are investigated.

Dr Manco since 1987 has co-authored over 100 publications and has been responsible of several national and international projects.

 

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