求是理学论坛�Per Berglund

报告题目：Promiscuous Enzymes for Biocatalysis 报告人：Prof. Per Berglund                 生物化学教授，瑞典皇家工学院副教务长 单   位：瑞典皇家工学院 报告时间：2011年4月28日（周四）上午10:00 报告地点：浙江大学玉泉校区化学楼，教八–107

报告简介：

Enzyme catalysis is based on two principal steps, binding of the substrate(s) and stabilisation of the transition state. There are many examples on the use of protein engineering to change the binding site to achieve altered substrate specificity. However the catalytic site, which stabilizes the transition state, has almost exclusively been mutated to study the role of specific amino acid residues in the reaction mechanisms. This project focuses on changes of reaction specificities of lipases, where the main effort and the new challenge are to alter the catalytic site to facilitate catalysis of new reactions. Serine hydrolase enzymes are very well studied at a molecular level, many 3D structures are available, and the reaction mechanism is well known. The active site of these enzymes is designed by nature for catalysing ester bond cleavage or synthesis. We are taking advantage of part of this catalytic machinery for alternative promiscuous reactions such as carbon-carbon bond forming reactions. This is a multidisciplinary project integrating enzymology, molecular biology and organic chemistry. The experimental work is guided and followed up by computational techniques. 
 
报告人简介：
Professor in Biochemistry
1995 Ph.D. Organic Chemistry, Mid Sweden University, Sundsvall
1995-96 Postdoctoral fellow at University of Toronto, Canada
1997-2001 Assistant professor at KTH Biotechnology, Stockholm, Sweden
2000 Associate professor organic chemistry at KTH
2002-2009 Senior lecturer at division of biochemistry, KTH
2006-2010 Director of Undergraduate and Masters' studies at KTH Biotechnology
2009-at present Professor Biochemistry, School of Biotechnology, KTH
2010- Vice Dean of Faculty at KTH, Responsible for educational structure and content