【摘 要】
：
A carboxylesterase(E8)has been identified in a marine bacterium,Croceicoccus marinus from the East Pacific and has been cloned and overexpressed in Escherichia coli.E8 is a novel esterase that doesnt
【机 构】
：
State Key Laboratory of Genetic Engineering,Collaborative Innovation Center of Genetics and Developm
【出 处】
：
中国生物化学与分子生物学会2016年全国学术会议
论文部分内容阅读
A carboxylesterase(E8)has been identified in a marine bacterium,Croceicoccus marinus from the East Pacific and has been cloned and overexpressed in Escherichia coli.E8 is a novel esterase that doesnt belong to any known family.Biochemical characterization revealed that E8 has a preference for p-nitrophenyl esters with shortchain acyl esters(shorter than 10 carbon atoms),especially p-nitrophenyl butyrate,and exhibites optimal activity at 50℃ and at pH 7.5.We solved the crystal structure of E8 at 1.5 (A)-resolution,which revealed a classical-hydro laαse/βdomain with a catalytic triad consisting of Ser77,Asp101 and His222.Mutation studies confirmed that the active sites of E8 were highly conserved among esterase family.As E8 has high enzymatic activity and only shares low homology with other esterases,it could be a potential candidate for industrial enzymes.
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