Promiscuous esterase activities of the C-C hydrolases from Dyella ginsengisoli.

Hao Zhou, Yuanyuan Qu, Chunlei Kong, Yingge Wu, Kang Zhu, Jie Yang, Jiti Zhou

State Key Laboratory of Fine Chemicals and Industrial Ecology and Environmental Engineering (Ministry of Education, China), School of Environmental Science and Technology, Dalian University of Technology, Dalian, China.

Biotechnology letters 2012 Jun

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A C-C hydrolase gene (bphD(LA-4)) from strain Dyella ginsengisoli LA-4 was cloned and expressed in Escherichia coli BL21 (DE3). BphD(LA-4) together with another hydrolase MfphA(LA-4), which derived from the same strain, possessed esterase activities. p-Nitrophenyl butyrate was the best substrate for both enzymes. BphD(LA-4) had high catalytic efficiency to p-nitrophenyl benzoate, whereas MfphA(LA-4) had no activity. Homology modeling and docking studies demonstrated that the proper hydrogen bond interaction was important for the reactivity of specific substrate.

Citation

Hao Zhou, Yuanyuan Qu, Chunlei Kong, Yingge Wu, Kang Zhu, Jie Yang, Jiti Zhou. Promiscuous esterase activities of the C-C hydrolases from Dyella ginsengisoli. Biotechnology letters. 2012 Jun;34(6):1107-13