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| The Structural Studies of 6-Hydroxy-3-succinoyl-pyridine Monooxygenase |
| LI Peng-peng1, YU Hao1,2, XU Ping1, TANG Hong-zhi1 |
1. State Key Laboratory of Microbial Metabolism, School of Life Science and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China;
2. Collage of Life Science, Qingdao Agriculture University, Qingdao 266109, China |
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Abstract Pyridine derivatives are the important value-added chemicals, and biocatalysis is a potential technology for the industrial synthesis of pyridine derivatives. The structure information of 6-hydroxy-3-succinoyl-pyridine monooxygenase (HspB) by mutant construction was investigated. The space structure of HspB has been built through computer modeling and docked with its substrate HSP(2,5-dihydroxy-pyridine). Then 25 mutations of HspB were constructed and studied, according to molecular simulation, sequence alignment, and homologous crystal references. All the mutants have been expressed and purified, and the kinetic parameters of soluble mutants have been measured. According to the properties of mutants, it can infer that the correct binding of FAD possesses important roles in protein stability, and moreover, substrate HSP, and co-enzyme NADH live in the same activity center in HSP but interact with different amino acids. The structure information will help us for the industrial application of pyridine monooxygenase.
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Received: 13 March 2015
Published: 25 August 2015
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