Crystal structure and site-directed mutagenesis of a nitroalkane oxidase from Streptomyces ansochromogenes |
| |
Authors: | Li Yanhua Gao Zengqiang Hou Haifeng Li Lei Zhang Jihui Yang Haihua Dong Yuhui Tan Huarong |
| |
Affiliation: | aState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;bBeijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China |
| |
Abstract: | Nitroalkane oxidase (NAO) catalyzes neutral nitroalkanes to their corresponding aldehydes or ketones, hydrogen peroxide and nitrite. The crystal structure of NAO from Streptomyces ansochromogenes was determined; it consists of two domains, a TIM barrel domain bound to FMN and C-terminal domain with a novel folding pattern. Site-directed mutagenesis of His179, which is spatially adjacent to FMN, resulted in the loss of enzyme activity, demonstrating that this amino acid residue is important for catalysis. The crystal structure of mutant H179D-nitroethane was also analyzed. Interestingly, Sa-NAO shows the typical function as nitroalkane oxidase but its structure is similar to that of 2-nitropropane dioxygenase. Overall, these results suggest that Sa-NAO is a novel nitroalkane oxidase with TIM barrel structure. |
| |
Keywords: | Nitroalkane oxidase Crystallization Site-directed mutagenesis TIM barrel |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|