Characterization of the Propham Biodegradation Pathway in Starkeya sp. Strain YW6 and Cloning of a Novel Amidase Gene mmH
文献类型： 外文期刊
作者： Sun, Lina 1 ; Gao, Xinhua 1 ; Chen, Wei 1 ; Huang, Kaihua 1 ; Bai, Naling 1 ; Lyu, Weiguang 1 ; Liu, Hongming 2 ;
作者机构： 1.Shanghai Acad Agr Sci, Ecoenvironm Protect Res Inst, Shanghai 201403, Peoples R China
2.Anhui Normal Univ, Inst Mol Biol & Biotechnol, Wuhu 241000, Anhui, Peoples R China
3.Shanghai Engn Res Ctr Low Carbon Agr SERCLA, Shanghai 201403, Peoples R China
4.Shanghai Key Lab Hort Technol, Shanghai 201403, Peoples R China
5.Minist Agr, Shanghai Agr Environm & Farmland Conservat Expt S, Shanghai 201403, Peoples R China
6.Environm Protect Monitoring Stn Shanghai, Shanghai 201403, Peoples R China
关键词： MmH; amidase; propham; gene cloning
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）
ISSN： 0021-8561
年卷期： 2019 年 67 卷 15 期
页码：
收录情况： SCI
摘要： We previously isolated a monocrotophos-degrading strain Starkeya sp. YW6, which could also degrade propham. Here, we show that strain YW6 metabolizes propham via a pathway in which propham is initially hydrolyzed to aniline and then converted to catechol, which is then oxidized via an ortho-cleavage pathway. The novel amidase gene mmH was cloned from strain YW6 and expressed in Escherichia coli BL21(DE3). MmH, which exhibits aryl acylamidase activity, was purified for enzymatic analysis. Bioinformatic analysis confirmed that MmH belongs to the amidase signature (AS) enzyme family and shares 26-50% identity with several AS family members. MmH (molecular mass of 53 kDa) was most active at 40 degrees C and pH 8.0 and showed high activity toward propham, with K-cat and K-m values of 33.4 s(-1) and 16.9 mu M, respectively. These characteristics make MmH suitable for novel amide biosynthesis and environmental remediation.
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