二甲戊灵
硝基还原酶
枯草芽孢杆菌
化学
转位酶
酶
生物化学
生物
细菌
遗传学
农学
基因
染色体易位
杂草
作者
Haiyan Ni,Na Li,Meng Qian,Jian He,Qing Chen,Yunhong Huang,Long Zou,Zhong-er Long,Fei Wang
标识
DOI:10.1021/acs.jafc.9b04354
摘要
Microbial degradation plays a major role in the dissipation of pendimethalin, and nitroreduction is an initial and detoxicating step. Previously, a pendimethalin nitroreductase, PNR, was identified in Bacillus subtilis Y3. Here, another pendimethalin nitroreductase from strain Y3, LNR, was identified. LNR shares only 40% identity with PNR and reduces the aromatic ring C-6 nitro group of pendimethalin and both nitro groups of trifluralin, butralin, and oryzalin. The catalytic activities against the four dinitroanilines were much higher for LNR than for PNR. lnr deletion significantly reduced the pendimethalin-reduction activity (60% activity loss), while pnr deletion led to only 30% activity loss, indicating that both LNR and PNR were involved in pendimethalin nitroreduction in strain Y3; however, LNR played the major role. This study facilitates the elucidation of pendimethalin catabolism and provides degrading enzyme resources for the removal of dinitroaniline herbicide residues in environment and agricultural products.
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