Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.
Institute for Biodiversity and Ecosystem Dynamics, University of Amsterdam , Science Park 904, 1098 XH Amsterdam, The Netherlands.
J Agric Food Chem. 2017 Jul 12;65(27):5453-5462. doi: 10.1021/acs.jafc.7b01333. Epub 2017 Jun 30.
The two-spotted spider mite Tetranychus urticae is a polyphagous agricultural pest and poses a high risk to global crop production as it is rapidly developing pesticide resistance. Genomic and transcriptomic analysis has revealed the presence of a remarkable cyanase gene in T. urticae and related mite species within the Acariformes lineage. Cyanase catalyzes the detoxification of cyanate and is potentially an attractive protein target for the development of new acaricides. Phylogenetic analysis indicates that within the Acariformes, the cyanase gene originates from a single horizontal gene transfer event, which precedes subsequent speciation. Our structural studies presented here compare and contrast prokaryotic cyanases to T. urticae cyanase, which all form homodecamers and have conserved active site residues, but display different surface areas between homodimers in the overall decameric structure.
二斑叶螨（Tetranychus urticae）是一种多食性农业害虫，由于其对农药的快速抗性发展，对全球作物生产构成了高风险。基因组和转录组分析表明，在蜱螨目谱系中，二斑叶螨及其相关螨种存在一种显著的氰酸酶基因。氰酸酶催化氰酸盐的解毒，可能是开发新型杀螨剂的有吸引力的蛋白靶标。系统发育分析表明，在蜱螨目中，氰酸酶基因源自单一的水平基因转移事件，该事件先于随后的物种形成。我们在此呈现的结构研究将原核氰酸酶与二斑叶螨的氰酸酶进行了比较和对比，两者均形成同源三聚体，具有保守的活性位点残基，但在整个十聚体结构中，同源二聚体之间的表面积不同。
