Structural insights into the mechanism for recognizing substrate of the cytochrome P450 enzyme TxtE.
作者: Feng YuMinjun LiChunyan XuZhijun WangHuan ZhouMin YangYaxing ChenLin TangJianhua He
刊名: PLoS ONE, 2018, Vol.8 (11)
来源数据库: Directory of Open Access Journals
DOI: 10.1371/journal.pone.0081526
原始语种摘要: Thaxtomins, a family of phytotoxins produced by Streptomyces spp., can cause dramatic plant cell hypertrophy and seedling stunting. Thaxtomin A is the dominant form from Streptomyces scabies and has demonstrated herbicidal action. TxtE, a cytochrome P450 enzyme from Streptomyces scabies 87.22, catalyzes direct nitration of the indolyl moiety of L-tryptophan to L-4-nitrotryptophan using nitric oxide, dioxygen and NADPH. The crystal structure of TxtE was determined at 2.1 Å resolution and described in this work. A clearly defined substrate access channel is observed and can be classified as channel 2a, which is common in bacteria cytochrome P450 enzymes. A continuous hydrogen bond chain from the active site to the external solvent is observed. Compared with other cytochrome P450 enzymes,...
全文获取路径: DOAJ  (合作)
影响因子:3.73 (2012)

  • cytochrome 细胞色素
  • substrate 基质
  • tryptophan 色氨酸
  • enzyme 
  • binding 装订
  • scabies 疥疮
  • docking 靠泊
  • potentially 可能地
  • recognition 识别
  • recognizing 识别