Asn336 is involved in the substrate affinity of glycine oxidase from Bacillus cereus
作者: Gaobing WuTao ZhanYiming GuoAshok KumarZiduo Liu
作者单位: 1State Key Laboratory of Agricultural Microbiology, College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, China
2State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China
刊名: Electronic Journal of Biotechnology, 2016, Vol.22 , pp.26-30
来源数据库: Elsevier Journal
DOI: 10.1016/j.ejbt.2016.02.009
关键词: Bacillus cereusError-prone PCRGlycine oxidaseSite-directed mutagenesisSubstrate affinity
原始语种摘要: Abstract(#br)Background(#br)Glycine oxidase (GO), a type of d -amino acid oxidase, is of biotechnological interest for its potential in several fields. In our previous study, we have characterized a new glycine oxidase (BceGO) from Bacillus cereus HYC-7. Here, a variant of N336K with increased the affinity against all the tested substrate was obtained by screening a random mutant library of BceGO. It is observed that the residue N336 is invariable between its homogeneous enzymes. This work was aimed to explore the role of the residue N336 in glycine oxidase by site-directed mutagenesis, kinetic assay, structure modeling and substrate docking.(#br)Results(#br)The results showed that the affinity of N336H, N336K and N336R increased gradually toward all the substrates, with increase in...
全文获取路径: Elsevier  (合作)
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关键词翻译
关键词翻译
  • affinity 亲和力
  • substrate 基质
  • glycine 甘氨酸
  • involved 涉及
  • cereus 仙人掌
  • oxidase 氧化酶
  • mutagenesis 突变形成
  • random 随机的
  • increased 增加
  • isoalloxazine 异咯嗪