期刊
CHEMICAL COMMUNICATIONS
卷 48, 期 13, 页码 1880-1882出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2cc17211a
关键词
-
资金
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [0952875] Funding Source: National Science Foundation
The conserved threonine (Thr) residue in the penultimate position of the leader peptide of lasso peptides microcin J25 and capistruin can be effectively replaced by several amino acids close in size and shape to Thr. These findings suggest a model for lasso peptide biosynthesis in which the Thr sidechain is a recognition element for the lasso peptide maturation machinery.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据