title: Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation.
abstract: We performed the first circular permutation analysis for E. coli 5-enolpyruvylshikimate-3-phosphate synthase, and identified one circular permutant with notably increased resistance to its specific inhibitor and several others with moderately improved catalytic activity. Valid circular permutation sites can be used as effective split sites of protein fragment complementation.
authors.affiliation: State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, 100871, China. wangyp@pku.edu.cn.
authors.forename: Xiongfeng
authors.initials: X
authors.lastname: Dai
authors.forename: Manlu
authors.initials: M
authors.lastname: Zhu
authors.forename: Yi-Ping
authors.initials: YP
authors.lastname: Wang
mesh_terms: D051229:3-Phosphoshikimate 1-Carboxyvinyltransferase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D055162:Biocatalysis; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology*; D005998:Glycine / Q000031:analogs & derivatives / Q000494:pharmacology; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D000097797:Glyphosate
chemical_list: D051229:3-Phosphoshikimate 1-Carboxyvinyltransferase; D004791:Enzyme Inhibitors; D005998:Glycine; D000097797:Glyphosate