Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation

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 s...

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Bibliographic Details
Published in:Chem. Commun.
Main Authors: Dai, Xiongfeng, Zhu, Manlu, Wang, Yi-Ping
Other Authors: Wang, YP (reprint author), Beijing Univ, Sch Life Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China., Beijing Univ, Sch Life Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China.
Format: Journal/Newspaper
Language:English
Published: chemical communications 2014
Subjects:
DIRECTED EVOLUTION
INCREMENTAL TRUNCATION
HERBICIDE RESISTANCE
CANDIDA-ANTARCTICA
LIPASE-B
GENES
DOMAIN
Antarc*
Antarctica
Online Access:https://hdl.handle.net/20.500.11897/189651
https://doi.org/10.1039/c3cc48722a
Description
Summary: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. http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000330774500013&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 Chemistry, Multidisciplinary SCI(E) PubMed 4 ARTICLE wangyp@pku.edu.cn 15 1830-1832 50

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