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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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
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spelling ftpekinguniv:oai:localhost:20.500.11897/189651 2023-05-15T13:50:36+02:00 Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation Dai, Xiongfeng Zhu, Manlu Wang, Yi-Ping 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. 2014 https://hdl.handle.net/20.500.11897/189651 https://doi.org/10.1039/c3cc48722a en eng chemical communications CHEMICAL COMMUNICATIONS.2014,50,(15),1830-1832. 654100 1359-7345 http://hdl.handle.net/20.500.11897/189651 1364-548X doi:10.1039/c3cc48722a 24402609 WOS:000330774500013 PubMed SCI DIRECTED EVOLUTION INCREMENTAL TRUNCATION HERBICIDE RESISTANCE CANDIDA-ANTARCTICA LIPASE-B GENES DOMAIN Journal 2014 ftpekinguniv https://doi.org/20.500.11897/189651 https://doi.org/10.1039/c3cc48722a 2021-08-01T08:20:53Z 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 Journal/Newspaper Antarc* Antarctica Peking University Institutional Repository (PKU IR) Chem. Commun. 50 15 1830 1832
institution Open Polar
collection Peking University Institutional Repository (PKU IR)
op_collection_id ftpekinguniv
language English
topic DIRECTED EVOLUTION
INCREMENTAL TRUNCATION
HERBICIDE RESISTANCE
CANDIDA-ANTARCTICA
LIPASE-B
GENES
DOMAIN
spellingShingle DIRECTED EVOLUTION
INCREMENTAL TRUNCATION
HERBICIDE RESISTANCE
CANDIDA-ANTARCTICA
LIPASE-B
GENES
DOMAIN
Dai, Xiongfeng
Zhu, Manlu
Wang, Yi-Ping
Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation
topic_facet DIRECTED EVOLUTION
INCREMENTAL TRUNCATION
HERBICIDE RESISTANCE
CANDIDA-ANTARCTICA
LIPASE-B
GENES
DOMAIN
description 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
author2 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
author Dai, Xiongfeng
Zhu, Manlu
Wang, Yi-Ping
author_facet Dai, Xiongfeng
Zhu, Manlu
Wang, Yi-Ping
author_sort Dai, Xiongfeng
title Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation
title_short Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation
title_full Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation
title_fullStr Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation
title_full_unstemmed Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation
title_sort circular permutation of e. coli epsp synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation
publisher chemical communications
publishDate 2014
url https://hdl.handle.net/20.500.11897/189651
https://doi.org/10.1039/c3cc48722a
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source PubMed
SCI
op_relation CHEMICAL COMMUNICATIONS.2014,50,(15),1830-1832.
654100
1359-7345
http://hdl.handle.net/20.500.11897/189651
1364-548X
doi:10.1039/c3cc48722a
24402609
WOS:000330774500013
op_doi https://doi.org/20.500.11897/189651
https://doi.org/10.1039/c3cc48722a
container_title Chem. Commun.
container_volume 50
container_issue 15
container_start_page 1830
op_container_end_page 1832
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