Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step

Han Zhang et al. report molecular dynamics simulations and mutational analysis of a key process of the E. coli glycine cleavage system, an important enzyme complex in C1 metabolism. They identify a key amino acid residue controlling the release of the swinging aminomethyl lipoate arm and increase th...

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Autores principales: Han Zhang, Yuchen Li, Jinglei Nie, Jie Ren, An-Ping Zeng
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/78e895b2a82e49aea72b3a9bd99928e3
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spelling oai:doaj.org-article:78e895b2a82e49aea72b3a9bd99928e32021-12-02T11:43:43ZStructure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step10.1038/s42003-020-01401-62399-3642https://doaj.org/article/78e895b2a82e49aea72b3a9bd99928e32020-12-01T00:00:00Zhttps://doi.org/10.1038/s42003-020-01401-6https://doaj.org/toc/2399-3642Han Zhang et al. report molecular dynamics simulations and mutational analysis of a key process of the E. coli glycine cleavage system, an important enzyme complex in C1 metabolism. They identify a key amino acid residue controlling the release of the swinging aminomethyl lipoate arm and increase the overall reaction rate of glycine cleavage by more than twice, providing a strategy for manipulating this reaction system for use in synthetic biology.Han ZhangYuchen LiJinglei NieJie RenAn-Ping ZengNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 3, Iss 1, Pp 1-12 (2020)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Han Zhang
Yuchen Li
Jinglei Nie
Jie Ren
An-Ping Zeng
Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step
description Han Zhang et al. report molecular dynamics simulations and mutational analysis of a key process of the E. coli glycine cleavage system, an important enzyme complex in C1 metabolism. They identify a key amino acid residue controlling the release of the swinging aminomethyl lipoate arm and increase the overall reaction rate of glycine cleavage by more than twice, providing a strategy for manipulating this reaction system for use in synthetic biology.
format article
author Han Zhang
Yuchen Li
Jinglei Nie
Jie Ren
An-Ping Zeng
author_facet Han Zhang
Yuchen Li
Jinglei Nie
Jie Ren
An-Ping Zeng
author_sort Han Zhang
title Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step
title_short Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step
title_full Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step
title_fullStr Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step
title_full_unstemmed Structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step
title_sort structure-based dynamic analysis of the glycine cleavage system suggests key residues for control of a key reaction step
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/78e895b2a82e49aea72b3a9bd99928e3
work_keys_str_mv AT hanzhang structurebaseddynamicanalysisoftheglycinecleavagesystemsuggestskeyresiduesforcontrolofakeyreactionstep
AT yuchenli structurebaseddynamicanalysisoftheglycinecleavagesystemsuggestskeyresiduesforcontrolofakeyreactionstep
AT jingleinie structurebaseddynamicanalysisoftheglycinecleavagesystemsuggestskeyresiduesforcontrolofakeyreactionstep
AT jieren structurebaseddynamicanalysisoftheglycinecleavagesystemsuggestskeyresiduesforcontrolofakeyreactionstep
AT anpingzeng structurebaseddynamicanalysisoftheglycinecleavagesystemsuggestskeyresiduesforcontrolofakeyreactionstep
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