Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases

Asparaginyl endopeptidases (AEPs) are plant proteases that can also function as ligases, catalyzing the production of cyclic plant peptides. Here, the authors identify structural features that govern AEP ligase activity, providing insights to aid the discovery and engineering of ligase-type AEPs.

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Autores principales:	M. A. Jackson, E. K. Gilding, T. Shafee, K. S. Harris, Q. Kaas, S. Poon, K. Yap, H. Jia, R. Guarino, L. Y. Chan, T. Durek, M. A. Anderson, D. J. Craik
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1a99ceed0b0643118c6ddef2be35adf9
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spelling	oai:doaj.org-article:1a99ceed0b0643118c6ddef2be35adf92021-12-02T16:49:55ZMolecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases10.1038/s41467-018-04669-92041-1723https://doaj.org/article/1a99ceed0b0643118c6ddef2be35adf92018-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04669-9https://doaj.org/toc/2041-1723Asparaginyl endopeptidases (AEPs) are plant proteases that can also function as ligases, catalyzing the production of cyclic plant peptides. Here, the authors identify structural features that govern AEP ligase activity, providing insights to aid the discovery and engineering of ligase-type AEPs.M. A. JacksonE. K. GildingT. ShafeeK. S. HarrisQ. KaasS. PoonK. YapH. JiaR. GuarinoL. Y. ChanT. DurekM. A. AndersonD. J. CraikNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q M. A. Jackson E. K. Gilding T. Shafee K. S. Harris Q. Kaas S. Poon K. Yap H. Jia R. Guarino L. Y. Chan T. Durek M. A. Anderson D. J. Craik Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases
description	Asparaginyl endopeptidases (AEPs) are plant proteases that can also function as ligases, catalyzing the production of cyclic plant peptides. Here, the authors identify structural features that govern AEP ligase activity, providing insights to aid the discovery and engineering of ligase-type AEPs.
format	article
author	M. A. Jackson E. K. Gilding T. Shafee K. S. Harris Q. Kaas S. Poon K. Yap H. Jia R. Guarino L. Y. Chan T. Durek M. A. Anderson D. J. Craik
author_facet	M. A. Jackson E. K. Gilding T. Shafee K. S. Harris Q. Kaas S. Poon K. Yap H. Jia R. Guarino L. Y. Chan T. Durek M. A. Anderson D. J. Craik
author_sort	M. A. Jackson
title	Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases
title_short	Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases
title_full	Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases
title_fullStr	Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases
title_full_unstemmed	Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases
title_sort	molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/1a99ceed0b0643118c6ddef2be35adf9
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Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases

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