A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors

Asparaginyl endopeptidases (AEPs) catalyze the cyclization step during the biosynthesis of cyclic peptides in plants. Here, the authors report a recombinantly produced AEP that catalyzes the backbone cyclization of a linear cyclotide precursor and an engineered analog with high efficiency and in a p...

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Autores principales:	Junqiao Du, Kuok Yap, Lai Yue Chan, Fabian B. H. Rehm, Fong Yang Looi, Aaron G. Poth, Edward K. Gilding, Quentin Kaas, Thomas Durek, David J. Craik
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2374d960c8e2417095bdec822494ebdd
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spelling	oai:doaj.org-article:2374d960c8e2417095bdec822494ebdd2021-12-02T14:40:42ZA bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors10.1038/s41467-020-15418-22041-1723https://doaj.org/article/2374d960c8e2417095bdec822494ebdd2020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15418-2https://doaj.org/toc/2041-1723Asparaginyl endopeptidases (AEPs) catalyze the cyclization step during the biosynthesis of cyclic peptides in plants. Here, the authors report a recombinantly produced AEP that catalyzes the backbone cyclization of a linear cyclotide precursor and an engineered analog with high efficiency and in a pH-dependent manner.Junqiao DuKuok YapLai Yue ChanFabian B. H. RehmFong Yang LooiAaron G. PothEdward K. GildingQuentin KaasThomas DurekDavid J. CraikNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Junqiao Du Kuok Yap Lai Yue Chan Fabian B. H. Rehm Fong Yang Looi Aaron G. Poth Edward K. Gilding Quentin Kaas Thomas Durek David J. Craik A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors
description	Asparaginyl endopeptidases (AEPs) catalyze the cyclization step during the biosynthesis of cyclic peptides in plants. Here, the authors report a recombinantly produced AEP that catalyzes the backbone cyclization of a linear cyclotide precursor and an engineered analog with high efficiency and in a pH-dependent manner.
format	article
author	Junqiao Du Kuok Yap Lai Yue Chan Fabian B. H. Rehm Fong Yang Looi Aaron G. Poth Edward K. Gilding Quentin Kaas Thomas Durek David J. Craik
author_facet	Junqiao Du Kuok Yap Lai Yue Chan Fabian B. H. Rehm Fong Yang Looi Aaron G. Poth Edward K. Gilding Quentin Kaas Thomas Durek David J. Craik
author_sort	Junqiao Du
title	A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors
title_short	A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors
title_full	A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors
title_fullStr	A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors
title_full_unstemmed	A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors
title_sort	bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/2374d960c8e2417095bdec822494ebdd
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A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors

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