Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases

Regioselective prenylation of small aromatic natural molecules is crucial for their biological activity. Here, the authors present the biochemical and structural characterisation of two prenyltransferases and a structure-based engineering strategy to modulate their substrate specificity.

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Main Authors:	Takahiro Mori, Lihan Zhang, Takayoshi Awakawa, Shotaro Hoshino, Masahiro Okada, Hiroyuki Morita, Ikuro Abe
Format:	article
Language:	EN
Published:	Nature Portfolio 2016
Subjects:	Science Q
Online Access:	https://doaj.org/article/1d1274fc43d442cab02cdc00a5e5fe6f
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spelling	oai:doaj.org-article:1d1274fc43d442cab02cdc00a5e5fe6f2021-12-02T17:32:05ZManipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases10.1038/ncomms108492041-1723https://doaj.org/article/1d1274fc43d442cab02cdc00a5e5fe6f2016-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms10849https://doaj.org/toc/2041-1723Regioselective prenylation of small aromatic natural molecules is crucial for their biological activity. Here, the authors present the biochemical and structural characterisation of two prenyltransferases and a structure-based engineering strategy to modulate their substrate specificity.Takahiro MoriLihan ZhangTakayoshi AwakawaShotaro HoshinoMasahiro OkadaHiroyuki MoritaIkuro AbeNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Takahiro Mori Lihan Zhang Takayoshi Awakawa Shotaro Hoshino Masahiro Okada Hiroyuki Morita Ikuro Abe Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases
description	Regioselective prenylation of small aromatic natural molecules is crucial for their biological activity. Here, the authors present the biochemical and structural characterisation of two prenyltransferases and a structure-based engineering strategy to modulate their substrate specificity.
format	article
author	Takahiro Mori Lihan Zhang Takayoshi Awakawa Shotaro Hoshino Masahiro Okada Hiroyuki Morita Ikuro Abe
author_facet	Takahiro Mori Lihan Zhang Takayoshi Awakawa Shotaro Hoshino Masahiro Okada Hiroyuki Morita Ikuro Abe
author_sort	Takahiro Mori
title	Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases
title_short	Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases
title_full	Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases
title_fullStr	Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases
title_full_unstemmed	Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases
title_sort	manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/1d1274fc43d442cab02cdc00a5e5fe6f
work_keys_str_mv	AT takahiromori manipulationofprenylationreactionsbystructurebasedengineeringofbacterialindolactamprenyltransferases AT lihanzhang manipulationofprenylationreactionsbystructurebasedengineeringofbacterialindolactamprenyltransferases AT takayoshiawakawa manipulationofprenylationreactionsbystructurebasedengineeringofbacterialindolactamprenyltransferases AT shotarohoshino manipulationofprenylationreactionsbystructurebasedengineeringofbacterialindolactamprenyltransferases AT masahirookada manipulationofprenylationreactionsbystructurebasedengineeringofbacterialindolactamprenyltransferases AT hiroyukimorita manipulationofprenylationreactionsbystructurebasedengineeringofbacterialindolactamprenyltransferases AT ikuroabe manipulationofprenylationreactionsbystructurebasedengineeringofbacterialindolactamprenyltransferases
_version_	1718380353731690496

Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases

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