Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase

Amine dehydrogenases (AmDHs) catalyse the conversion of ketones into amines. Here, the authors created AmDH variants, the best of which showing a substrate-dependent stereo-switchable selectivity, affording either S- or R-configured amine products with up to >99.9% enantiomeric excess.

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Autores principales:	Vasilis Tseliou, Tanja Knaus, Marcelo F. Masman, Maria L. Corrado, Francesco G. Mutti
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/25ed70914fb742879be1c98e1f6f963c
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spelling	oai:doaj.org-article:25ed70914fb742879be1c98e1f6f963c2021-12-02T16:57:25ZGeneration of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase10.1038/s41467-019-11509-x2041-1723https://doaj.org/article/25ed70914fb742879be1c98e1f6f963c2019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11509-xhttps://doaj.org/toc/2041-1723Amine dehydrogenases (AmDHs) catalyse the conversion of ketones into amines. Here, the authors created AmDH variants, the best of which showing a substrate-dependent stereo-switchable selectivity, affording either S- or R-configured amine products with up to >99.9% enantiomeric excess.Vasilis TseliouTanja KnausMarcelo F. MasmanMaria L. CorradoFrancesco G. MuttiNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Vasilis Tseliou Tanja Knaus Marcelo F. Masman Maria L. Corrado Francesco G. Mutti Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase
description	Amine dehydrogenases (AmDHs) catalyse the conversion of ketones into amines. Here, the authors created AmDH variants, the best of which showing a substrate-dependent stereo-switchable selectivity, affording either S- or R-configured amine products with up to >99.9% enantiomeric excess.
format	article
author	Vasilis Tseliou Tanja Knaus Marcelo F. Masman Maria L. Corrado Francesco G. Mutti
author_facet	Vasilis Tseliou Tanja Knaus Marcelo F. Masman Maria L. Corrado Francesco G. Mutti
author_sort	Vasilis Tseliou
title	Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase
title_short	Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase
title_full	Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase
title_fullStr	Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase
title_full_unstemmed	Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase
title_sort	generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating l-lysine dehydrogenase
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/25ed70914fb742879be1c98e1f6f963c
work_keys_str_mv	AT vasilistseliou generationofaminedehydrogenaseswithincreasedcatalyticperformanceandsubstratescopefromedeaminatingllysinedehydrogenase AT tanjaknaus generationofaminedehydrogenaseswithincreasedcatalyticperformanceandsubstratescopefromedeaminatingllysinedehydrogenase AT marcelofmasman generationofaminedehydrogenaseswithincreasedcatalyticperformanceandsubstratescopefromedeaminatingllysinedehydrogenase AT marialcorrado generationofaminedehydrogenaseswithincreasedcatalyticperformanceandsubstratescopefromedeaminatingllysinedehydrogenase AT francescogmutti generationofaminedehydrogenaseswithincreasedcatalyticperformanceandsubstratescopefromedeaminatingllysinedehydrogenase
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Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase

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