Discovery of novel highly active and stable aspartate dehydrogenases

Abstract Aspartate family amino acids (AFAAs) have important commercial values due to their wide spectrum of applications. Most if not all AFAAs are produced under aerobic conditions which is energy-intensive. To establish a cost-effective anaerobic process for production of AFAAs, it holds great pr...

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Autores principales:	Hao Li, Taicheng Zhu, Liangtian Miao, Dan Zhang, Yongxian Li, Qi Li, Yin Li
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e7cb8903d4ae45d79b908595693c99c6
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spelling	oai:doaj.org-article:e7cb8903d4ae45d79b908595693c99c62021-12-02T12:32:58ZDiscovery of novel highly active and stable aspartate dehydrogenases10.1038/s41598-017-05522-72045-2322https://doaj.org/article/e7cb8903d4ae45d79b908595693c99c62017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05522-7https://doaj.org/toc/2045-2322Abstract Aspartate family amino acids (AFAAs) have important commercial values due to their wide spectrum of applications. Most if not all AFAAs are produced under aerobic conditions which is energy-intensive. To establish a cost-effective anaerobic process for production of AFAAs, it holds great promise to develop a new pathway enabling the conversion of oxoloacetate into aspartate through direct amination which is catalyzed by aspartate dehydrogenase (AspDH). Compared with the well studied aspartate aminotransferase and aspartate ammonia-lyase, only a few AspDHs are characterized till date, and failure to reproduce the high activity of AspDH from Rastonia eutropha documented in the literature encouraged us to screen and characterize novel AspDHs from different origins. Interestingly, the AspDHs from Klebsiella pneumoniae 34618 (KpnAspDH) and Delftia sp. Cs1–4 (DelAspDH) showed successful soluble expression. KpnAspDH and DelAspDH containing C-terminal hexa-histidine tags were purified and characterized for their catalytic properties. Notably, in addition to its high reductive amination activity, DelAspDH exhibited considerable stability as compared to the other source of AspDHs. This work thus provides novel enzyme resource for engineering strains capable of producing AFAAs under anaerobic conditions.Hao LiTaicheng ZhuLiangtian MiaoDan ZhangYongxian LiQi LiYin LiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hao Li Taicheng Zhu Liangtian Miao Dan Zhang Yongxian Li Qi Li Yin Li Discovery of novel highly active and stable aspartate dehydrogenases
description	Abstract Aspartate family amino acids (AFAAs) have important commercial values due to their wide spectrum of applications. Most if not all AFAAs are produced under aerobic conditions which is energy-intensive. To establish a cost-effective anaerobic process for production of AFAAs, it holds great promise to develop a new pathway enabling the conversion of oxoloacetate into aspartate through direct amination which is catalyzed by aspartate dehydrogenase (AspDH). Compared with the well studied aspartate aminotransferase and aspartate ammonia-lyase, only a few AspDHs are characterized till date, and failure to reproduce the high activity of AspDH from Rastonia eutropha documented in the literature encouraged us to screen and characterize novel AspDHs from different origins. Interestingly, the AspDHs from Klebsiella pneumoniae 34618 (KpnAspDH) and Delftia sp. Cs1–4 (DelAspDH) showed successful soluble expression. KpnAspDH and DelAspDH containing C-terminal hexa-histidine tags were purified and characterized for their catalytic properties. Notably, in addition to its high reductive amination activity, DelAspDH exhibited considerable stability as compared to the other source of AspDHs. This work thus provides novel enzyme resource for engineering strains capable of producing AFAAs under anaerobic conditions.
format	article
author	Hao Li Taicheng Zhu Liangtian Miao Dan Zhang Yongxian Li Qi Li Yin Li
author_facet	Hao Li Taicheng Zhu Liangtian Miao Dan Zhang Yongxian Li Qi Li Yin Li
author_sort	Hao Li
title	Discovery of novel highly active and stable aspartate dehydrogenases
title_short	Discovery of novel highly active and stable aspartate dehydrogenases
title_full	Discovery of novel highly active and stable aspartate dehydrogenases
title_fullStr	Discovery of novel highly active and stable aspartate dehydrogenases
title_full_unstemmed	Discovery of novel highly active and stable aspartate dehydrogenases
title_sort	discovery of novel highly active and stable aspartate dehydrogenases
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/e7cb8903d4ae45d79b908595693c99c6
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Discovery of novel highly active and stable aspartate dehydrogenases

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