Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach

Abstract Recently, the program INTMSAlign_HiSol for identifying aggregation hotspots in proteins only requiring secondary structure data was introduced. We explored the utility of this program further and applied it for engineering of the aldoxime dehydratase from Bacillus sp. OxB-1. Towards this en...

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Autores principales:	Keiko Oike, Jens Sproß, Daisuke Matsui, Yasuhisa Asano, Harald Gröger
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/07ea2c0a72214d78b00d5898091ddd88
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spelling	oai:doaj.org-article:07ea2c0a72214d78b00d5898091ddd882021-12-02T16:14:09ZProtein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach10.1038/s41598-021-92749-02045-2322https://doaj.org/article/07ea2c0a72214d78b00d5898091ddd882021-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-92749-0https://doaj.org/toc/2045-2322Abstract Recently, the program INTMSAlign_HiSol for identifying aggregation hotspots in proteins only requiring secondary structure data was introduced. We explored the utility of this program further and applied it for engineering of the aldoxime dehydratase from Bacillus sp. OxB-1. Towards this end, the effect of inverting the hydropathy at selected positions of the amino acid sequence on the enzymatic activity was studied leading to 60% of our constructed variants, which showed improved activity. In part, this activity increase can be rationalised by an improved heme incorporation of the variants. For example, a single mutation gave a 1.8 fold increased enzymatic activity and 30% improved absolute heme incorporation.Keiko OikeJens SproßDaisuke MatsuiYasuhisa AsanoHarald GrögerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Keiko Oike Jens Sproß Daisuke Matsui Yasuhisa Asano Harald Gröger Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach
description	Abstract Recently, the program INTMSAlign_HiSol for identifying aggregation hotspots in proteins only requiring secondary structure data was introduced. We explored the utility of this program further and applied it for engineering of the aldoxime dehydratase from Bacillus sp. OxB-1. Towards this end, the effect of inverting the hydropathy at selected positions of the amino acid sequence on the enzymatic activity was studied leading to 60% of our constructed variants, which showed improved activity. In part, this activity increase can be rationalised by an improved heme incorporation of the variants. For example, a single mutation gave a 1.8 fold increased enzymatic activity and 30% improved absolute heme incorporation.
format	article
author	Keiko Oike Jens Sproß Daisuke Matsui Yasuhisa Asano Harald Gröger
author_facet	Keiko Oike Jens Sproß Daisuke Matsui Yasuhisa Asano Harald Gröger
author_sort	Keiko Oike
title	Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach
title_short	Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach
title_full	Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach
title_fullStr	Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach
title_full_unstemmed	Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach
title_sort	protein engineering of the aldoxime dehydratase from bacillus sp. oxb-1 based on a rational sequence alignment approach
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/07ea2c0a72214d78b00d5898091ddd88
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Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach

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