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Identification and characterization of a novel GNAT superfamily N(α)‐acetyltransferase from Salinicoccus halodurans H3B36
N(α)‐acetyl‐α‐lysine was found as a new type of compatible solutes that acted as an organic cytoprotectant in the strain of Salinicoccus halodurans H3B36. A novel lysine N(α)‐acetyltransferase gene (shkat), encoding an enzyme that catalysed the acetylation of lysine exclusively at α position, was id...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9049628/ https://www.ncbi.nlm.nih.gov/pubmed/34985185 http://dx.doi.org/10.1111/1751-7915.13998 |
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author | Ma, Xiaochen Jiang, Kai Zhou, Cheng Xue, Yanfen Ma, Yanhe |
author_facet | Ma, Xiaochen Jiang, Kai Zhou, Cheng Xue, Yanfen Ma, Yanhe |
author_sort | Ma, Xiaochen |
collection | PubMed |
description | N(α)‐acetyl‐α‐lysine was found as a new type of compatible solutes that acted as an organic cytoprotectant in the strain of Salinicoccus halodurans H3B36. A novel lysine N(α)‐acetyltransferase gene (shkat), encoding an enzyme that catalysed the acetylation of lysine exclusively at α position, was identified from this moderate halophilic strain and expressed in Escherichia coli. Sequence analysis indicated ShKAT contained a highly conserved pyrophosphate‐binding loop (Arg‐Gly‐Asn‐Gly‐Asn‐Gly), which was a signature of the GNAT superfamily. ShKAT exclusively recognized free amino acids as substrate, including lysine and other basic amino acids. The enzyme showed a wide range of optimal pH value and was tolerant to high‐alkali and high‐salinity conditions. As a new member of the GNAT superfamily, the ShKAT was the first enzyme recognized free lysine as substrate. We believe this work gives an expanded perspective of the GNAT superfamily, and reveals great potential of the shkat gene to be applied in genetic engineering for resisting extreme conditions. |
format | Online Article Text |
id | pubmed-9049628 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-90496282022-05-02 Identification and characterization of a novel GNAT superfamily N(α)‐acetyltransferase from Salinicoccus halodurans H3B36 Ma, Xiaochen Jiang, Kai Zhou, Cheng Xue, Yanfen Ma, Yanhe Microb Biotechnol Engineering Biology and Synthetic Biology N(α)‐acetyl‐α‐lysine was found as a new type of compatible solutes that acted as an organic cytoprotectant in the strain of Salinicoccus halodurans H3B36. A novel lysine N(α)‐acetyltransferase gene (shkat), encoding an enzyme that catalysed the acetylation of lysine exclusively at α position, was identified from this moderate halophilic strain and expressed in Escherichia coli. Sequence analysis indicated ShKAT contained a highly conserved pyrophosphate‐binding loop (Arg‐Gly‐Asn‐Gly‐Asn‐Gly), which was a signature of the GNAT superfamily. ShKAT exclusively recognized free amino acids as substrate, including lysine and other basic amino acids. The enzyme showed a wide range of optimal pH value and was tolerant to high‐alkali and high‐salinity conditions. As a new member of the GNAT superfamily, the ShKAT was the first enzyme recognized free lysine as substrate. We believe this work gives an expanded perspective of the GNAT superfamily, and reveals great potential of the shkat gene to be applied in genetic engineering for resisting extreme conditions. John Wiley and Sons Inc. 2022-01-05 /pmc/articles/PMC9049628/ /pubmed/34985185 http://dx.doi.org/10.1111/1751-7915.13998 Text en © 2022 The Authors. Microbial Biotechnology published by Society for Applied Microbiology and John Wiley & Sons Ltd. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Engineering Biology and Synthetic Biology Ma, Xiaochen Jiang, Kai Zhou, Cheng Xue, Yanfen Ma, Yanhe Identification and characterization of a novel GNAT superfamily N(α)‐acetyltransferase from Salinicoccus halodurans H3B36 |
title | Identification and characterization of a novel GNAT superfamily N(α)‐acetyltransferase from Salinicoccus halodurans H3B36 |
title_full | Identification and characterization of a novel GNAT superfamily N(α)‐acetyltransferase from Salinicoccus halodurans H3B36 |
title_fullStr | Identification and characterization of a novel GNAT superfamily N(α)‐acetyltransferase from Salinicoccus halodurans H3B36 |
title_full_unstemmed | Identification and characterization of a novel GNAT superfamily N(α)‐acetyltransferase from Salinicoccus halodurans H3B36 |
title_short | Identification and characterization of a novel GNAT superfamily N(α)‐acetyltransferase from Salinicoccus halodurans H3B36 |
title_sort | identification and characterization of a novel gnat superfamily n(α)‐acetyltransferase from salinicoccus halodurans h3b36 |
topic | Engineering Biology and Synthetic Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9049628/ https://www.ncbi.nlm.nih.gov/pubmed/34985185 http://dx.doi.org/10.1111/1751-7915.13998 |
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