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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...

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Autores principales: Ma, Xiaochen, Jiang, Kai, Zhou, Cheng, Xue, Yanfen, Ma, Yanhe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
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.
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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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