Proteomics

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Aeromonas hydrophila CobQ is a new type of NAD+/Zn2+ independent protein lysine deacetylase in prokaryote


ABSTRACT: Protein NƐ-lysine acetylation (Kac) modification plays crucial roles on diverse physiological and pathological functions in cell.

ORGANISM(S): Aeromonas Hydrophila Subsp. Hydrophila Atcc 7966

SUBMITTER: Xiangmin Lin  

PROVIDER: PXD038735 | iProX | Fri Dec 09 00:00:00 GMT 2022

REPOSITORIES: iProX

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<i>Aeromonas hydrophila</i> CobQ is a new type of NAD<sup>+</sup>- and Zn<sup>2+</sup>-independent protein lysine deacetylase.

Wang Yuqian Y   Wang Guibin G   Zhang Lishan L   Cai Qilan Q   Lin Meizhen M   Huang Dongping D   Xie Yuyue Y   Lin Wenxiong W   Lin Xiangmin X  

eLife 20250225


Protein N<sup>Ɛ</sup>-lysine acetylation (Kac) modifications play crucial roles in diverse physiological and pathological functions in cells. In prokaryotic cells, there are only two types of lysine deacetylases (KDACs) that are Zn<sup>2+</sup>- or NAD<sup>+</sup>-dependent. In this study, we reported a protein, AhCobQ, in <i>Aeromonas hydrophila</i> ATCC 7966 that presents NAD<sup>+</sup>- and Zn<sup>2+</sup>-independent KDAC activity. Furthermore, its KDAC activity is located in an unidentifie  ...[more]

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