Ontology highlight
ABSTRACT:
ORGANISM(S): Aeromonas Hydrophila Subsp. Hydrophila Atcc 7966
SUBMITTER:
Xiangmin Lin
PROVIDER: PXD038735 | iProX | Fri Dec 09 00:00:00 GMT 2022
REPOSITORIES: iProX

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]