<i>Aeromonas hydrophila</i> CobQ is a new type of NAD<sup>+</sup>- and Zn<sup>2+</sup>-independent protein lysine deacetylase.
Ontology highlight
ABSTRACT: Protein NƐ-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 Zn2+- or NAD+-dependent. In this study, we reported a protein, AhCobQ, in Aeromonas hydrophila ATCC 7966 that presents NAD+- and Zn2+-independent KDAC activity. Furthermore, its KDAC activity is located in an unidentified domain (from 195 to 245 aa). Interestingly, AhCobQ has no homology with current known KDACs, and no homologous protein was found in eukaryotic cells. A protein substrate analysis showed that AhCobQ has specific protein substrates in common with other known KDACs, indicating that these KDACs can dy
SUBMITTER: Wang Y
PROVIDER: S-EPMC11856932 | biostudies-literature | 2025 Feb
REPOSITORIES: biostudies-literature
ACCESS DATA