Autocitrullination and Changes in the Activity of Peptidylarginine Deiminase 3 Induced by High Ca²⁺ Concentrations.

ABSTRACT: Peptidylarginine deiminases (PADs) are enzymes that catalyze the Ca²⁺-dependent conversion of arginine residues into proteins to citrulline residues. Five PAD isozymes have been identified in mammals. Several studies have shown that the active-site pockets of these isozymes are formed when Ca²⁺ ions are properly bound. We previously characterized the structures of PAD3 in six states. Among these, we identified a "nonproductive" form of PAD3 in which the active site was disordered even though five Ca²⁺ ions were bound. This strange structure was probably obtained as a result of either high Ca²⁺ concentration (∼260 mM)-induced denaturation during the crystallization process or high Ca²⁺-concentration-induced autocitrullination. While aut

SUBMITTER: Sawata M 

PROVIDER: S-EPMC9386831 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature