%0 Journal Article 
%A Palma, José M.
%A Mateos Bernal, Rosa María
%A López-Jaramillo, Javier
%A Rodríguez-Ruiz, Marta
%A González-Gordo, Salvador
%A Lechuga Sancho, Alfonso María
%A Corpas, Francisco J.
%T Plant catalases as NO and H2S targets
%D 2020
%@ 2213-2317
%U http://hdl.handle.net/10498/23402
%X Catalase is a powerful antioxidant metalloenzyme located in peroxisomes which also plays a central role in signaling processes under physiological and adverse situations. Whereas animals contain a single catalase gene, in plants this enzyme is encoded by a multigene family providing multiple isoenzymes whose number varies depending on the species, and their expression is regulated according to their tissue/organ distribution and the environmental conditions. This enzyme can be modulated by reactive oxygen and nitrogen species (ROS/RNS) as well as by hydrogen sulfide (H2S). Catalase is the major protein undergoing Tyr-nitration [post-translational modification (PTM) promoted by RNS] during fruit ripening, but the enzyme from diverse sources is also susceptible to undergo other activity-modifying PTMs. Data on S-nitrosation and persulfidation of catalase from different plant origins are given and compared here with results from obese children where S-nitrosation of catalase occurs. The cysteine residues prone to be S-nitrosated in catalase from plants and from bovine liver have been identified. These evidences assign to peroxisomes a crucial statement in the signaling crossroads among relevant molecules (NO and H2S), since catalase is allocated in these organelles. This review depicts a scenario where the regulation of catalase through PTMs, especially S-nitrosation and persulfidation, is highlighted.
%K Docking
%K Nitration
%K S-nitrosation
%K Persulfidation
%K Post-translational modifications
%K Signaling
%~ Universidad de Cádiz