%0 Journal Article %A Palma, José M. %A Mateos, Rosa M. %A López-Jaramillo, Javier %A Rodríguez-Ruiz, Marta %A González-Gordo, Salvador %A Lechuga-Sancho, Alfonso M. %A Corpas, Francisco J. %T Plant catalases as NO and H2S targets %D 2020 %U http://hdl.handle.net/10668/3737 %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 %K Nitración %K Simulación del acoplamiento molecular %K Nitrosación %K Procesamiento proteico-postraduccional %K Sulfuro de hidrógeno %~