RT journal article
T1 Plant catalases as NO and H2S targets
A1 Palma, José M.
A1 Mateos Bernal, Rosa María
A1 López-Jaramillo, Javier
A1 Rodríguez-Ruiz, Marta
A1 González-Gordo, Salvador
A1 Lechuga Sancho, Alfonso María
A1 Corpas, Francisco J.
A2 BiomedicinaBiotecnología y Salud Pública
A2 Materno-Infantil y Radiología
K1 Docking
K1 Nitration
K1 S-nitrosation
K1 Persulfidation
K1 Post-translational modifications
K1 Signaling
AB 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.
PB ELSEVIER
SN 2213-2317
YR 2020
FD 2020-07
LK http://hdl.handle.net/10498/23402
UL http://hdl.handle.net/10498/23402
LA eng
DS Repositorio Institucional de la Universidad de Cádiz
RD 11-nov-2026