Ontology highlight
ABSTRACT:
SUBMITTER: Tarrago L
PROVIDER: S-EPMC7402097 | biostudies-literature | 2020 Jul
REPOSITORIES: biostudies-literature
Tarrago Lionel L Grosse Sandrine S Lemaire David D Faure Laetitia L Tribout Mathilde M Siponen Marina I MI Kojadinovic-Sirinelli Mila M Pignol David D Arnoux Pascal P Sabaty Monique M
Antioxidants (Basel, Switzerland) 20200714 7
In proteins, methionine (Met) can be oxidized into Met sulfoxide (MetO). The ubiquitous methionine sulfoxide reductases (Msr) A and B are thiol-oxidoreductases reducing MetO. Reversible Met oxidation has a wide range of consequences, from protection against oxidative stress to fine-tuned regulation of protein functions. Bacteria distinguish themselves by the production of molybdenum-containing enzymes reducing MetO, such as the periplasmic MsrP which protects proteins during acute oxidative stre ...[more]