PMID:8633035

Citation	Cabiscol, E and Levine, RL (1996) The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation. Proc. Natl. Acad. Sci. U.S.A. 93:4170-4
Abstract	Carbonic anhydrase isozyme III (CAIII) is unique among the carbonic anhydrases because it demonstrates phosphatase activity. CAIII forms a disulfide link between glutathione and two of its five cysteine residues, a process termed S-glutathiolation. Glutathiolation of CAIII occurs in vivo and is increased during aging and under acute oxidative stress. We show that glutathiolation serves to reversibly regulate the phosphatase activity of CAIII. Glutathiolation of Cys-186 is required for phosphatase activity, while glutathiolation of Cys-181 blocks activity. Phosphotyrosine is the preferred substrate, although phosphoserine and phosphothreonine can also be cleaved. Thus, glutathiolation is a reversible covalent modification that can regulate CAIII, a phosphatase that may function in the cellular response to oxidative stress.
Links	PubMed PMC39506
Keywords	Amino Acid Sequence; Animals; Carbonic Anhydrases/isolation & purification; Carbonic Anhydrases/metabolism; Cysteine; Fluoresceins; Fluorescent Dyes; Glutathione/metabolism; Humans; Isoenzymes/isolation & purification; Isoenzymes/metabolism; Kinetics; Male; Molecular Sequence Data; Phosphopeptides/chemistry; Protein Tyrosine Phosphatases/metabolism; Protein-Tyrosine Kinases/metabolism; Rats; Rats, Inbred F344; Recombinant Proteins/metabolism; Substrate Specificity
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
RAT:CAH3		GO:0016791: phosphatase activity	ECO:0000314:		F		Figure 3	complete CACAO 5520
RAT:CAH3	enables	GO:0016791: phosphatase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete

References

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