6533b838fe1ef96bd12a5033

RESEARCH PRODUCT

Increased susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolytic degradation caused by oxidative treatments

Joaquín MorenoLola Peñarrubia

subject

OxygenaseTime FactorsRibulose-Bisphosphate CarboxylaseProteolysisBiophysicsBiochemistryDithiothreitolchemistry.chemical_compoundEnzyme StabilitymedicineCysteineMolecular Biologychemistry.chemical_classificationChymotrypsinRibulose 15-bisphosphatebiologymedicine.diagnostic_testHydrolysisPlantsTrypsinPyruvate carboxylaseEnzymechemistryBiochemistrybiology.proteinOxidation-ReductionPeptide Hydrolasesmedicine.drug

description

The susceptibility of the chloroplastic enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolysis by trypsin, chymotrypsin, proteinase K, and papain is enhanced by oxidative treatments including spontaneous oxidation of cysteines. Proteinases exhibit a high specificity for the oxidized inactive form of the carboxylase, cleaving its large subunit. Treatment of the inactive enzyme with dithiothreitol results in partial recovery of both carboxylase activity and resistance to proteolysis. This behavior may explain the specific degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase that occurs in vivo during leaf senescence.

yearjournalcountryeditionlanguage
1990-09-01Archives of Biochemistry and Biophysics
https://doi.org/10.1016/0003-9861(90)90450-d