Increased susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolytic degradation caused by oxidative treatments.
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.
Department de Bioquímica i Biologia Molecular, Fac. Ciencias, Universitat de Valencia, Spain.
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Peñarrubia
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Moreno
D003545:Cysteine / Q000032:analysis; D004795:Enzyme Stability; D006868:Hydrolysis; D010084:Oxidation-Reduction; D010447:Peptide Hydrolases / Q000378:metabolism*; D010944:Plants / Q000201:enzymology; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D013997:Time Factors
D010447:Peptide Hydrolases; D012273:Ribulose-Bisphosphate Carboxylase; D003545:Cysteine