Ribulose-1,5-bisphosphate carboxylase from plants adapted to extreme environments

The K_m and V_max of ribulose-1,5-bisphosphate carboxylase (RuBPCase)in selenium absorbing plants (Astragalus flavus Barn., Astragalusrafaelensis Barn. and Stanleya pinnata Bril.) were similar toRuBPCase from tomato (Lycopersicon esculentum L. var. tropic).The pH optima for RuBPCase activity was 8.0 for L. esculentumand A. flavus and 7.0 for A. rafaelensis and S. pinnata. TheActivation Energy (E) values for the enzymes were as follows:A.flavus (21.37), S.pinnata (19.85), A. rafaelensis (19.12)and L. escudentum (18.58). The energy of activation was higherfor the desert plants as compared to the tomato. The Arrheniusplot curves were linear to 50?C far the desert plants as comparedto 45?C for tomato. Enzyme kinetics of RuBPCase from halophytic plants (Salicorniapacifica Stand., var. utahensis (Tidestrom) Munz. and Salicorniarubra Nels.) indicated the enzyme was at least as sensitiveto NaCl concentrations as the enzyme from tomato. (Received November 9, 1976; )