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Articles

Variations in Kinetic Properties of Ribulose-1,5-bisphosphate Carboxylases among Plants

Research School of Biological Sciences, The Australian National University, P.O. Box 475, Canberra City 2601 Australia

Studies of ribulose-1,5-bisphosphate (RuBP) carboxylase from taxonomically diverse plants show that the enzyme from C₃ and crassulacean acid metabolism pathway species exhibits lower K_m(CO₂) values (12-25 micromolar) than does that from C₄ species (28-34 micromolar). RuBP carboxylase from aquatic angiosperms, an aquatic bryophyte, fresh water and marine algae has yielded consistently high K_m(CO₂) values (30-70 micromolar), similar in range to that of the enzyme from C₄ terrestrial plants. This variation in K_m(CO₂) is discussed in relation to the correlation between the existence of CO₂-concentrating mechanisms for photosynthesis and the affinity of the enzyme for CO₂. The K_m(RuBP) of the enzyme from various sources ranges from 10 to 136 micromolar; mean ± SD = 36 ± 20 micromolar. This variation in K_m(RuBP) does not correlate with different photosynthetic pathways, but shows taxonomic patterns. Among the dicotyledons, the enzyme from crassinucellate species exhibits lower K_m(RuBP) (18 ± 4 micromolar) than does that from tenuinucellate species (25 ± 7 micromolar). Among the Poaceae, RuBP carboxylase from Triticeae, chloridoids, andropogonoids, Microlaena, and Tetrarrhena has yielded lower K_m(RuBP) values (29 ± 11 micromolar) than has that from other members of the grass family (46 ± 10 micromolar).

² Department of Environmental Biology.

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