Plant Physiology 79:57-61 (1985)
© 1985 American Society of Plant Biologists
Articles
Enzymic Properties of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Purified from Rice Leaves
Amane Makino,
Tadahiko Mae and
Koji Ohira
Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Amamiyamachi-Tsutsumidori, Sendai 980, Japan
The enzymic properties of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase purified from rice (Oryza sativa L.) leaves were studied. Rice RuBPcarboxylase, activated by preincubation with CO2 and Mg2+ like other higher plant carboxylases, had an activation equilibrium constant (KcKMg) of 1.90 x 105 to 2.41 x 105 micromolar2 (pH 8.2 and 25°C). Kinetic parameters of carboxylation and oxygenation catalyzed by the completely activated enzyme were examined at 25°C and the respective optimal pHs. The Km(CO2), Km(RuBP), and Vmax values for carboxylation were 8 micromolar, 31 micromolar, and 1.79 units milligram–1, respectively. The Km(O2), Km(RuBP), and Vmax values for oxygenation were 370 micromolar, 29 micromolar, and 0.60 units milligram–1, respectively.
Comparison of rice leaf RuBP carboxylase with other C3 plant carboxylases showed that it had a relatively high affinity for CO2 but the lowest catalytic turnover number (Vmax) among the species examined.
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