Enzymic Properties of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Purified from Rice Leaves.
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Journal: 2010/June - Plant Physiology
ISSN: 0032-0889
PUBMED: 16664401
Abstract:
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 CO(2) and Mg(2+) like other higher plant carboxylases, had an activation equilibrium constant (K(c)K(Mg)) of 1.90 x 10(5) to 2.41 x 10(5) micromolar(2) (pH 8.2 and 25 degrees C). Kinetic parameters of carboxylation and oxygenation catalyzed by the completely activated enzyme were examined at 25 degrees C and the respective optimal pHs. The K(m)(CO(2)), K(m)(RuBP), and V(max) values for carboxylation were 8 micromolar, 31 micromolar, and 1.79 units milligram(-1), respectively. The K(m)(O(2)), K(m)(RuBP), and V(max) values for oxygenation were 370 micromolar, 29 micromolar, and 0.60 units milligram(-1), respectively.Comparison of rice leaf RuBP carboxylase with other C(3) plant carboxylases showed that it had a relatively high affinity for CO(2) but the lowest catalytic turnover number (V(max)) among the species examined.
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Plant Physiol 79(1): 57-61
PMID: 16664401

Enzymic Properties of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Purified from Rice Leaves

Abstract

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 Mg like other higher plant carboxylases, had an activation equilibrium constant (KcKMg) of 1.90 × 10 to 2.41 × 10 micromolar (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, respectively. The Km(O2), Km(RuBP), and Vmax values for oxygenation were 370 micromolar, 29 micromolar, and 0.60 units milligram, 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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Selected References

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Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University, Amamiyamachi-Tsutsumidori, Sendai 980, Japan
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Abstract
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 Mg like other higher plant carboxylases, had an activation equilibrium constant (KcKMg) of 1.90 × 10 to 2.41 × 10 micromolar (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, respectively. The Km(O2), Km(RuBP), and Vmax values for oxygenation were 370 micromolar, 29 micromolar, and 0.60 units milligram, 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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