PEP Carboxylases from Two C_4 Species of Panicum with Markedly Different Susceptibilities to Cold Inactivation

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概要

• 論文の詳細を見る

• Phosphoenolpyruvate carboxylase (PEPC) (EC 4.1.1.31) assayed in extracts of Panicum maximum Jacq. loses up to 50% of its activity after incubation for 60 minutes at 0℃ while the enzyme from P. miliaceum L. is completely stable under these conditions. Following dilution at room temperature the enzyme from P. maximum is labile, while that from P. miliaceum is stable. The P. maximum enzyme can be largely stabilized against dilution and against cold-inactivation by D_2O which stabilizes hydrophobic bonds and the compatible solutes proline, betaine and trimethylamine-N-oxide. Mineral ions, previously demonstrated to be protective against cold inactivation of pyruvate, P_i dikinase from maize, provide no protection of P. maximum PEPC against either cold or dilution. The chaotropic ion SCN^- causes partial inactivation of the enzyme from P. miliaceum in the cold. The possible interrelationship between inactivation by dilution and inactivation by cold is discussed. The enzyme from both species, when assayed without preincubation at low temperature, exhibits similar, slightly curvilinear Arrhenius plots; and no differences were found between the two species in the temperature dependence of photosynthesis.

• 日本植物生理学会の論文

著者

• Edwards Gerald

  Botany Department Washington State University

• Edwards Gerald

  Botany Department And Institute Of Biological Chemistry Washington State University

• Krall J

  Botany Department Washington State University:(present)botany Dept. University Of California

• KRALL John

  Botany Department, Washington State University

関連論文

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• Quantity and Kinetic Properties of Ribulose 1,5-Bisphosphate Carboxylase in C_3, C_4, and C_3-C_4 Intermediate Species of Flaveria (Asteraceae)
• PEP Carboxylases from Two C_4 Species of Panicum with Markedly Different Susceptibilities to Cold Inactivation

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