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Hysteretic nature of phosphoenolpyruvate carboxylase isolated from maize

Archives of Biochemistry and Biophysics, 1990
The hysteretic nature of phosphoenolpyruvate carboxylase from maize was investigated at pH 7 by (a) transient kinetic studies, (b) kinetics of inhibition by 2-PG, a structural analog of PEP, and (c) effect of 2-PG on equilibrium binding of Mg2+. The lag time as a function of substrate concentration was nonlinear with an oblique asymptote. During steady
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[46] Phosphoenolpyruvate carboxylase from Pseudomonas AM1

1969
Publisher Summary The chapter describes the purification procedure and properties of phosphoenolpyruvate carboxylase from Pseudomonas AM1. This enzyme was first discovered in spinach and has since been found in several species of bacteria. The enzyme is assayed by two methods: measurement of the amount of isotope fixed in nonvolatile products from ...
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The regulation of phosphoenolpyruvate carboxylase in CAM plants

Trends in Plant Science, 2000
Phosphoenolpyruvate carboxylase catalyses the primary assimilation of CO(2) in Crassulacean acid metabolism plants. It is activated by phosphorylation, and this plays a major role in setting the day-night pattern of metabolism in these plants. The key factor that controls the phosphorylation state of phosphoenolpyruvate carboxylase is the activity of ...
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Phosphoenolpyruvate Carboxylase of Escherichia coli

The Journal of Biochemistry, 1978
Isamu KAMESHITA   +2 more
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Phosphoenolpyruvate Carboxylase of Escherichia coli

The Journal of Biochemistry, 1979
Aiko NAIDE   +3 more
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Lipogenesis inhibitors: therapeutic opportunities and challenges

Nature Reviews Drug Discovery, 2022
Gregory R Steinberg
exaly  

Phosphoenolpyruvate carboxylase

1990
Dietmar Schomburg, Margit Salzmann
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Corn leaf phosphoenolpyruvate carboxylases

Archives of Biochemistry and Biophysics, 1977
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