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Literature summary for 4.1.1.31 extracted from

  • Salahas, G.; Cormas, E.; Zervoudakis, G.
    Cold inactivation of phosphoenolpyruvate carboxylase and pyruvate orthophosphate dikinase from the C4 perennial plant Atriplex halimus (2002), Russ. J. Plant Physiol., 49, 211-215.
No PubMed abstract available

General Stability

General Stability Organism
10 mM Mg2+ stabilizes the enzyme against cold inactivation. At low Mg2+ concentrations, 4 mM, the enzyme is strongly protected by phosphoenolpyruvate, glucose-6-phosphate, and, partially, by L-malate Atriplex halimus

Organism

Organism UniProt Comment Textmining
Atriplex halimus
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + CO2
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Atriplex halimus phosphate + oxaloacetate
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?

Synonyms

Synonyms Comment Organism
PEPC
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Atriplex halimus
Phosphoenolpyruvate carboxylase
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Atriplex halimus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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10 mM Mg2+ stabilizes the enzyme against cold inactivation. At low Mg2+ concentrations, 4 mM, the enzyme is strongly protected by phosphoenolpyruvate, glucose-6-phosphate, and, partially, by L-malate Atriplex halimus
-
-
45 min, 70% loss of activity without addition of stabilizing agent, 14% loss of activity in presence of 10 mM MgCl2, 8% loss of activity in presence of 4 mM phosphoenolpyruvate, 73% loss of activity in presence of 5 mM pyruvate, 41% loss of activity in presence of 6 mM L-malate, 5% loss of activity in presence of 10 mM glucose-6-phosphate Atriplex halimus
24
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45 min, 12% loss of activity without addition of stabilizing agent, 1% loss of activity in presence of 10 mM MgCl2, no loss of activity in presence of 4 mM phosphoenolpyruvate, 17% loss of activity in presence of 5 mM pyruvate, no loss of activity in presence of 6 mM L-malate, no loss of activity in presence of 10 mM glucose-6-phosphate Atriplex halimus