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Literature summary for 4.1.1.31 extracted from

  • Yuan, J.; Sayegh, J.; Mendez, J.; Sward, L.; Sanchez, N.; Sanchez, S.; Waldrop, G.; Grover, S.
    The regulatory role of residues 226-232 in phosphoenolpyruvate carboxylase from maize (2006), Photosynth. Res., 88, 73-81.
    View publication on PubMed
Search for more literature for 4.1.1.31

Activating Compound

Activating Compound Comment Organism Structure
glucose 6-phosphate
-
 Zea mays
glycine
-
 Zea mays

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3)pLysS Zea mays

Protein Variants

Protein Variants Comment Organism
D228N reduced apparent affinity for the activator glycine Zea mays
E229A maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is lower than wild-type value Zea mays
R226Q maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is significantly higher than that of wild-type enzyme Zea mays
R231A decreased apparent affinity for the activator glucose 6-phosphate Zea mays
R232Q decreased apparent affinity for the activator glucose 6-phosphate, reduced apparent affinity for the activator glycine Zea mays

Inhibitors

Inhibitors Comment Organism Structure
aspartate
-
 Zea mays
malate
-
 Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + HCO3-
-
 Zea mays phosphate + oxaloacetate
-
 ?