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PMID:20600561

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Citation

Cerný, M, Doubnerová, V, Müller, K and Ryšlavá, H (2010) Characterization of phosphoenolpyruvate carboxylase from mature maize seeds: properties of phosphorylated and dephosphorylated forms. Biochimie 92:1362-70

Abstract

Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) from mature maize seeds (Zea mays L.) was purified to homogeneity and a final specific activity of 13.3 μmol min⁻¹ mg⁻¹. Purified PEPC was treated with phosphatase from bovine intestinal mucosa or protein kinase A to study its apparent phosphorylation level. Kinetic parameters of the enzyme reaction catalyzed by phosphorylated and dephosphorylated forms under different conditions were compared, as well as an effect of modulators. The enzyme dephosphorylation resulted in the change of hyperbolic kinetics to the sigmoidal one (with respect to PEP), following with the decrease of maximal reaction rate and the increase of sensitivity to L-malate inhibition. The hyperbolic kinetics of native PEPC present in dry maize seeds was not changed after the protein kinase A treatment, while it was converted to the sigmoidal one after dephosphorylation. Level of PEPC phosphorylation was not affected during seed imbibition.

Links

PubMed Online version:10.1016/j.biochi.2010.06.019

Keywords

Animals; Cattle; Cyclic AMP-Dependent Protein Kinases/pharmacology; Kinetics; Malates/pharmacology; Phosphoenolpyruvate Carboxylase/antagonists & inhibitors; Phosphoenolpyruvate Carboxylase/isolation & purification; Phosphoenolpyruvate Carboxylase/metabolism; Phosphorylation; Seeds/enzymology; Zea mays/enzymology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

MAIZE:CAPP1

GO:0008964: phosphoenolpyruvate carboxylase activity

ECO:0000314:

F

Figure 3 shows the effects of alkaline phosphatase and PK A treatment on PEPC activity

complete
CACAO 5604

MAIZE:CAPP1

enables

GO:0008964: phosphoenolpyruvate carboxylase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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