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Effect of calcium ions on pyruvate carboxylase from pigeon liver.

Authors :
Dugal BS
Göpel G
Source :
Biochimica et biophysica acta [Biochim Biophys Acta] 1975 Dec 18; Vol. 410 (2), pp. 407-13.
Publication Year :
1975

Abstract

Pigeon liver pyruvate carboxylase (pyruvate: CO2 ligase (ADP forming), EC 6.4.1.1) shows allosteric properties similar to those of chicken or rat liver enzyme. Kinetic methods have been used to determine the effect of Ca2+ on this enzyme. The Ca2+ activation effect is absolutely dependent on the Mg2+ concentration; in the absence of Mg2+, pyruvate carboxylase has no catalytic activity. Furthermore, Ca2+ cannot replace Mg2+ and also shows a paradoxical effect on the liver enzyme activity. It is an activator at low pyruvate or Mg2+ concentrations; at increased pyruvate concentrations, however, it becomes an inhibitor. At low levels of ATP a pronounced activation of pigeon liver pyruvate carboxylase by Ca2+ has been demonstrated. The results of this communication demonstrate pigeon liver pyruvate carboxylase to be different from pyruvate carboxylase from other sources.

Details

Language :
English
ISSN :
0006-3002
Volume :
410
Issue :
2
Database :
MEDLINE
Journal :
Biochimica et biophysica acta
Publication Type :
Academic Journal
Accession number :
1239301
Full Text :
https://doi.org/10.1016/0005-2744(75)90242-9