Activation of ribulose 1,5-bisphosphate carboxylase by Ca2+

Parry, Martin A J and Schmidt, C. N Godfrey and Keys, Alfred J. and Gutteridge, Steven (1983) Activation of ribulose 1,5-bisphosphate carboxylase by Ca2+. FEBS Letters, 159 (1-2). pp. 107-111. ISSN 0014-5793

Full text not available from this repository.


Purified RuBP carboxylase requires activation by reaction with CO2 and a divalent metal ion. Mg2+ is the most effective metal ion, and is probably involved in activation in vivo. Ca2+ is reported not to be an activator. Several oxyanions, including phosphate esters, are effectors of activation of RuBP carboxylase by Co2 and Mg2+. It is now shown that Ca2+ is an effective activator of RuBP carboxylase and that PO4 3-, FBP, NADPH and 6-phosphogluconate are effectors of this activation. The ratio of oxygenase to carboxylase activity of enzyme activated with Ca2+ is similar to that for the enzyme activated with Mg2+.

Item Type:
Journal Article
Journal or Publication Title:
FEBS Letters
Uncontrolled Keywords:
?? 6-phosphogluconateactivation by caoxyanion effectorrubp carboxylasebiochemistrybiophysicsmolecular biologystructural biologycell biologygenetics ??
ID Code:
Deposited By:
Deposited On:
21 Oct 2015 05:04
Last Modified:
15 Jul 2024 15:31