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

Research output: Contribution to journalJournal articlepeer-review

<mark>Journal publication date</mark>8/08/1983
<mark>Journal</mark>FEBS Letters
Issue number1-2
Number of pages5
Pages (from-to)107-111
Publication StatusPublished
<mark>Original language</mark>English


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+.