Research output: Contribution to Journal/Magazine › Journal article › peer-review
<mark>Journal publication date</mark> | 8/08/1983 |
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<mark>Journal</mark> | FEBS Letters |
Issue number | 1-2 |
Volume | 159 |
Number of pages | 5 |
Pages (from-to) | 107-111 |
Publication Status | Published |
<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+.