Research output: Contribution to Journal/Magazine › Journal article › peer-review
<mark>Journal publication date</mark> | 06/1996 |
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<mark>Journal</mark> | The Biochemical journal |
Issue number | 2 |
Volume | 316 |
Number of pages | 5 |
Pages (from-to) | 389-393 |
Publication Status | Published |
<mark>Original language</mark> | English |
Transfer of the phosphate group of 2-carboxy-D-arabinitol 1-phosphate (CA1P) to 14C-labelled 2-carboxy-D-arabinitol (CA) was catalysed by extracts from leaves of Phaseolus vulgaris. This phosphotransferase activity co-purified with CA1P phosphatase, described previously. This activity was increased, up to 16-fold, by addition of bicarbonate ions at pH 9-10, suggesting rate enhancement by enzyme carbamylation. A Vmax of 1.5 μmol/min per mg of protein and a Km (for CA) of 1.8 mM were estimated for the exchange reaction, with the purified phosphatase. 2-Carboxy-D-arabinitol 1,5-bisphosphate and 2-carboxy-D-ribitol 1,5-bisphosphate, but not D-ribulose 1,5-bisphosphate, could replace CA1P as phosphate donor to [14C]CA.