An enzyme that releases P(i) from 2-carboxy-D-arabinitol 1-phosphate, a naturally occurring tightly binding inhibitor of ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 126.96.36.199), was purified from leaves of French bean seedlings. It was a monomeric protein of M(r) about 56,000. Catalytic activity was stimulated by increased concentrations of inorganic salts to a maximum at an ionic strength above 0.2. NADPH and D-fructose 1,6-bisphosphate increased the activity of the enzyme in both the presence and absence of 0.2 M-KCl. The pure enzyme did not require dithiothreitol for activity. The pH optimum was 7, the Km for 2-carboxy-D-arabinitol 1-phosphate was 0.43 mM and the specific activity 6.8 mumol/min per mg of protein. The enzyme had little or no activity against phosphate ester intermediates of photosynthetic metabolism and glycolysis but hydrolysed the 1,5-bisphosphates of 2′-carboxy-D-ribitol and 2′-carboxy-D-arabinitol more rapidly than 2′-carboxy-D-arabinitol 1-phosphate.
Purification and properties of a phosphatase in French bean (Phaseolus vulgaris L.) leaves that hydrolyses 2′-carboxy-d-arabinitol 1-phosphate
- Views Icon Views
- Share Icon Share
A H Kingston-Smith, I Major, M A J Parry, A J Keys; Purification and properties of a phosphatase in French bean (Phaseolus vulgaris L.) leaves that hydrolyses 2′-carboxy-d-arabinitol 1-phosphate. Biochem J 1 November 1992; 287 (3): 821–825. doi: https://doi.org/10.1042/bj2870821
Download citation file: