Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Purification and properties of a phosphatase in French bean (Phaseolus vulgaris L.) leaves that hydrolyses 2'-carboxy-D-arabinitol 1-phosphate
AU - Kingston-Smith, A. H.
AU - Major, I.
AU - Parry, M. A J
AU - Keys, A. J.
PY - 1992/1/1
Y1 - 1992/1/1
N2 - An enzyme that releases P. from 2-carboxy-D-arabinitol l-phosphate, a naturally occurring tightly binding inhibitor of ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4. 1.1. 39), was purified from leaves of French bean seedlings. It was a monomeric protein of M(r) about 56000. 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 K(m) for 2-carboxy-D-arabinitol l-phosphate was 0.43 mM and the specific activity 6.8 μmol/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.
AB - An enzyme that releases P. from 2-carboxy-D-arabinitol l-phosphate, a naturally occurring tightly binding inhibitor of ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4. 1.1. 39), was purified from leaves of French bean seedlings. It was a monomeric protein of M(r) about 56000. 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 K(m) for 2-carboxy-D-arabinitol l-phosphate was 0.43 mM and the specific activity 6.8 μmol/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.
UR - http://www.scopus.com/inward/record.url?scp=0026440717&partnerID=8YFLogxK
U2 - 10.1042/bj2870821
DO - 10.1042/bj2870821
M3 - Journal article
C2 - 1332682
AN - SCOPUS:0026440717
VL - 287
SP - 821
EP - 825
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 3
ER -