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Purification and properties of a phosphatase in French bean (Phaseolus vulgaris L.) leaves that hydrolyses 2'-carboxy-D-arabinitol 1-phosphate

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Purification and properties of a phosphatase in French bean (Phaseolus vulgaris L.) leaves that hydrolyses 2'-carboxy-D-arabinitol 1-phosphate. / Kingston-Smith, A. H.; Major, I.; Parry, M. A J; Keys, A. J.

In: Biochemical Journal, Vol. 287, No. 3, 01.01.1992, p. 821-825.

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Kingston-Smith, A. H. ; Major, I. ; Parry, M. A J ; Keys, A. J. / Purification and properties of a phosphatase in French bean (Phaseolus vulgaris L.) leaves that hydrolyses 2'-carboxy-D-arabinitol 1-phosphate. In: Biochemical Journal. 1992 ; Vol. 287, No. 3. pp. 821-825.

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@article{5a9bc1f2c3e2435f94a1cf98c19f4d7c,
title = "Purification and properties of a phosphatase in French bean (Phaseolus vulgaris L.) leaves that hydrolyses 2'-carboxy-D-arabinitol 1-phosphate",
abstract = "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.",
author = "Kingston-Smith, {A. H.} and I. Major and Parry, {M. A J} and Keys, {A. J.}",
year = "1992",
month = jan,
day = "1",
doi = "10.1042/bj2870821",
language = "English",
volume = "287",
pages = "821--825",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "3",

}

RIS

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 -