Journal Article

Carboxyarabinitol 1-Phosphate Phosphatase from Leaves of <i>Phaseolus vulgaris</i> and Other Species

Therese Charlet, Brandon d. Moore and Jeffrey R. Seemann

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 38, issue 5, pages 511-517
Published in print January 1997 | ISSN: 0032-0781
Published online January 1997 | e-ISSN: 1471-9053 | DOI:
Carboxyarabinitol 1-Phosphate Phosphatase from Leaves of Phaseolus vulgaris and Other Species

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  • Biochemistry
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Carboxyarabinitol 1-phosphate (CA1P) phosphatase activity occurred in leaves of 10 species examined, with the highest activity in leaves of Phaseolus vulgaris. Enzyme was purified from P. vulgaris 1,580-fold to a final specific activity of 6.1 μmol min−1 (mg protein)−1. Structural characteristics of positive effectors and substrate analogs for the CA1P phosphatase reaction were examined. Positive effectors were compounds that contained one phosphate group in close proximity to a second phosphate or a carboxyl group (e.g. 2-phosphoglycolate, pyrophosphate, 3-phosphoglycerate, and carboxyethylphosphonic acid). Many of the activators are structurally quite similar to CA1P, but were not used as substrates. In addition to the natural substrate CA1P, carboxypentitol and carboxyhexitol bisphosphates were shown to be good substrates (e.g. carboxyarabinitol bisphosphate and carboxymannitol bis-phosphate). A substrate arabinitol configuration (R) was preferred at C-2, and reactivity was lost when a hydroxymethyl group was substituted for the carboxyl group. Despite structural similarities to positive effectors, none of the tested reaction substrates could activate the enzyme.

Keywords: Branched-chain sugar phosphates; Carboxyarabinitol 1-phosphate phosphatase; Phaseolus vulgaris; Photosynthesis; Ribulose 1,5-bisphosphate carboxylase/oxygenase

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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