The localisation of 2-carboxy-D-arabinitol 1-phosphate and inhibition of Rubisco in leaves of Phaseolus vulgaris L
| Autor: | Alfred J. Keys, Helen M Lowe, Martin A. J. Parry, P. J. Andralojc |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
inorganic chemicals
Chlorophyll Biochemistry & Molecular Biology Inhibitor Chloroplasts Time Factors Light Photoperiod Ribulose-Bisphosphate Carboxylase Biophysics 2-carboxy-D-arabinitol 1-phosphate 2-Carboxy-d-arabinitol-1-phosphate Photosynthesis Biochemistry Phaseolus vulgaris chemistry.chemical_compound Structural Biology In vivo Genetics Binding site Enzyme Inhibitors Molecular Biology Pentosephosphates Binding Sites Plants Medicinal biology Sulfates RuBisCO fungi food and beverages Fabaceae Cell Biology biology.organism_classification Ribulose 1 5-bisphosphate carboxylase/oxygenase Chloroplast Dark-adapted leaves Plant Leaves Freeze Drying chemistry biology.protein Phaseolus |
| Zdroj: | FEBS letters. 444(1) |
| ISSN: | 0014-5793 |
| Popis: | A recent controversial report suggests that the nocturnal inhibitor of Rubisco, 2-carboxy-D-arabinitol 1-phosphate (CA1P), does not bind to Rubisco in vivo and therefore that CA1P has no physiological relevance to photosynthetic regulation. It is now proved that a direct rapid assay can be used to distinguish between Rubisco-bound and free CA1P, as postulated in the controversial report. Application of this direct assay demonstrates that CA1P is bound to Rubisco in vivo in dark-adapted leaves. Furthermore, CA1P is shown to be in the chloroplasts of mesophyll cells, Thus, CA1P does play a physiological role in the regulation of Rubisco, (C) 1999 Federation of European Biochemical Societies. |
| Databáze: | OpenAIRE |
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