Effects of synthetic peptides on thylakoid phosphoprotein phosphatase reactions
| Autor: | Lüling Cheng, John F. Allen, Dalibor Stys |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
inorganic chemicals
chemistry.chemical_classification Physiology Phosphopeptide food and beverages Peptide macromolecular substances Cell Biology Plant Science General Medicine Biology environment and public health Dephosphorylation enzymes and coenzymes (carbohydrates) Biochemistry chemistry Thylakoid Phosphoprotein Genetics Phosphorylation Protein phosphorylation Protein kinase A |
| Zdroj: | Physiologia Plantarum. 93:173-178 |
| ISSN: | 0031-9317 |
| DOI: | 10.1034/j.1399-3054.1995.930124.x |
| Popis: | A synthetic peptide analogue of the phosphorylation site of LHC II, when phosphorylated by thylakoid membranes, served as a substrate for the thylakoid phosphoprotein phosphatase. The phosphopeptide became dephosphorylated at a low rate, comparable to that of the 9 kDa phosphoprotein. Phospho-LHC II itself became dephosphorylated much more rapidly, at a rate unaffected by endogenous phosphorylation of the peptide. Endogenous phosphorylation of the peptide was also without effect on other thylakoid protein phosphorylation and dephosphorylation reactions. In contrast, dephosphorylation of many thylakoid phosphoproteins was inhibited by addition of a pure, chemically-synthesised phosphopeptide analogue of phospho-LHC II |
| Databáze: | OpenAIRE |
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