Abstract
Phosphorolysis rather than phosphorylation of amylolysis products was found to be the major pathway of sugar phosphate formation from amylopectin by pea (Pisum sativum L.) chloroplast stromal proteins. The Km for inorganic phosphate incorporation was 2.5 mm, and ATP did not stimulate amylopectin-dependent phosphate incorporation. Arsenate (10 mm) inhibited phosphate incorporation into glucose monophosphates up to 46% and phosphoglucomutase activity 96%, resulting in glucose 1-phosphate accumulation as a product of amylopectin degradation. The intracellular distribution of enzymes of starch utilization was determined. Phosphorylase, phosphoglucomutase, and hexokinase were found in the chloroplast and cytoplasm, while β-amylase was restricted to the cytoplasm. Maltase was not detectable; maltose phosphorylase was active in the chloroplast.
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Selected References
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- AVRON M. Photophosphorylation by swiss-chard chloroplasts. Biochim Biophys Acta. 1960 May 20;40:257–272. doi: 10.1016/0006-3002(60)91350-0. [DOI] [PubMed] [Google Scholar]
- Burr B., Nelson O. E. Maize alpha-glucan phosphorylase. Eur J Biochem. 1975 Aug 15;56(2):539–546. doi: 10.1111/j.1432-1033.1975.tb02260.x. [DOI] [PubMed] [Google Scholar]
- Chapman G. W., Jr, Pallas J. E., Jr, Mendicino J. The hydrolysis of maltodextrins by a -amylase isolated from leaves of Vicia faba. Biochim Biophys Acta. 1972 Aug 28;276(2):491–507. doi: 10.1016/0005-2744(72)91010-8. [DOI] [PubMed] [Google Scholar]
- Gold A. M., Johnson R. M., Sánchez G. R. Kinetic mechanism of potato phosphorylase. J Biol Chem. 1971 Jun 10;246(11):3444–3450. [PubMed] [Google Scholar]
- Heldt H. W., Chon C. J., Maronde D. Role of orthophosphate and other factors in the regulation of starch formation in leaves and isolated chloroplasts. Plant Physiol. 1977 Jun;59(6):1146–1155. doi: 10.1104/pp.59.6.1146. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Levi C., Gibbs M. Starch degradation in isolated spinach chloroplasts. Plant Physiol. 1976 Jun;57(6):933–935. doi: 10.1104/pp.57.6.933. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Santarius K. A., Stocking C. R. Intracellular localization of enzymes in leaves and chloroplast membrane permeability to compounds involved in amino acid syntheses. Z Naturforsch B. 1969 Sep;24(9):1170–1179. doi: 10.1515/znb-1969-0915. [DOI] [PubMed] [Google Scholar]
- Steup M., Peavey D. G., Gibbs M. The regulation of starch metabolism by inorganic phosphate. Biochem Biophys Res Commun. 1976 Oct 18;72(4):1554–1561. doi: 10.1016/s0006-291x(76)80191-x. [DOI] [PubMed] [Google Scholar]
- Swain R. R., Dekker E. E. Seed germination studies. II. Pathways for starch degradation in germinating pea seedlings. Biochim Biophys Acta. 1966 Jul 6;122(1):87–100. doi: 10.1016/0926-6593(66)90093-2. [DOI] [PubMed] [Google Scholar]
