Skip to main content

myo-Inositol Polyphosphates and Their Role in Cellular Metabolism

A Proposed Cycle Involving Glucose-6-Phosphate and myo-Inositol Phosphates

  • Chapter
Subcellular Biochemistry

Abstract

Life is characterized by complex organization, precise regulation, and colorful diversity. It is a biochemical system that is always far from thermodynamic equilibrium. The maintenance of such a state demands a constant expenditure of energy to maintain a unidirectional flow of metabolites. A network of anabolic and catabolic pathways operates in every living cell. It is well known that phosphate esters in living organisms are essential intermediates in metabolic transformations and these phosphorylated compounds are invariably associated with energy balance, which is fundamental to life processes. The sources of energy for living organisms are extremely diverse, but it is not clear why phosphate esters rather than the esters of other inorganic acids predominate in biological systems. It is probably significant that phosphate anhydrides combine high activation energies of nonenzymatic hydrolysis with large negative free energies of hydrolysis. This permits controlled enzymatic cleavage of the anhydride, rather than spontaneous hydrolysis. Lipmann (1951) has pointed out that acetic anhydride is hydrolyzed rapidly in neutral conditions, acetylphosphate is more stable, and pyrophosphate is resistant to hydrolysis at neutral pH. Phosphates are probably protected from hydroxyl attack by their negative charge. The discussion in this chapter is centered around a biologically important phosphocompound that was discovered as early as 1872 by Pfeffer (1872). This was subsequently identified as a salt of phytic acid (or more correctly myo-inositol hexakisphosphate), which is the major phosphorus constituent of cereal grain (Williams, 1970).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Agranoff, B. W., Bradley, R. M., and Brady, R. O., 1958, The enzymatic synethesis of inositol phosphatide, J. Biol. Chem 233: 1077–1083.

    PubMed  CAS  Google Scholar 

  • Agranoff, B. W., Benjamin, J. A., and Haira, A. K., 1969, Biosynthesis of phosphatidylinositol, Ann. N. Y. Acad. Sci 165: 755–760.

    PubMed  CAS  Google Scholar 

  • Albaum, H. G., and Umbreit, W. W., 1943, Phosphorus transformation during the development of the oat embryo, Am. J. Bot 30: 553–558.

    CAS  Google Scholar 

  • Anderson, R. J., 1914, Concerning the organic phosphoric acid of cotton meal II J. Biol. Chem 17: 141–150.

    CAS  Google Scholar 

  • Asada, K., Tanaka, K., and Kasai, Z., 1969, Phytate synthesis in cereal grains, Ann. N.Y. Acad. Sci 165: 801–814.

    PubMed  CAS  Google Scholar 

  • Atherton, R. S., and Hawthorne, J. N., 1968, The phosphoinositide inositol phospholydrolase of guinea pig intestinal mucosa, Eur. J. Biochem 4: 68–75.

    PubMed  CAS  Google Scholar 

  • Atkinson, D. E., 1968, The energy charge of the adenylate pool as a regulatory parameter: Interaction with feedback modifiers, Biochemistry 7: 4030–4040.

    PubMed  CAS  Google Scholar 

  • Atkinson, M. R., and Morton, R.K., 1960, Free Energy and the biosynthesis of phosphates, in: Comparative Biochemistry, Vol. 2 ( M. Florkin and H. S. Mason, eds.), pp. 1–95, Academic Press, New York.

    Google Scholar 

  • Barnett, J. E. G., Rasheed, A., and Corina, D. L., 1973, Partial reactions of D-glucose 6-phosphate-1 and L-myo-inositol 1-phosphate cyclase, Biochem. J 131: 21–30.

    PubMed  CAS  Google Scholar 

  • Bianchetti, R., and Sartirana, M. L., 1967, The mechanism of the repression by inorganic phosphate of phytase Synthesis in the germinating wheat embryo, Biochem. Biophys. Acta 145: 485–490.

    PubMed  CAS  Google Scholar 

  • Biswas, B. B., Biswas, S., Chakrabarti, S., and De, B. P., 1978, A novel metabolic cycle involving myo-inositol phosphate during formation and germination of seeds, in: Cyclitols and Phosphoinositides( W. W. Wells and F. Eisenberg, Jr., eds.), pp. 57–68, Academic Press, New York.

    Google Scholar 

  • Biswas, S., and Biswas, B. B., 1965, Enzymic synthesis of guanosine triphosphate from phytin and guanosine diphosphate, Biochim. Biophys. Acta 108: 710–713.

    PubMed  CAS  Google Scholar 

  • Biswas, S., Barman, S., and Biswas, B. B., 1975, Inositol hexaphosphate guanosine diphosphate phosphotransferase from Phaseolus aureus, Phytochemistry 14: 373–375.

    CAS  Google Scholar 

  • Biswas, S., Maiti, I. B., Chakrabarti, S., and Biswas, B. B., 1978, Purification and characterization of myo-inositol hexaphosphate-adenosine diphosphate phosphotransferase from Phaseolus aureus, Arch. Biochem. Biophys 185: 557–566.

    PubMed  CAS  Google Scholar 

  • Blank, G. E., Pletcher, J., and Sax, M., 1971, The structure of myoinositol hexaphosphate dodecasodium salt octatriacontahydrate: A single crystal X-ray analysis. Biochem. Biophys. Res. Commun 44: 319–325.

    PubMed  CAS  Google Scholar 

  • Brockerhoff, H., and Ballou, C. E., 1961, The structure of phosphoinositide-complex of beef brain, J. Biol. Chem 236: 1907–1911.

    CAS  Google Scholar 

  • Brockerhoff, H. and Ballou, C. E., 1962, On the metabolism of the brain phosphoinositide complex, J. Biol. Chem 237:1764–1766.

    PubMed  CAS  Google Scholar 

  • Brown, E. G., 1965, Changes in the free nucleotide and nucleoside pattern of pea seeds in relation to germination, Biochem. J 95: 509–514.

    PubMed  CAS  Google Scholar 

  • Brunner, A., Pina, M. Z., Chagoya de Sanchez, V., and Pina, E., 1972, Effect of (NH4)2SO4 and glycerol on the preservation of the NAD+independent activity of D-glucose-6-phosphate, L-myo-inositol-1-phosphate cycloaldolase from Neurospora crassa, Arch. Biochem. Biophys 150: 32–37.

    PubMed  CAS  Google Scholar 

  • Burton, L. E., and Wells, W. W., 1977, Studies on the effect of 5-thio-D-glucose and 2-deoxy-D-glucose on myo-inositol metabolism, Arch. Biochem. Biophys 181: 384–392.

    PubMed  CAS  Google Scholar 

  • Byun, S. M., and Jeanness, R., 1981, Stereospecitivity of L-myo-inositol 1-phosphate synthase for nicotinamide adenine dinucleotide, Biochemistry 20: 5174–5177.

    PubMed  CAS  Google Scholar 

  • Chakrabarti, S., and Biswas, B. B., 1981a, Two forms of phosphoinositol kinase from germinating mung bean seeds, Phytochemistry 20:1815–1817.

    CAS  Google Scholar 

  • Chakrabarti, S., and Biswas, B. B., 1981b, Evidence for the existence of a phosphoinositol kinase in chicken erythrocytes, Indian J. Biochem. Biophys 18: 398–401.

    CAS  Google Scholar 

  • Charalampous, F. C., 1960, Biochemical studies on inositol. VI. Mechanism of cleavage of inositol to D-glucuronic acid, J. Biol. Chem 235: 1286–1291.

    PubMed  CAS  Google Scholar 

  • Chen, C. H. Y., and Eisenberg, F., Jr., 1975, Myoinosose-2 1-phosphate: An intermediate in the myoinositol 1-phosphate synthase reaction, J. Biol. Chem 250: 2963–2967.

    PubMed  CAS  Google Scholar 

  • Chen, I. W., and Charalampous, F. C., 1965, Inositol- 1 -phosphate as intermediate in the conversion of glucose-6-phosphate to inositol, Biochem. Biophys. Res. Commun 19: 144–149.

    CAS  Google Scholar 

  • Colodzin, M., and Kennedy, E. P., 1965, Biosynthesis of diphosphoinositide in brain, J. Biol. Chem 240: 3771–3780.

    PubMed  CAS  Google Scholar 

  • Cosgrove, D. J., 1966, The chemistry and biochemistry of inositol phosphates, Rev. Pure Appl. Chem 16: 209–224.

    CAS  Google Scholar 

  • Cosgrove, D. J., 1980, Studies in Organic Chemistry 4: Inositol Phosphates—Their Chemistry, Biochemistry and Physiology, Elsevier, Amsterdam.

    Google Scholar 

  • Cosgrove D. J., Irving, G. C. J., and Bromfield, S. M., 1970, Inositol phosphate phosphatases of microbiological origin: The isolation of soil bacteria having inositolphosphate phosphatase activity, Aust. J. Biol. Sci 23: 339–343.

    CAS  Google Scholar 

  • Courtois, J. E., 1951a, Les esters phosphoniques de l’inositol, Bull. Soc. Chim. Biol 33: 1075–1085.

    CAS  Google Scholar 

  • Crick, F. H. C., and Orgel, L. E., 1964, The theory of interallelic complementation, J. Mol. Biol 8: 161–165.

    PubMed  CAS  Google Scholar 

  • Culbertson, M. R., and Henry, S. A., 1975, Inositol requiring mutants of Saccharomyces cerevisiae, Genetics 80: 23–40.

    CAS  Google Scholar 

  • Culbertson, M. R., Donahue, T. F., and Henry, S. A., 1976, Control of inositol biosynthesis in Saccharomyces cerevisiae: Properties of a repressible enzyme system in extracts of wild type (Ino+) Cells, J. Bacteriol 126: 232–242.

    PubMed  CAS  Google Scholar 

  • Darbre, A., and Norris, F. W., 1957, Determination of free and combined inositol in the ungerminated bean seed and the young plant, Biochem. J 66: 404–407.

    PubMed  CAS  Google Scholar 

  • Dawson, R. M. C., and Thompson, W., 1964, The triphosphoinositide phosphomonoesterase of brain tissue, Biochem. J 91: 244–250.

    PubMed  CAS  Google Scholar 

  • De, B. P., and Biswas, B. B., 1979, Evidence for the existence of a novel enzyme system: myo-inositol-1-phosphate dehydrogenase in Phaseolus aureus, J. Biol. Chem 254: 8717–8719.

    PubMed  CAS  Google Scholar 

  • Diemair, W., and Beoker, H., 1955, The physiology and chemistry of phytin, Dtsch. Lebensm. Rundsch 51: 18–96.

    CAS  Google Scholar 

  • Dietz, M., and Albersheim, P., 1965, The enzymatic phosphorylation of myo-inositol, Biochem. Biophys. Res. Commun 19: 598–603.

    PubMed  CAS  Google Scholar 

  • Donahue, T. F., and Henry, S. A., 1981a, myo-Inositol-1-phosphate synthase: Characteristics of the enzyme and identification of its structural gene in yeast, J. Biol. Chem 256:7077–7085.

    CAS  Google Scholar 

  • Donahue, T. F., and Henry, S. A., 1981b, Inositol mutants of yeast: Mapping of the ino-1locus and characteristics of the alleles of loci ino-1, ino-2and ino-4, Genetics 98: 491–503.

    CAS  Google Scholar 

  • Donahue, T. F., Atkinson, K., Kolat, A., and Henry, S. A., 1978, Inositol-1-phosphate synthase mutants of the yeast, Saccharomyces cerevisiae, in: Cyclitols and phosphoinositides( W. W. Wells and F. Eisenberg, Jr., eds.), pp. 311–316, Academic Press, New York.

    Google Scholar 

  • Dure, L. S., 1960, Site of origin and extent of activity of amylases in maize germination, Plant Physiol 35: 925–934.

    PubMed  CAS  Google Scholar 

  • Eastwood, D., Tavener, R. J. A., and Laidman, D. L., 1969, Induction of lipase and phytase activities in the aleurone tissue of germinating wheat grains, Biochem. J 113:32P–33P.

    PubMed  CAS  Google Scholar 

  • Eisenberg, F., Jr., 1967, D-myo-Inositol-1-P as product of cylization of glucose-6-P and substrate for a specific phosphatase in rat tissue, J. Biol. Chem 242: 1375–1382.

    PubMed  CAS  Google Scholar 

  • Eisenberg, F., Jr., 1969, Cyclitols and phosphoinositides: Chemistry, metabolism, and function, Ann. N. Y. Acad. Sci 165: 509–819.

    Google Scholar 

  • English, P. D., Dietz, M., and Albersheim, P., 1966, myo-Inositol kinase: Partial purification and identification of product, Science 151:198–199.

    PubMed  CAS  Google Scholar 

  • Ergle, D. R., and Guinn, G., 1959, Phosphorus compounds of cotton embryos and their changes during germination, Plant Physiol 34: 476–481.

    PubMed  CAS  Google Scholar 

  • Esko, J. D., and Raetz, C. R. H., 1978, Replica plating and in situenzymatic assay of animal cell colonies established on filter paper, Proc. Natl. Acad. Sci. U.S.A 75: 1190–1193.

    PubMed  CAS  Google Scholar 

  • Folch, J., 1949, Brain diphosphoinositide, a new phosphatide having inositol meta-diphosphate as a constituent, J. Biol. Chem 177: 505–519.

    PubMed  CAS  Google Scholar 

  • Ghosh, R., Abrol, P. and Sinha, S. K., 1974, Amylase heterosis and complementation in sorghum, Plant Sci. Lett 2: 173–176.

    Google Scholar 

  • Gibbins, L. N., and Norris, F. W., 1963, Phytase and acid phosphatase in the dwarf bean. Phaseolus vulgaris, Biochem. J 86: 67–71.

    CAS  Google Scholar 

  • Goldstein, L. D., and Jennings, P. H., 1975, The occurrence and development of amylase enzymes in incubated, deembryonated maize kernels, Plant Physiol 55: 893–898.

    PubMed  CAS  Google Scholar 

  • Grado, C., and Ballou, C. E., 1960, Myoinositol phosphates from beef brain phosphoinositide, J. Biol. Chem 235: 23–24.

    Google Scholar 

  • Grado, C., and Ballou, C. E., 1961, Myinositol phosphates obtained by alkaline hydrolysis of beef brain phosphoinositide, J. Biol. Chem 236: 54–60.

    PubMed  CAS  Google Scholar 

  • Greaves, M. P., Anderson, G., and Webly, D. M., 1967, The hydrolysis of inositol phosphates by Aerobacter aerogenes, Biochim. Biophys. Acta 132: 412–418.

    PubMed  CAS  Google Scholar 

  • Greenberg, M. L., 1980, Genetic regulation of the bio-synthesis and utilization of inositol in yeast, Ph.D. thesis, Albert Einstein College of Medicine, New York.

    Google Scholar 

  • Greenwood, C. T., and MacGregor, A. W., 1965, The isolation of α-amylase from barley and malted barley, and a study of the properties and action-patterns of the enzymes, J. Inst. Brew. London 71: 405–417.

    CAS  Google Scholar 

  • Hasegawa, R., and Eisenberg, F., Jr., 1981, Selective hormonal control of myo-inositol biosynthesis in reproductive organs and liver of the male rat, Proc. Nat. Acad. Sci. USA 78: 4863–4866.

    PubMed  CAS  Google Scholar 

  • Hawthorne, J. N., 1960, The inositol phospholipids, J. Lipid Res 1: 255–280.

    PubMed  CAS  Google Scholar 

  • Hoffmann-Ostenhof, O., Jungwirth, C., and David, I. B., 1958, Enzymatische Phosphorylierung von Myo-Inosit. durch ein Enzym aus Hefe, Naturwissenschaften 45: 265.

    Google Scholar 

  • Hübscher, G., and Hawthorne, J. N., 1957, Isolation of inositol monophosphate from liver, Biochem. J 67: 523–527.

    PubMed  Google Scholar 

  • Huggins, C. G., Hurst, M. W., Tou, J. S., and Lee, T. C., 1969, The metabolism of the polyphosphoinositides in kidney: Studies on the phosphatidylinositol kinase, Ann. N. Y. Acad. Sci 165: 790–800.

    PubMed  CAS  Google Scholar 

  • Irving, G. C. J., and Cosgrove, D. J., 1972, Inositol phosphate phosphatases of microbiological origin: The inositol pentaphosphate products of Aspergillus ficuum phytases, J. Bacteriol 112: 434–438.

    PubMed  CAS  Google Scholar 

  • Irving, G. C. J., and Cosgrove, D. J., 1974, Inositol phosphate phosphatases of microbiological origin: Some properties of the partially purified phosphatases of Aspergillus ficuumNRRL 3135, Aust. J. Biol. Sci 27: 361–368.

    PubMed  CAS  Google Scholar 

  • Jennings, A. C., and Morton, R. K., 1963, Changes in nucleic acid and other phosphorus containing compounds of developing wheat grain, Aust. J. Biol. Sci 16: 332–341.

    CAS  Google Scholar 

  • Johnson, L. F., and Tate, M. E., 1969, Structure of “phytic acids,” Can. J. Chem 47: 63–73.

    CAS  Google Scholar 

  • Juliano, B. O., and Varner, J. E., 1969, Enzymic degradation of starch granules in the cotyledons of germinating peas, Plant Physiol 44: 886–892.

    PubMed  CAS  Google Scholar 

  • Jungalwala, F. B., Freinkel, N., and Dawson, R. M. C., 1971. The metabolism of phosphatidylinositol in the thyroid gland of the pig, Biochem. J 123: 19–33.

    PubMed  CAS  Google Scholar 

  • Kai, M., White, G. L., and Hawthorne, J. N., 1966, The phosphatidylinositol kinase of rat brain, Biochem. J 101: 328–337.

    PubMed  CAS  Google Scholar 

  • Kai, M., Salway, J. G., and Hawthorne, J. N., 1968, The diphosphoinositide of rat brain, Biochem. J 106: 791–801.

    PubMed  CAS  Google Scholar 

  • Kao, T., and Puck, T. T., 1968, Genetics of somatic mammalian cells. VII. Induction and isolation of nutritional mutants in Chinese hamster cells, Proc. Natl. Acad. Sci. U.S.A 60: 1275–1281.

    PubMed  CAS  Google Scholar 

  • Kasugai, A., 1963, Studies on the relation between germination and α-amylase formation in mung bean sprout, J. Agri. Chem. Soc. Jpn 12: 761–768.

    Google Scholar 

  • Kimura, G., 1967, Phytic acid, Yuki Gosei Kagaku Kyokai Shi 26: 167–179.

    Google Scholar 

  • Kindl, H., 1966, cyclitols and phosphoinositides. in: The Proceedings of the 2nd Meeting of the Federation of European Biochemical Societies, Vienna, Vol. 2, Pergamon Press, New York.

    Google Scholar 

  • Koller, D., Mayer, A. M., Pabjakoff-Mayher, A., and Klein, S., 1962, Seed germination, Annu. Rev. Plant Physiol 13: 437–464.

    CAS  Google Scholar 

  • Konno, S., and Aimi, R., 1959, Behavior of phosphorus compounds during the ripening of rice plants, Proc. Crop Sci. Soc. Jpn 27: 408–411.

    Google Scholar 

  • Kovacs, M. I. P., and Simpson, G. M., 1976, Dormancy and enzyme levels in seeds of wild oats, Phytochemistry. 15: 455–458.

    CAS  Google Scholar 

  • Kurasawa, H., Hayakawa, T., and Motoda, S., 1967, Biosynthesis of inositol by an enzyme system in rice seeds, Agric. Biol. Chem 31: 382–384.

    CAS  Google Scholar 

  • Lim, P. E., and Tate, M. E., 1971, The phytases. I. Lysolecithin activated phytase from wheat bran, Biochim. Biophys. Acta 250: 155–164.

    PubMed  CAS  Google Scholar 

  • Lim, P. E., and Tate, M. E., 1973, The phytases. II. Properties of phytase reactions F1 and F2 from wheat bran and the myo-inositol phosphates produced by fraction F2, Biochim. Biophys. Acta 302: 316–328.

    PubMed  CAS  Google Scholar 

  • Lipmann, F., 1951, The chemistry and thermodynamics of phosphate bonds, in: Phosphorus Metabolism, ( W. D. McElroy and B. Glass, eds.), pp. 521–550, Johns Hopkins University Press, Baltimore.

    Google Scholar 

  • Loewus, F. A., 1971, Carbohydrate interconversions, Ann Rev. Plant Physiol 22: 337–364.

    CAS  Google Scholar 

  • Loewus, F. A., 1974, The biochemistry of myo-inositol in plants, Rec. Adv. Phytochem 8: 179–207.

    CAS  Google Scholar 

  • Loewus, F. A., and Kelly, S., 1962, Conversion of glucose to inositol in parsley leaves, Biochem. Biophys. Res. Commun 7: 204–208.

    PubMed  CAS  Google Scholar 

  • Loewus, F. A., and Kelly, S., 1963, Inositol metabolism in plants. I. Labeling patterns in cell wall polysaccharides from detached plants given myo-inositol-2-t or -2-C14, Arch. Biochem. Biophys 102: 96–105.

    CAS  Google Scholar 

  • Loewus, F. A., and Loewus, M. W., 1980, myo-Inositol: Biosynthesis and metabolism, in: Biochemistry of Plants, Vol. 3 (P. K. Stumpf and E. E. Conn, eds.), pp. 43–76, Academic Press, New York.

    Google Scholar 

  • Loewus, F. A., and Loewus, M. W., 1983, myo-inositol: its biosynthesis and metabolism, Annu. Rev. Plant Physiol 34:137–161.

    CAS  Google Scholar 

  • Loewus, F. A., Loewus, M. W., Maity, I. B., and Rosenfield, C.-L., 1978, Aspects of myo-inositol metabolism and biosynthesis in higher plants, in: Cyclitols and phosphoinositides( W. W. Wells and F. Eisenberg, Jr., eds.), pp. 249–267, Academic Press, New York.

    Google Scholar 

  • Loewus, M. W., 1977, Hydrogen isotope effects in the cyclization of D-glucose-6-phosphate by myo-inositol-1-phosphate synthase, J. Biol. Chem 252: 7221–7223.

    PubMed  CAS  Google Scholar 

  • Loewus, M. W., and Loewus, F. A., 1971, The inositol and characteriszation of D-glucose-6-phosphate cycloaldolase (NAD-dependent) from Acer pseudoplatanusL. cell cultures. Its occurrence in plants, Plant Physiol 48: 255–260.

    PubMed  CAS  Google Scholar 

  • Loewus, M. W., and Loewus, F. A., 1973, D-Glucose 6-phosphate cycloaldolase: Inhibition studies and aldolase function, Plant Physiol 51: 263–266.

    PubMed  CAS  Google Scholar 

  • Maeda, T., and Eisenberg, F., Jr., 1980, Purification, structure and catalytic properties of L-myo-inositol-1-phosphate synthase from rat testis, J. Biol. Chem 255: 8458–8464.

    PubMed  CAS  Google Scholar 

  • Maiti, I. B., Majumder, A. L., and Biswas, B. B., 1974, Purification and mode of action of phytase from Phaseolus aureus, Phytochemistry 13:1047–1051.

    CAS  Google Scholar 

  • Majumder, A. L., 1972, Biosynthesis of inositol phosphates in plant, Ph.D. thesis, Calcutta University.

    Google Scholar 

  • Majumder, A. L., 1981, Coupling between fructose- 1,6-bisphosphatase and myo-inositol synthase: An hypothesis for rescue synthesis of myo-inositol, FEBS Lett. 133: 189–193.

    PubMed  CAS  Google Scholar 

  • Majumder, A. L., and Biswas, B. B., 1973a, Further characterisation of phosphoinositol kinase, Phytochemistry 12: 315–319.

    CAS  Google Scholar 

  • Majumder, A. L., and Biswas, B. B., 1973b, A protein inhibitor for phosphoinositol kinase from ungerminated mung bean seeds, Phytochemistry 12: 321–326.

    CAS  Google Scholar 

  • Majumder, A. L., and Biswas, B. B., 1973c, Metabolism of inositol phosphates. V. Biosynthesis of inositol phosphates during ripening of mung bean (Phaseolus aureus) seeds, Indian J. Exp. Biol 11: 120–123.

    CAS  Google Scholar 

  • Majumder, A. L., Mandal, N. C., and Biswas, B. B., 1972, Phosphoinositol kinase from germinating mung bean seeds, Phytochemistry 11: 503–508.

    CAS  Google Scholar 

  • Majumder, A. L., Duttagupta, S., Goldwasser, P., Donahue, T. F., and Henry, S. A., 1981, The mechanism of interallelic complementation at the ino-1locus in yeast: Immunological analysis of mutants, Mol. Gen. Geneti 184: 347–354.

    CAS  Google Scholar 

  • Mandal, N. C., and Biswas, B. B., 1970a, Metabolism of inositol phosphates. II. Biosynthesis of inositol polyphosphates in germinating seeds of Phaseolus aureus, Indian J. Biochem 7: 63–67.

    CAS  Google Scholar 

  • Mandal, N. C., and Biswas, B. B., 1970b, Metabolism of inositol phosphates. I. Phytase synthesis during germination in cotyledons of mung beans, Phaseolus aureus, Plant Physiol 45: 4–7.

    CAS  Google Scholar 

  • Mandal, N. C., Barman, S., and Biswas, B. B., 1972, Isolation, purification and characterization of phytase from germinating mung beans, Phytochemistry. 11: 495–502.

    CAS  Google Scholar 

  • Matheson, N. K., and Strother, S., 1969, The utilization of phytate by germinating wheat, Phytochemistry. 8: 1349–1356.

    CAS  Google Scholar 

  • Mauck, L. A., Wong, Y., and Sherman, W. R., 1980, L-myo-Inositol-1-phosphate synthase from bovine testis: Puification to homogeneity and partial characterization, Biochemistry 19:3623–3629.

    PubMed  CAS  Google Scholar 

  • Mayer, A. M., 1958, The breakdown of phytin and phytase activity in germinating lettuce seeds, Enzymologia 19: 1–8.

    PubMed  CAS  Google Scholar 

  • Mayer, A. M., and Mapson, L. W., 1962, Esterification of inorganic phosphate by glycolysis in extracts from normal and pentam-1-ol treated pea cotyledons, J. Exp. Bot 13: 201–212.

    CAS  Google Scholar 

  • Mayer, A. M., and Shain, Y., 1974, Control of seed germination, Annu. Rev. Plant Physiol 25: 167–193.

    CAS  Google Scholar 

  • McCane, R. A., and Widdowson, E. M., 1935, CCCXX. Phytin in human nutrition, Biochem. J 29: 2694–2699.

    Google Scholar 

  • Michell, R. H., and Hawthorne, J. N., 1965, The site of diphosphoinositide synthesis in rat liver, Biochem. Biophys. Res. Commun 21: 333–338.

    PubMed  CAS  Google Scholar 

  • Molinari, E., and Hoffmann-Ostenhof, O., 1967, On the biosynthesis of phytic acid, Indian J. Biochem. 4:17P–18P.

    Google Scholar 

  • Mori, H., 1969, Studies on phytin. 3. Changes in inositol phosphates during the ripening of soybean, Jpn. Soc. Food. Nutr. J 22: 122–125.

    CAS  Google Scholar 

  • Morohashi, Y., and Shimokoriyama, M., 1972, Physiological studies on germination of Phaseolus mango seeds, J. Exp. Bot 23: 54–61.

    CAS  Google Scholar 

  • Morton, R. K., and Raison, J. K., 1963, A complete intracellular unit for incorporation of amino acid into storage protein utilizing adenosine triphosphate generated from phytate., Nature (London) 200: 429–433.

    CAS  Google Scholar 

  • Mossberg, Y., Mayer, A. M., and Mapson, L. W., 1964, Inhibition of glycolysis by adenosine triphosphate, J. Exp. Bot, 15: 29–34.

    CAS  Google Scholar 

  • Murata, T., Akazowa, T., and Fukuchi, S., 1968, Enzymic mechanism of starch breakdown in germinating rice seeds. 1. An analytical study, Plant Physiol 43: 1899–1905.

    PubMed  CAS  Google Scholar 

  • Nagai, Y., and Funahashi, S., 1962, Phytase (myoinositolhexaphosphate phosphohydrolase) from wheat bran. 1. Purification and substrate specificity, Agric. Biol. Chem 26: 794–803.

    CAS  Google Scholar 

  • Paulus, H., and Kennedy, E. P., 1960, The enzymatic synthesis of inositol monophosphatide, J. Biol. Chem 235: 1303–1311.

    PubMed  CAS  Google Scholar 

  • Pfeffer, E., 1872, Pringsheim’s Jahrb. Wiss. Bot 8: 429–475.

    Google Scholar 

  • Pina, M. Z., Castanedo, C., Escamilla, E., and Pina, E., 1978, Further characterization of the myo-inositol-l-phosphate synthase from Neurospora crassa, in: Cyclitols and Phosphoinositides( W. W. Wells and F. Eisenberg, Jr., eds.), pp. 297–310, Academic Press, New York.

    Google Scholar 

  • Pittner, F., and Hoffmann-Ostenhof, O., 1976, Herstellung hochgereinigter myo-Inosit-l-phosphat synthase aus Stierhoden and vergleich mit dem entsprechender Enzym aus Rattenhoder, Monatsh. Chem 107: 793–797.

    CAS  Google Scholar 

  • Powar, V. K., and Jagannathan, V., 1967, Phytase from Bacillus subtilis, Indian J. Biochem 4: 184–185.

    PubMed  CAS  Google Scholar 

  • Preece, I. A., Grav, H. J., and Wadham, A. T., 1960, J. Inst. Brewing 66: 487.

    CAS  Google Scholar 

  • Quebedeaux, B., 1981, Adenylate and nicotinamide nucleotides in developing soy bean seeds during seed-fill, Plant Physiol 68: 23–27.

    PubMed  CAS  Google Scholar 

  • Raison, J. K., and Evans, W. J., 1968, The enthalpy change in the hydrolysis of the phosphate esters of myo-inositol, Biochim. Biophys. Acta 170: 448–451.

    PubMed  CAS  Google Scholar 

  • Roberts, R. M., and Loewus, F. A., 1968, Inositol metabolism in plants. VI. Conversion of myo-inositol to phytic acid in Wolffiella floridana, Plant Physiol 43: 1710–1716.

    PubMed  CAS  Google Scholar 

  • Rosenfield, C. L., and Loewus, F. A., 1978, Metabolic studies on intermediates in the myo-inositol oxidation pathway in Lilium longiflorumpollen. III. Polysaccharidic origin of labelled glucose, Plant Physiol 61: 101–103.

    PubMed  CAS  Google Scholar 

  • Saio, K., 1964, The change in inositol phosphates during the ripening of rice grains, Plant Cell Physio 5: 393–400.

    CAS  Google Scholar 

  • Sartirana, M. L., and Bianchetti, R., 1967, The effects of phosphate on the development of phytase in the wheat embryo, Physiol. Plant 20: 1066–1075.

    CAS  Google Scholar 

  • Schablik, M., Zsindely, A., Aradi, J., Fekete, Z., and Szabo, G., 1978, Differences between transformed and spontaneous revenant strains of Neurospora crassa, Neurospora News Lett. O. N., 25, p. 22.

    Google Scholar 

  • Sexton, J. C., and Morre, S. T., Jr., 1981, Phosphatidylinositol synthesis by a Mn+2-dependent exchange enzyme in caster bean endosperm, Plant Physiol 68: 18–22.

    PubMed  CAS  Google Scholar 

  • Sherman, W. K., Rasheed, A., Mauck, L. A., and Wiecko, 1977, Incubations of testis myo-inositol-1 -phosphate synthase with D-[5-18)] glucose-6-phosphate and with H218O show no evidence of Schiff base formation, J. Biol. Chem 252: 5672–5676.

    PubMed  CAS  Google Scholar 

  • Sherman, W. R., Hipps, P. P., Mauck, L. A., and Rasheed, A., 1978, Studies on enzymes of inositol metabolism, in: Cyclitols and Phosphoinositides( W. W. Wells and F. Eisenberg, Jr., eds.), pp. 279–295, Academic Press, New York.

    Google Scholar 

  • Simmonds, J. A., and Simpson, G. M., 1971, Increased participation of pentose phosphate pathway in response to after-ripening and gibberellic acid treatment caryopses of Avena fatua, Can. J. Bot 49:1833–1840.

    CAS  Google Scholar 

  • Sloane-Stanley, G. H., 1953, Anaerobic reactions of phospholiids in brain suspensions, Biochem. J 53: 613–619.

    PubMed  CAS  Google Scholar 

  • Sobolev., A. M., 1962, Occurrence, formation and utilization of phytin in higher plants, Usp. Biol. Khim 4: 248–261.

    CAS  Google Scholar 

  • Swain, R. R., and Dekker, E. E., 1966a, Seed germination studies. 1. Purification and properties of an α-amylase from the cotyledons of germinating peas, Biochim. Biophys. Acta 122: 75–86.

    CAS  Google Scholar 

  • Swain, R. R., and Dekker, E. E., 1966b, Seed germination studies. II. Pathways for starch degradation in germinating pea seedlings, Biochim. Biophys. Acta 122: 87–100.

    CAS  Google Scholar 

  • Swain, R. R., and Dekker, E. E., 1969, Seed germination studies. III. Properties of a cell-free amino acid incorporating system from pea cotyledons: Possible origin of cotyledonary α-amylase, Plant Physiol 44: 319–325.

    PubMed  CAS  Google Scholar 

  • Takenawa, T., Saito, M., Nayal, Y., and Egawa, K., 1977, Solublization of the enzyme catalyzing CDP-diglyceride-independent incorporation of myo-inositol into phosphatidylinositol and its comparison to CDP-diglyceride:inositol transferase, Arch. Biochem. Biophys 182: 244–250.

    PubMed  CAS  Google Scholar 

  • Tanaka, K., Watanabe, K., Asada, K., and Kasai, Z., 1971, Occurrence of myo-inositol nomo-phosphate and its role in ripening rice grains, Agric. Biol. Chem 35: 314–320.

    CAS  Google Scholar 

  • Tanaka, K., Yoshida, T., Asada, K., and Kasai, Z., 1973, Subcellular particles isolated from aleurona layer of rice seeds, Arch. Biochem. Biophys 155: 136–143.

    PubMed  CAS  Google Scholar 

  • Tanaka, Y., Ito, T., and Akazawa, T., 1970, Enzymic mechanism of starch breakdown in germinating rice seeds. III. α-Amylase isozymes, Plant Physiol 46: 650–654.

    PubMed  CAS  Google Scholar 

  • Tarrago, J. F., and Nicolas, G., 1976, Starch degradation in the cotyledons of germinating lentils, Plant Physiol 58: 618–621.

    PubMed  CAS  Google Scholar 

  • Taylorson, R. B., and Hendricks, S. B., 1977, Dormancy in seeds, Annu. Rev. Plant Physiol 28: 331–354.

    CAS  Google Scholar 

  • Theodorou, C., 1971, The phytase activity of the mycorrhizal fungus Rhizopogon luteolus, Soil Biol. Biochem 3: 89–90.

    CAS  Google Scholar 

  • Thompson, W., and Dawson, R. M. C., 1964a, The hydrolysis of triphosphoinositide by extracts of ox brain, Biochem. J 91: 233–236.

    CAS  Google Scholar 

  • Thompson, W. and Dawson, R. M. C., 1964b, The triphosphoinositide phosphodiesterase of brain tissue, Biochem. J 91: 237–243.

    CAS  Google Scholar 

  • Tomlinson, R. V., and Ballou, C. E., 1962, myo-Inositol polyphosphate intermediates in the dephosphorylation of phytic acid by phytase, Biochemistry. 1:166–171.

    PubMed  CAS  Google Scholar 

  • Umezurike, G. M., and Numfor, F. A., 1979, Changes in the content of starch and activities of some enzymes of carbohydrate metabolism in cotyledons of germinating seeds of Voandzeia subterranea, J. Exp. Bot 30: 583–588.

    CAS  Google Scholar 

  • Waime, J. M., 1958, Accumulation de I’acide phosphorique (phytime, polyphosphates), in: Handbuch der pflanzen physiologie, Vol. IX ( W. Rhuland, ed.), pp. 136–148, Springer-Verlag, Berlin.

    Google Scholar 

  • Wells, W. W., and Eisenberg, F., Jr., (eds.), 1978, Cyclitols and Phosphoinositides, Academic Press, New York.

    Google Scholar 

  • Williams, S. G., 1970, The role of phytic acid in wheat grain, Plant Physiol 45: 376–381.

    PubMed  CAS  Google Scholar 

  • Williams, S. G., 1971, Biosynthesis of inositol by inositol-less mutants of Neurospora crassa, Aust. J. Biol. Sci 24: 1181–1188.

    CAS  Google Scholar 

  • Yamamoto, Y., 1963, Pyridine nucleotide content in the higher plant: Effect of age of tissue, Plant Physiol 38: 45–54.

    PubMed  CAS  Google Scholar 

  • Yamamoto, Y., 1966, NAD kinase in higher plants, Plants Physiol 41: 523–528.

    CAS  Google Scholar 

  • Zsindely, A., Szaboles, M., Aradi, J., Schablik, M., Kiss, A., and Szabo, G., 1977, Investigations on myo-inositol-l-phosphate synthase from the wild type and the inositol-dependent mutant of Neurospora crassa, Acta. Biol. Acad. Sci. Hung 28: 281–290.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1984 Plenum Press, New York

About this chapter

Cite this chapter

Biswas, B.B., Ghosh, B., Majumder, A.L. (1984). myo-Inositol Polyphosphates and Their Role in Cellular Metabolism. In: Roodyn, D.B. (eds) Subcellular Biochemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2709-7_4

Download citation

  • DOI: https://doi.org/10.1007/978-1-4613-2709-7_4

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-9682-9

  • Online ISBN: 978-1-4613-2709-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics