Occurrence of neo-Inositol Hexaphosphate in Soil

Cosgrove, D. J.; Tate, Max E.

doi:10.1038/200568b0

Cited by 33 publications

(25 citation statements)

References 4 publications

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“…Similar small increases in specific activity in the purification of extracellular fungal enzymes have been reported for a crystalline preparation of a proteinase from A. sydowi (purification = ·45) (Danno and Yoshimura 1967) and for leucine aminopeptidase I from A. oryzae (purification = 4·4) (Nakadai et al 1973).…”

Section: Discussionmentioning

confidence: 57%

“…The order of ease of hydrolysis of the isomers ofmyo-inositol hexakisphosphate by the phytase at pH 5·3 (Table 3) is the inverse of the order of their abundance in soil (Cosgrove 1963;Cosgrove and Tate 1963). This suggests that extracellular phytases produced in soil by fungi similar to A.ficuum NRRL 3135 could playa part in determining the relative abundance of these isomers in soil.…”

Section: (Iii) Relative Rates Of Hydrolysis Of Inositol Hexakisphosphmentioning

confidence: 82%

“…The relative rates of hydrolysis of those isomers of inositol hexakisphosphate known to occur in soil (Cosgrove 1962;Cosgrove and Tate 1963) are recorded in Table 3, together with the relative rates for binary equimolar (0· 7 mM) mixtures of each of the isomers with myo-inositol hexakisphosphate. The use of the binary mixtures was to determine if the two isomers were hydrolysed by the same or by different active centres on the enzyme.…”

Section: Relative Rates Of Hydrolysis Of Inositol Hexakisphosphatesmentioning

confidence: 99%

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Inositol Phosphate Phosphatases of Microbiological Origin. Some Properties of the Partially Purified Phosphatases of Aspergillus ficuum NRRL 3135

Gc¹,

Dj²

1974

Aust. Jnl. Of Bio. Sci.

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Partially purified samples of the acid phosphatase (EC 3.1.3.2) and of the phytase (EC 3.1.3.8) from A. ficuum were prepared by gel-filtration and ion-exchange dextran chromatography.The pH optimum in o· 02M phthalate buffer of the acid phosphatase was found to be 2·2, while in the same buffer the phytase was found to have at least two optima at pH 2·5 and 5·3, with the suggestion of a third at pH 2·8.The Km value of the acid phosphatase was 1 ·27 x 10-4M with sodium myo-inositol hexakisphosphate as substrate at pH 2· 2. Similarly the Km value of the phytase at pH 2· 5 was 2·44 x 10-sM and at pH 5·3 it was 1·29 x 10-SM.Of a range of inositol hexakisphosphates tested as substrates the order of ease of hydrolysis wasfor the phytase at pH 5·3.The major pentakisphosphate produced by the acid phosphatase at pH 2·2 from both D-chiroand L-chiro-inositol hexakisphosphate was the respective 1,2,3,4,6-pentakisphosphate. In the case of the phytase, at both pH 2·5 and 5·3 the major pentakisphosphate products were the 1,2,3,4,6-and the 1,2,3,5,6-isomers from the D-chiro-and L-chiro-substrates respectively.Neither enzyme was inhibited by 1 mM oxalate, 1 mM citrate, 1 mM EDTA or 1 mM (+ )-tartrate The activity of the acid phosphatase was reduced to 17% and that of the phytase at pH 2·5 to 69% by 1 mM fluoride. The phytase was not inhibited at pH 5·3 by any of the anions tested.

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Section: Discussionmentioning

confidence: 57%

Section: (Iii) Relative Rates Of Hydrolysis Of Inositol Hexakisphosphmentioning

confidence: 82%

Section: Relative Rates Of Hydrolysis Of Inositol Hexakisphosphatesmentioning

confidence: 99%

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Inositol Phosphate Phosphatases of Microbiological Origin. Some Properties of the Partially Purified Phosphatases of Aspergillus ficuum NRRL 3135

Gc¹,

Dj²

1974

Aust. Jnl. Of Bio. Sci.

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“…The greatest concentrations appear to occur in grassland soils, but IP 6 has also been detected in crop soils, forest soils, and rice paddies (Turner, 2007). Four stereoisomers of IP 6 have been identified in soils; the most abundant is the myo isomer, with smaller amounts of the scyllo, neo and D-chiro isomers (Cosgrove, 1962;Cosgrove and Tate, 1963;Turner, 2007;Turner et al, 2012). myo-Inositol hexakisphosphate is the main P compound in seeds and is also present in manure from monogastric animals, which are not able to digest myo-IP 6 (Cosgrove, 1980;Leytem and Maguire, 2007).…”

Section: Introductionmentioning

confidence: 99%

Identification of inositol hexakisphosphate binding sites in soils by selective extraction and solution 31P NMR spectroscopy

Jørgensen

Turner²,

Reitzel

2015

Geoderma

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“…So far, the most abundant inositol isomer encountered in nature has been myo-inositol, whereas neo-inositol is only a relatively rare isomer. Neo-InsP 6 has first been recognized as a soil constituent (22). Mixtures of myo-, scyllo-, chiro-, and neo-inositol are indeed present in soil as their pentakisphosphate and hexakisphosphate esters (23).…”

Section: Discussionmentioning

confidence: 99%

neo-Inositol Polyphosphates in the AmoebaEntamoeba histolytica

Martin

Laussmann

Bakker-Grunwald

et al. 2000

Journal of Biological Chemistry

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We have reexamined the structure of inositol phosphates present in trophozoites of the parasitic amoeba Entamoeba histolytica and show here that, rather than being myo-inositol derivatives (Martin, J.-B., BakkerGrunwald, T., and Klein, G. (1993) Eur. J. Biochem. 214, 711-718), these compounds belong to a new class of inositol phosphates in which the cyclitol isomer is neoinositol. The structures of neo-inositol hexakisphosphate, 2-diphospho-neo-inositol pentakisphosphate, and 2,5-bisdiphospho-neo-inositol tetrakisphosphate, which are present in E. histolytica at concentrations of 0.08 -0.36 mM, were solved by two-dimensional 31 P-1 H NMR spectroscopy. No evidence for the co-existence of their myo-inositol counterparts has been found. These neoinositol compounds were not substrates of 6-diphosphoinositol pentakisphosphate 5-kinase, an enzyme purified from Dictyostelium discoideum that phosphorylates 6-diphospho-myo-inositol pentakisphosphate and more slowly also myo-inositol hexakisphosphate, specifically on position 5. Because preliminary data indicate that large amounts of the same neo-inositol phosphate and diphosphate esters are also present in another primitive amoeba, Phreatamoeba balamuthi, the occurrence of high concentrations of neo-inositol polyphosphates may be much more general than previously thought.Inositol phosphates are members of a large family of naturally occurring compounds that because of their complex role in cell signaling and homoeostasis have been intensively studied during the last two decades (1). Research has focused mainly on the commonly known myo-derivatives, although many other naturally occurring inositol stereoisomers are known. The most abundant and ubiquitous member of the family, myo-InsP 6 , has been shown to reach an intracellular concentration close to 1 mM in Dictyostelium discoideum (2, 3). Recently, new members of this class of compounds have been identified in cellular slime molds as 5-PP-and 6-PP-myo-InsP 5 1 and 3,5-bis-PP-and 5,6-bis-PP-myo-InsP 4 (4 -6). The same or similar highly phosphorylated and diphosphorylated compounds have been detected in free living and parasitic amoebae and a number of mammalian cell types (7-11). The latter molecules may function in cell signaling (2,(12)(13)(14). Entamoeba histolytica is a human intestinal parasite that causes amoebiasis. Its trophozoites contain high amounts of inositol polyphosphates (8). myo-Inositol is the major cyclitol building natural inositol polyphosphates, and other isomers are only rarely found and in very low concentrations. Consequently, the two major inositol phosphates of E. histolytica have been preliminarily identified as myo-inositol 2,4,6-triphosphate and 5-PP-myo-InsP 5 (8). However, we subsequently noticed during comparative studies by high resolution anion exchange chromatography that the inositol polyphosphates from E. histolytica were not eluted exactly with the same retention time as the myo-inositols used as reference. This casted some doubt on the previous identification. Therefore, we have r...

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Occurrence of neo-Inositol Hexaphosphate in Soil

Cited by 33 publications

References 4 publications

Inositol Phosphate Phosphatases of Microbiological Origin. Some Properties of the Partially Purified Phosphatases of Aspergillus ficuum NRRL 3135

Inositol Phosphate Phosphatases of Microbiological Origin. Some Properties of the Partially Purified Phosphatases of Aspergillus ficuum NRRL 3135

Identification of inositol hexakisphosphate binding sites in soils by selective extraction and solution 31P NMR spectroscopy

neo-Inositol Polyphosphates in the AmoebaEntamoeba histolytica

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