Myoinositol Polyphosphate Intermediates in the Dephosphorylation of Phytic Acid by Phytase<sup>*</sup>

Tomlinson, R. V.; Ballou, Clinton E.

doi:10.1021/bi00907a025

Cited by 89 publications

(44 citation statements)

References 11 publications

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“…Tomlinson and Ballou (1962) had previously made a similar observation in connection with the pathway of degradation of myo-inositol hexaphosphate (I) by wheat-bran phytase. In terms of the proposed model this preferential hydrolysis, by Pseudomonas phytase, of phosphate groups which are vicinal to a hydroxyl group can be explained by the fact that a hydroxyl oxygen atom would be a stronger nucleophile than a phosphate ester-bond oxygen and so would compete more effectively for site B (Fig.…”

Section: Resultsmentioning

confidence: 61%

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Inositol Phosphate Phosphatases of Microbiological Origin.Observations on the Nature of the Active Centre of a Bacterial (Pseudomonas Sp.) Phytase

Irving¹,

Cosgrove²

1971

Aust. Jnl. Of Bio. Sci.

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Ab8tractThe pentaphosphates produced by a bacterial phytase acting on myo-and I,-ckiro-inositol hexaphosphates as substrates were identified by ion-exchange chromatography. On the basis of the structures of these pentaphosphates and the previously published properties of the bacterial phytase, a simple model for the active centre of the enzyme is proposed which is capable of explaining the intermediates, as far as the diphosphate stage, isolated by Cosgrove from the hydl'olysates of myo·, D.ckiro-, and 8cyllo-inositol hexaphosphates due to the action of this enzyme.With slight modification this model for the active centre is also capable of explaining, as far as the diphosphate stage, the intermediates isolated by Tomlinson and Ballou from the hydrolysate of myo·inositol hexaphosphate by wheat-bran phytase.

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Section: Resultsmentioning

confidence: 61%

“…In addition, if sites A and B in Figure 3 are transposed, a model is created which is capable of explaining the intermediates, as far as the diphosphate stage, detected by Tomlinson and Ballou (1962) in the hydrolysate of myo-inositol hexaphosphate (I) by wheat-bran phytase.…”

Section: Resultsmentioning

confidence: 99%

Inositol Phosphate Phosphatases of Microbiological Origin.Observations on the Nature of the Active Centre of a Bacterial (Pseudomonas Sp.) Phytase

Irving¹,

Cosgrove²

1971

Aust. Jnl. Of Bio. Sci.

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“…2 (12) and TOMLINSON and BALLOU (17), Na-IP 8 was hydrolyzed with phytase until SO% of the phosphorus was liberated. The hydrolysate was adjusted to pH 7.…”

Section: ) Preparation Of the Thin Layermentioning

confidence: 99%

Thin layer chromatography of inositol phosphates and inositol in humic and fulvic acid fractions

Hong

Yamane

1980

Soil Science and Plant Nutrition

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“…(ii) Kinetics myo-Inositol hexaphosphate is hydrolysed by both wheat-bran phytase (Tomlinson and Ballou 1962) and Pseudomonas phytase (Cosgrove 1970) in a stepwise manner. In order to limit the kinetic study of the Pseudomonas phytase, as far as possible, to the hexaphosphate -+ pentaphosphate step the assays were carried out on a large scale and the maximum degree of hydrolysis thus limited to 5% of the total ester-phosphate present in the added substrate.…”

Section: (B) Properties Of Partially Pur~fied Pseudomonas Phytase (I)mentioning

confidence: 99%

Inositol Phosphate Phosphatases of Microbiological Origin. Some Properties of a Partially Purified Bacterial (Pseudomonas Sp.) Phytase

Irving¹,

Cosgrove²

1971

Aust. Jnl. Of Bio. Sci.

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A phytase (E.C. 3.1.3.8) was extracted from a bacterium (Pseudomonas sp.) and purified 25-fold by ammonium sulphate fractionation, gel filtration, and ionexchange cellulose chromatography. Its properties are compared with the published properties of some plant phytases and a bacterial phytase.The pH optimum at 40°C is 5· 5, and at this pH the kinetics, at substrate concentrations above 18·3 JLM, are consistent with partially non-competitive substrate inhibition. At lower substrate concentrations the kinetics deviate from this model.Of a range of potential substrates tested at 0·36 mM, only p-nitrophenyl phosphate and inositol hexaphosphates were hydrolysed. The order of the rates of hydrolysis of the inositol hexaphosphates was myo-The enzyme is inhibited by 1 mM (+ )-tartrate and 1 mM EDTA; 1 mM oxalate and citrate are without effect on the activity of the enzyme while the degree of inhibition of the enzyme by fluoride ion appears to be a function of the cube of the fluoride ion concentration.

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Myoinositol Polyphosphate Intermediates in the Dephosphorylation of Phytic Acid by Phytase^*

Cited by 89 publications

References 11 publications

Inositol Phosphate Phosphatases of Microbiological Origin.Observations on the Nature of the Active Centre of a Bacterial (Pseudomonas Sp.) Phytase

Inositol Phosphate Phosphatases of Microbiological Origin.Observations on the Nature of the Active Centre of a Bacterial (Pseudomonas Sp.) Phytase

Thin layer chromatography of inositol phosphates and inositol in humic and fulvic acid fractions

Inositol Phosphate Phosphatases of Microbiological Origin. Some Properties of a Partially Purified Bacterial (Pseudomonas Sp.) Phytase

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Myoinositol Polyphosphate Intermediates in the Dephosphorylation of Phytic Acid by Phytase*

Cited by 89 publications

References 11 publications

Inositol Phosphate Phosphatases of Microbiological Origin.Observations on the Nature of the Active Centre of a Bacterial (Pseudomonas Sp.) Phytase

Inositol Phosphate Phosphatases of Microbiological Origin.Observations on the Nature of the Active Centre of a Bacterial (Pseudomonas Sp.) Phytase

Thin layer chromatography of inositol phosphates and inositol in humic and fulvic acid fractions

Inositol Phosphate Phosphatases of Microbiological Origin. Some Properties of a Partially Purified Bacterial (Pseudomonas Sp.) Phytase

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Myoinositol Polyphosphate Intermediates in the Dephosphorylation of Phytic Acid by Phytase^*