Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.8 (phytase)
 1,997 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Basal and stimulated levels of inositol phosphates were determined in the protozoan Paramecium labelled with myo-[3H]inositol. Under resting conditions, intracellular InsP6 (phytic acid), InsP5 and InsP4 concentrations were 140, 10 and 2 microM, respectively. InsP5 was comprised of 56% Ins(1,2,3,4,5)P5 and/or Ins(1,2,3,5,6)P5, 40% Ins(1,2,4,5,6)P5 and/or Ins(2,3,4,5,6)P5 and small amounts of Ins(1,3,4,5,6)P5 and Ins(1,2,3,4,6)P5. InsP4 was mainly Ins(1, 4, 5, 6)P4 and/or Ins(3, 4, 5, 6)P4. Other inositol phosphates were not detected at a detection limit of 50-85 nM. Using various depolarizing and hyperpolarizing stimuli, no significant changes in level of inositol phosphates were observed in vivo, indicating that in the ciliate a contribution of inositol phosphates to signal-transduction mechanisms is unlikely. In homogenates prepared from myo-[3H]inositol-labelled cells, a marked relative increase in InsP3 and InsP4 over the concentrations in vivo was observed. These inositol phosphates were identified as degradation products of endogenous InsP6. A novel separation methodology for inositol phosphates was established to allow unequivocal assignment of phosphate locations of all dephosphorylated InsP6-derived products. The dephosphorylation was catalyzed by a phytase-like enzyme with a molecular mass of 240 kDa, most likely of a hexameric structure. The enzyme had a pH optimum of 7.0 and did not require divalent cations for activity. Substrate concentrations above 300 microM were inhibitory. Dephosphorylation of InsP6 by the Paramecium enzyme differs from that of phytases from plants in that it proceeds via a sequential release of phosphate groups from positions 6, 5, 4 and 3 of the myo-inositol ring or/and positions 4, 5, 6 and 1.
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PMID:Metabolism of inositol phosphates in the protozoan Paramecium. Characterization of a novel inositol-hexakisphosphate-dephosphorylating enzyme. 162 59

The activities of phytase and alkaline phosphatase in the intestine gradually increased in parallel during development of rats, but the 70K and 90K subunits were expressed differentially; only the 70K subunit was detected at birth, whereas the 90K subunit appeared at the weaning period (3 weeks after birth). When rats were forced to wean at 18 days old and fed laboratory chow, the enzyme activity increased markedly and the 90K subunit appeared within 1 day. These findings suggest that weaning is involved in the change in the subunit composition. Increases in the enzyme activity and amount of the 90K subunit were significantly delayed by feeding weanling animals on casein diet, but induced significantly by feeding them on casein diet supplemented with phytate. Thus induction of the 90K subunit seems to be accelerated by intake of phytic acid in the diet. The Km value of the enzyme from suckling rats for phytate was 5.25 mM, while that of adult rats was 0.213 mM. In contrast, the Km value for p-nitrophenyl phosphate (PNPP) was constant during development. The phytase activity of suckling rats did not show a distinct pH-dependence. These findings suggest that the 90K subunit may play some important roles in expressing an efficient phytase activity.
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PMID:Developmental and dietary induction of the 90K subunit of rat intestinal phytase. 165 11

Phytate is one of the major inhibiting factor for zinc and iron absorption. When phytate is hydrolyzed during the food process the mineral availability is increased. By activation of the endogenous enzyme phytase which is present in plant foods, or addition of phytase, phytate is degraded to various inositolphosphates containing 1-5 phosphate groups per an inositol molecule. The effects of degradation products of phytate on availability of zinc, calcium and iron have to be further investigated. Food processes including soaking, germination and fermentation were under optimal conditions demonstrated to completely reduce the phytate content of cereals and vegetables. The results were related to in vitro measurements of iron availability and human iron and zinc absorption studies.
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PMID:The effect of food processing on phytate hydrolysis and availability of iron and zinc. 165 32

A phytase (EC 3.1.3.8) was extracted from rat intestinal bacterium, Klebsiella Sp. No. PG.-2, and purified 50-fold by ammonium sulphate fractionation, ion-exchange chromatography and gel filtration. The enzyme is inducible in nature. The pH optimum was at 6.0 for all the inositol phosphates studied and this characterized the enzyme as an acid phosphohydrolase. Of a range of potential substrates tested, only p-nitrophenyl phosphate alongwith the inositol phosphates was hydrolyzed. It exhibits a Km of 2.0 mM; temperature optimum of 37 degrees C and energy of activation 9,120 cal/mole for all the inositol phosphates studied. The activity was inhibited by Ag2+, Hg2+, Cu2+, fluoride and high substrate concentration.
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PMID:Phytase from Klebsiella Sp. No. PG-2: purification and properties. 216 21

Inositol compounds with three to five phosphate groups (IP3-IP5) were produced by hydrolysis of phytate (inositol hexaphosphate, IP6) and their binding affinities for calcium and zinc investigated at neutral pH with relative concentrations that had been found in a range of students' meals. Zn solubility was negligible at many of these concentrations, with less Zn bound to precipitates of Ca-IP6 than Ca-IP5. The capacity to precipitate Zn at these ratios fell between IP5 and IP3. Zn was partially desorbed by soluble chelators (histidine and picolinate), especially when it had been adsorbed to preformed Ca-IP precipitates. A lower proportion of Zn was accessible to soluble chelators from Ca-IP4 than the other compounds. IP3-IP4 were hydrolysed by phytase more readily than IP5-IP6.
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PMID:Binding of zinc and calcium to inositol phosphates (phytate) in vitro. 240 Jul 62

Soybean phytase (myo-inositol-hexakisphosphate phosphohydrolase; EC 3.1.3.8) was purified from 10-day-old germinating cotyledons using a four-step purification scheme. Phytase was separable from the major acid phosphatase present, and stained as a minor band of the three acid phosphatases detectable by activity staining after gel electrophoresis. The purified enzyme exhibited two closely migrating bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of approximately 59 and 60 KDa. The molar extinction coefficient of the enzyme at 280 nm was estimated to be 7.5 X 10(4) M-1 cm-1. The isoelectric point of phytase, as judged by the elution profile on chromatofocusing, was about 5.5. The enzyme was totally absorbed to a Procion Red HE3B column and eluted as a single protein component at a salt concentration of 250-300 mM. The enzyme possessed a high affinity for phytic acid (apparent Km = 48 microM), and was strongly inhibited by phosphate (apparent Ki = 18 microM), vanadate, and fluoride. Characteristic of other plant phytases, the pH and temperature optima were 4.5-4.8 and 55 degrees C, respectively.
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PMID:Purification and characterization of phytase from cotyledons of germinating soybean seeds. 282 33

Soybean acid phosphatase (orthophosphoric-monoester phosphohydrolase, EC 3.1.3.2) was completely separated from phytase (EC 3.1.3.8) isolated from cotyledons of germinating seeds and purified to homogeneity. A four-step purification regimen consisting of ammonium sulfate fractionation, and ion-exchange, affinity, and chromatofocusing gel chromatographies was employed to achieve a homogeneous preparation. Acid phosphatase activity appeared as a major band of the three forms of acid phosphatase identified on native gels. The purified enzyme had a molecular weight of 53,000 when electrophoresed on 8% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and a molecular weight of 53,000 from its mobility in a Fracto-gel TSK HW-50F gel permeation column. The molar extinction coefficient of the enzyme at 278 nm was estimated to be 4.2 X 10(4) M-1 cm-1. The isoelectric point of the protein, as revealed by chromatofocusing, was about 6.7. The optimal pH for activity, like other plant acid phosphatases, was 5.0. While the enzyme failed to accommodate phytate as a substrate, the enzyme did exhibit a broad substrate selectivity. The affinity of the enzyme for p-nitrophenyl phosphate was high (Km = 70 microM), and activity was competitively inhibited by orthophosphate (Ki = 280 microM). The estimated catalytic turnover number (Kcat) of the enzyme for p-nitrophenyl phosphate was about 430 per second. Although the purified enzyme was stable at 0 degrees C and exhibited maximum catalytic activity at 60 degrees C, thermal inactivation studies indicated that the enzyme lost 100% activity after treatment at 68 degrees C for 10 min.
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PMID:Purification and characterization of acid phosphatase from cotyledons of germinating soybean seeds. 282 34

Aspergillus ficuum phytase was covalently immobilized on Fractogel TSK HW-75 containing 2-oxy-l-alkylpyridinium salts. A packed-bed bioreactor was constructed with the immobilized phytase. An HPLC ion-exchange method was used to analyze the enzymatic products of the bioreactor. Immobilized fungal phytase was able to hydrolyze myo-inositol Hexa-, penta-, tetra-, tri-, and diphosphates. When the substrate solution was recirculated for 5 hr in the bioreactor about 50% inorganic orthophosphate was released and myo-inositol-diphosphate and mono-phosphate were the only remaining products.
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PMID:Immobilization of Aspergillus ficuum phytase: product characterization of the bioreactor. 285 8

The activity and basic kinetic constants of phytase were studied in chicken erythrocytes during animal development. The regulatory inhibition of phytase by IHP and 2,3-BPG takes place at key stages of the development. As in mammals, there is a specific control of the levels of organic phosphate involved in the oxygenation process of haemoglobin, during animal development.
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PMID:Phytase activity in chicken erythrocytes and its control by organic phosphates (glycerate-2,3-P2 and inositol-P5) during avian development. 298 56

Alkaline phosphatase, highly purified from bovine intestinal mucosa, has significant hydrolytic activity against phytate and CaATP. Phytase and CaATPase activities require quite different assay conditions than those which are optimal for conventional alkaline phosphatase substrates such as 4-nitrophenyl phosphate. We have used affinity chromatography and antibody recognition to demonstrate that the phytase and CaATPase activities are not due to contaminating enzymes, but are intrinsic activities of intestinal alkaline phosphatase. All of the phytase and CaATPase activities present in crude extracts of bovine intestinal mucosa can be accounted for by alkaline phosphatase. Apparently neither phytase nor CaATPase exist in this tissue as independent enzymes. Specific substrates which require assay conditions quite different from the conventional 4-nitrophenyl phosphate substrate may account for the physiological function of "alkaline phosphatase."
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PMID:The relationship of alkaline phosphatase, CaATPase, and phytase. 299 87


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