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

As the initial step in a project to provide a more cost-effective source of the phytase enzyme, this paper reports on the use of a polyclonal antibody raised to phytase purified from an isolate of Aspergillus niger (A. ficuum) to screen an A. niger lambda gt11 expression library and the use of amino acid sequencing to identify a clone containing part of the fungal phytase gene. The described use of amino acid sequence fragments to verify the cloning of a gene has potential applications in other cloning projects.
 ...
PMID:Positive identification of a lambda gt11 clone containing a region of fungal phytase gene by immunoprobe and sequence verification. 136 40

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.
 ...
PMID:Metabolism of inositol phosphates in the protozoan Paramecium. Characterization of a novel inositol-hexakisphosphate-dephosphorylating enzyme. 162 59

Some cereal by-products, such as bran, exhibit a high phytase activity that may enhance phytate P digestibility. This was studied in growing pigs fed a phytase-rich (1,200 IU/kg) diet containing 20% rye bran. The trial involved 12 animals; six were fed a control diet and six were fed a diet containing rye bran for 2 mo. Both diets contained the same levels of energy, protein, Ca (.7%) and total P (.4%). No inorganic P was added; thus, the dietary P was mainly phytic. Pigs fed the control diet, in contrast to those fed the diet containing rye bran, developed a P deficiency, as indicated by hypophosphatemia, hypophosphaturia, hyperhydroxyprolinuria, hypercalcemia, and hypercalciuria. Phosphorus from the rye bran diet was more completely absorbed (55 vs 36%) and retained (50 vs 36%) than that from the control diet. Calcium absorption was equal for the two diets, but Ca retention was higher in pigs fed rye bran than in controls. Pigs fed the rye bran diet showed greater bone density, ash content, and bending moments than controls. In conclusion, high dietary phytase levels or phytase-rich by-products increased phytate P availability and consequently improved bone scores.
 ...
PMID:Enhancement of phosphorus utilization in growing pigs fed phytate-rich diets by using rye bran. 164 62

Reaction of Aspergillus ficuum phytase with the arginine specific modifier 1,2-cyclohexanedione causes a rapid loss of activity. The inactivation can be partially reversed by 0.2 M hydroxylamine and exhibits pseudo-first order kinetics. The reaction order and second order rate constant of inactivation were 0.87 and 6.72 M-1 Min-1, respectively. Amino acid analysis of modified phytase indicates that about 7 arginine of the total 19 were modified. While the chymotryptic maps of treated and untreated phytase wer virtually identical, the tryptic maps had 4 peaks of altered mobility. An Arg containing tripeptide was identified in the phytase which is also present in other phosphohydrolases and may represent one of the labile Arg involved in the formation of the active site.
 ...
PMID:Cyclohexanedione modification of arginine at the active site of Aspergillus ficuum phytase. 164 14

Phytase (myo-inositol hexakisphosphate phosphohydrolase; EC 3.1.3.8 or 3.1.3.26) was purified from rat intestinal mucosa. The purified enzyme preparation exhibited two protein bands on SDS-polyacrylamide gel electrophoresis with estimated molecular masses of 70 kDa and 90 kDa. Rabbit antisera prepared against the 90K subunit cross-reacted with the 70K subunit on immunoblotting. The peptide maps of the 70K and 90K subunits were similar, and the N-terminal amino acid sequences of the two subunit proteins were almost identical. Treatments to remove sugar moieties from the proteins showed that the two subunit proteins had different oligosaccharide chains, although the difference in their molecular masses was not due to the difference in their oligosaccharide compositions. The purified enzyme also showed activity of alkaline phosphatase (orthophosphoric monoester phosphohydrolase; EC 3.1.3.1), but the properties of the two enzyme activities were different; the optimum pH for phytase activity was 7.5, while that for alkaline phosphatase was 10.4. Phytase activity did not necessarily require divalent cations, while Mg2+ was essential for alkaline phosphatase activity. Phenylalanine, a specific inhibitor of intestine-type alkaline phosphatase had no effect on the phytase activity.
 ...
PMID:Purification and characterization of phytase from rat intestinal mucosa. 165 10

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.
 ...
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.
 ...
PMID:The effect of food processing on phytate hydrolysis and availability of iron and zinc. 165 32

Oat products are increasingly used in human nutrition due to the rather high content of soluble fibre. Oat products, however, have a high content of phytate which may interfere with the absorption of non-haem iron. The iron balance situation is critical in several groups, especially in children, teenagers and women in their fertile years. It is therefore important to examine the effect of oat products on non-haem iron absorption in man. The present studies showed that oat bran and oat porridge markedly inhibited the absorption of non-haem iron. The inhibition can be explained by the high phytate content of oat products. This is partly due to a high resistance of oat phytate against exogenous phytase and partly to an inactivation of the endogenous phytase in oats caused by the usual heat treatment of oats which is made to prevent rancidity of oat lipids during storage. The inhibitory effect of oat products on iron absorption is sufficiently marked to be a serious consideration if such products are more regularly consumed.
 ...
PMID:Inhibitory effect of oat products on non-haem iron absorption in man. 208 7

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.
 ...
PMID:Phytase from Klebsiella Sp. No. PG-2: purification and properties. 216 21

Postweaning protein malnutrition imposed on normally weaned or neonatally undernourished rats fed a low-protein diet induced retardation of body and small intestinal growth. A sparing effect on intestinal growth as compared to body growth was observed during protein malnutrition. Postweaning protein malnutrition in normally weaned rats resulted in a significant elevation of specific activities of inositol triphosphatase and phytase in duodenum and jejunum without affecting the activity in ileum. On the other hand, protein malnutrition imposed on neonatally undernourished rats resulted in a significant decrease of enzyme activities in small intestinal segments. These results suggest altered activity of intestinal inositol phosphatase in postweaning protein malnutrition with the direction of effects dependent on the neonatal nutritional status.
 ...
PMID:Effects of postweaning protein malnutrition on intestinal inositol phosphatase activities in normally weaned and neonatally undernourished rats. 216 59


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>