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)

The genes encoding phytase (EC 3.1.3.8) and pH 2.5-optimum acid phosphatase (EC 3.1.3.2) have been cloned and sequenced from Aspergillus niger var. awamori. The translated nucleotide sequences yielded polypeptides of 467 and 479 amino acids (aa) for phytase and acid phosphatase, respectively. The genes were isolated using oligodeoxyribonucleotide probes based on the aa sequences of the purified proteins. Recombinant A. niger var. awamori strains carrying additional copies of the gene sequences demonstrated elevated enzyme activities.
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PMID:The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-optimum acid phosphatase (aph) from Aspergillus niger var. awamori. 822 94

Phytase (myo-inositol-hexakisphosphate phosphohydrolase, EC 3.1.3.8) has been purified from 5-7-day-old maize (Zea mays) seedlings, using a four-step purification procedure. The native protein has a molecular mass of about 76 kDa and is built up from two 38 kDa subunits. The pH and temperature optima of the purified enzyme were respectively 4.8 and 55 degrees C. The apparent Km for phytate was estimated to be 117 microM. Like other acidic phytases, the maize seedling enzyme exhibited a broad affinity for various phosphorylated substrates and especially for penta- and tri-phosphate esters of myo-inositol. The amino acid composition of the h.p.l.c.-purified protein indicated a high hydrophobicity (44% non-polar amino acids). Rabbit antibodies were produced in response to maize seedling phytase. Western-blot analyses clearly demonstrate that the increase of phytase activity observed during the first 7 days of germination corresponded to an accumulation of the protein in maize seedlings. Phytase accumulated essentially in the shoots (mesocotyl plus coleoptiles.
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PMID:Purification and characterization of a phytase (myo-inositol-hexakisphosphate phosphohydrolase) accumulated in maize (Zea mays) seedlings during germination. 824 Feb 38

Two experiments were conducted to evaluate the effect of dietary phytase and increasing levels of available phosphorus (P(av)) on the growth performance and phosphorus metabolism of broiler chicks. In both experiments, graded levels of P provided by dicalcium phosphate and of phytase were added to a low-P corn-soybean meal basal diet. In Experiment 1, diets providing .21, .29, .37, and .44% P(av) without phytase; .21% P(av) plus .05, .10, or .30% phytase; and .29% P(av) plus .10% phytase were each fed to four groups of seven chicks, 3 days of age. In Experiment 2, diets providing P(av) levels of .32, .38, and .44% and phytase levels of .5, 1.0, and 1.5% (250, 500, and 750 units/kg) in a factorial arrangement were each fed to four groups of eight chicks, 5 days of age. In Experiment 1, increasing dietary P(av), but not phytase, increased feed intake, weight gain, feed conversion, plasma inorganic P, tibia and toe ash, and tibia breaking strength (P < or = .05). Plasma inorganic P responded quadratically to increasing dietary phytase. In Experiment 2, feed intake and weight gain were increased by elevating the level of P(av), but not by phytase. Toe and tibia ash and plasma inorganic P were increased by dietary phytase and increasing levels of P(av) (P < or = .01). Tibia breaking strength was improved (P < or = .05) by dietary phytase but not by increasing levels of P(av). The P excretion was elevated (P < or = .01) by increasing levels of P(av) and was decreased by supplemental phytase (P < or = .05).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The effect of dietary phytase on growth performance and phosphorus utilization of broiler chicks. 826 99

Two experiments were conducted with weanling pigs to determine the effectiveness of a dietary supplement of Aspergillus niger phytase in improving the availability of phytate-P in corn-soybean meal diets without supplemental inorganic P. Experiment 1 consisted of two P and Ca balance trials and two feeding trials. Twelve pigs (8.18 +/- .44 kg BW) were housed individually in stainless steel metabolism cages. Six pigs received 750 phytase units (PU)/g of basal diet and the other six pigs received the basal diet without supplemental phytase as control. In Exp. 2, 96 pigs (8.81 +/- .75 kg BW) were allotted to 16 partially slotted floor pens and their basal diets were supplemented with either 0, 250, 500, or 750 PU/g for 4 wk. Individual pig weights and pen feed consumption were measured weekly. Blood samples were taken from all pigs at the end of each trial in Exp. 1 and from three pigs per pen weekly in Exp. 2 to measure serum (plasma) inorganic P (P) and Ca concentrations and alkaline phosphatase (AP) activities. The results of Exp. 1 indicated that dietary phytase increased P retention by 50% (P < .0001) and decreased fecal P excretion by 42% (P < .0001). Pigs that received dietary phytase had serum P and Ca concentrations and serum AP activities that were nearly normal, whereas control pigs had values indicative of a moderate P deficiency. Favorable effects of phytase disappeared when the phytase was removed from the diet.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Supplementing corn-soybean meal diets with microbial phytase linearly improves phytate phosphorus utilization by weanling pigs. 829 88

Two experiments were conducted with crossbred weanling pigs to determine the optimal dietary supplement of Aspergillus niger phytase activity to a low-P, corn-soybean meal basal diet (BD). In Exp. 1, 50 pigs (7.61 +/- .56 kg BW) received the BD supplemented with 750, 1,050, 1,250, or 1,350 phytase units (PU)/g, or .21% P as mono-dibasic calcium phosphate (MDCaP) for 4 wk. In Exp. 2, 12 pigs (6.39 +/- .74 kg BW) were individually housed in metabolism cages and received BD, BD plus the optimal phytase activity (1,200 PU/g), or BD plus .21% P as MDCaP for 2 wk. In Exp. 1, additions of phytase > 1,050 PU/g of BD did not improve ADG, ADFI, gain/feed, or plasma AP activity. Quadratic relationships between dietary phytase activity and these measures were found and their stationary points were at approximately 1,200 PU/g of BD. Estimated maximum responses of these measures in pigs fed phytase were > or = 90% compared with MDCaP. Pigs fed 1,250 PU/g of BD maintained normal plasma P and Ca concentrations. In Exp. 2, pigs that received 1,200 PU/g of BD utilized dietary P more effectively (P < .05) than pigs fed the BD or the BD plus MDCaP. Although they consumed 44% less P per day, these pigs retained only 7% less P than pigs that received MDCaP. One thousand units of phytase activity supported retention of 1.1 mg of P from the BD, and this level of phytase supplementation was equivalent in effect to .91 mg of P from MDCaP.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Supplementing corn-soybean meal diets with microbial phytase maximizes phytate phosphorus utilization by weanling pigs. 829 89

In pursuit of the physiological role of inositol 1,3,4,5-tetrakisphosphate 3-phosphatase, which also attacks inositol pentakisphosphate and inositol hexakisphosphate with much higher affinity (Nogimori, K., Hughes, P.J., Glennon, M.C., Hodgson, M.E., Putney, J.W., Jr., and Shears, S.B. (1991) J. Biol. Chem. 266, 16499-16506), we have studied the subcellular distribution of the enzyme in liver. Initially, we had to overcome the problem that potent endogenous inhibitor(s) compromise the detection of this enzyme in vitro (Hodgson, M.E., and Shears, S.B. (1990) Biochem. J. 267, 831-834). We partially purified these inhibitor(s) by anion-exchange chromatography and gel filtration; inhibitory activity co-eluted with standard inositol hexakisphosphate and was depleted by treatment with phytase. Thus, subcellular fractions were pretreated with phytase before assay of 3-phosphatase activity. Our experiments revealed that the hepatic 3-phosphatase was nearly exclusively restricted to the endoplasmic reticulum, and there was little or no activity in either the cytosol, plasma membranes, mitochondria, or nuclei. Detergent treatment of microsomes indicated that there was 93 +/- 2% latency to mannose-6-phosphatase, an intraorganelle enzyme activity (Vanstapel, F., Pua, K., and Blanckaert, N. (1986) Eur. J. Biochem. 156, 73-77). Similar latencies were found for the hydrolysis of inositol 1,3,4,5-tetrakisphosphate (95 +/- 1%), inositol 1,3,4,5,6-pentakisphosphate (94 +/- 1%), and inositol hexakisphosphate (93 +/- 2%). Treatment of microsomes with either sodium carbonate or phosphatidylcholine-specific phospholipase C, to release luminal contents, led to solubilization of approximately 90% of 3-phosphatase activity. Thus, hepatic 3-phosphatase has a highly restricted access to inositol polyphosphates in vivo that needs to be accounted for in the determination of the physiological role of this enzyme.
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PMID:Hepatic Ins(1,3,4,5)P4 3-phosphatase is compartmentalized inside endoplasmic reticulum. 838 1

Mobilization of Ca2+ from microsomal/vacuolar fractions was detected when InsP6-phytase was added after a definite time of hydrolysis which coincides with the time (20-30 min) of optimal production of Ins(2,4,5)P3 bound to phytase. The in vitro constituted Ins(1,4,5)P3 or Ins(2,4,5)P3-phytase complex is also effective in releasing Ca2+. InsP3-phytase complex releases 45% more microsomal Ca2+ than that released by free InsP3 under identical conditions. Other inositol-phytase complexes are ineffective. Furthermore InsP3-phytase complex is recognised by putative receptor associated with microsomal fraction suggesting that the myoinositol tris-phosphate-phytase complex can act as an elicitor in Ca2+ mobilization in plant systems where phytate and phytase occur.
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PMID:Myoinositol tris-phosphate-phytase complex as an elicitor in calcium mobilization in plants. 838 39

These studies were conducted to determine if supplementation of a corn-soybean meal diet with 1,25-dihydroxycholecalciferol [1,25-(OH)2D3] would increase the utilization of natural phytate phosphorus by broiler chickens. Two experiments were conducted to evaluate the effect of dietary 1,25-(OH)2D3 in the presence and absence of supplemental phytase and at several dietary levels of inorganic phosphorus supplementation. The criteria measured in these studies were weight gain, gain:feed ratio, bone ash, rickets due to phosphorus deficiency, plasma calcium and phosphorus and retention of calcium, phosphorus and phytate phosphorus. In the first experiment, the types and amounts of fecal inositol phosphates were determined by HPLC, and the total fecal phytate was determined by the classic FeCl3 precipitation technique. In the first experiment, the addition of 1,25-(OH)2D3 to the diet in the presence of dietary phytase resulted in greater 9-d weight and bone ash and lower incidence of rickets; the retention of total fecal phytate and phytate phosphorus was greater than in controls. The second experiment was a complete 2 x 2 x 2 factorial design [phosphorus levels x phytase x 1,25-(OH)2D3]. The addition of 1,25-(OH)2D3 alone to the diet resulted in greater 9-d weight and bone ash, lower incidence of rickets, and greater retention of total calcium and phosphorus and phytate phosphorus. The highest retention of phytate phosphorus (79.4%) was obtained when both phytase and 1,25-(OH)2D3 were present in the diet. The possible mode of action and importance of these results in many areas of nutrition and environmental science are discussed.
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PMID:Dietary 1,25-dihydroxycholecalciferol supplementation increases natural phytate phosphorus utilization in chickens. 838 10

The primary structure of Aspergillus ficuum phytase was deduced from overlaps in peptide sequences. The unglycosylated enzyme is a 441 residue protein with a molecular mass of 48.5-KDa, as calculated from the total covalent structure. The estimated pl of the protein is about 4.76. Of the 19 Asn residues, 9 were found to be glycosylated. The phytase consists of 37% non-polar, 42% polar, 11.5% acidic, and 9.5% basic amino acids. The putative active site of the enzyme containing the sequence RHG is located at the N-terminal region of the molecule and shows homology to the active site of both microbial and mammalian acid phosphatases, and phosphoglycerate mutase.
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PMID:Aspergillus ficuum phytase: complete primary structure elucidation by chemical sequencing. 838 89

Phytase catalyzes the hydrolysis of phytate (myo-inositol hexakisphosphate) to myo-inositol and inorganic phosphate. A gene (phyA) of Aspergillus niger NRRL3135 coding for extracellular, glycosylated phytase was isolated using degenerate oligodeoxyribonucleotides deduced from phytase amino acid (aa) sequences. Nucleotide (nt) sequence analysis of the cloned region revealed the presence of an open reading frame coding for 467 aa and interrupted once by an intron of 102 bp in the 5' part of the gene. The start codon is followed by a sequence coding for a putative signal peptide. Expression of phyA is controlled at the level of mRNA accumulation in response to inorganic phosphate levels. After cell growth in low-phosphate medium, a transcript of about 1.8 kb was visualized. Transcription of phyA initiates at at least seven start points within a region located 45-25 nt upstream from the start codon. In transformants of A. niger, expression of multiple copies of phyA resulted in up to more than tenfold higher phytase levels than in the wild-type strain.
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PMID:Cloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger. 838 47


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