Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Activities of ATPase, acid and alkaline pyrophosphatases and phytase in the germs and endosperms of rice seeds of varying germinative power were measured during their swelling and germination. Maximum ATPase activity was found in the cytoplasmic fraction. Activity of pyrophosphatase was higher in the germ and that of phytase in the endosperm. As the swelling and germination continued, the enzyme activity increased. Losses of germinating power during prolonged storage were accompanied by a decline in the activity of the enzymes which, however, never disappeared; the activity of pyrophosphatases was maintained by 55-70% and that of ATPase and phytase by 40-44%.
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PMID:[Change in the phosphatase activity in rice seeds of varying germination]. 22 79

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.
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PMID:Effects of postweaning protein malnutrition on intestinal inositol phosphatase activities in normally weaned and neonatally undernourished rats. 216 59

Undernutrition during the suckling period imposed by maternal protein deficiency during lactation resulted in elevated inositol triphosphatase activity (units per gram of wet tissue) in the ileum and lower phytase activity in the duodenum and jejunum. Activities of inositol triphosphatase in the duodenum and jejunum and phytase in ileum were unaffected. Postweaning nutritional rehabilitation resulted in elevated specific activities of both enzymes in all segments; however, activities of whole segments were similar to the corresponding control values. Elevation of inositol triphosphatase (ileum) and decline of phytase (duodenum and jejunum) activities due to undernutrition were reversed by the administration of hydrocortisone or thyroxine during undernutrition. These results suggest that maturation of activities of inositol triphosphatase in ileum (by hydrocortisone) and phytase in all segments (by both hydrocortisone and thyroxine) is under hormonal regulation, and the effects of neonatal undernutrition may be partly due to hormonal imbalances.
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PMID:Effects of neonatal undernutrition and subsequent nutritional rehabilitation or administration of thyroxine and hydrocortisone on the inositol phosphatase activities in rat intestine. 302 Feb 20

1. Three experiments were carried out to determine the phosphorus (P) requirements of laying hens aged 34 to 58 weeks (experiment 1), 59 to 70 weeks (experiment 2) and 22 to 50 weeks (experiment 3) given diets containing wheat, sorghum and soyabean meals as the main ingredients. Dietary total P (Pt) varied between 3.2 and 7.3 g/kg (experiment 1), 3.2 and 4.6 g/kg (experiment 2) and 3.0 and 6.6 g/kg (experiment 3). Hens were housed at either 18 degrees or 30 degrees C (experiments 1 and 2) and uncontrolled temperature (experiment 3), and in experiment 2 diets were fed without or with a phytase supplement of 500 units/g. 2. Dietary Pt had no significant effect on production measures in any experiment. Increases in dietary Pt adversely influenced egg shell quality although uterine calcium (Ca), ATPase and carbonic anhydrase activities were unaffected. 3. A 3-d-feeding trial in experiment 1 gave maximum Pt retentions of 228 mg/d at 18 degrees C and 204 mg/d at 30 degrees C. These were obtained with diets containing, respectively, 4.6 and 6.0 g Pt/kg. 4. Plasma inorganic P (Pi) increased consistently with increases in dietary Pt at all temperatures but plasma total Ca, and tibia Ca and P, were unaffected. 5. The inclusion of the phytase supplement in diets containing 3.2 and 4.6 g Pt/kg had an adverse effect on egg production at both temperatures in experiment 2. 6. A dietary Pt concentration of 3.2 g/kg, providing a calculated 1.2 g available P (Pav)/kg, with a dietary phytase activity of less than 200 units/kg, satisfied the P requirements of the hens used in these studies. However, the data from experiment 3 suggest that the Pt requirement of some flocks fed on wheat-based diets may be lower than 3.2 g/kg.
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PMID:Phosphorus requirements of laying hens fed on wheat-based diets. 765 2

Phosphatase activities associated with the intestinal brush border membrane (BBM) of the rat were examined histochemically in relation to the characteristic environment of the intestine, where luminal pH fluctuates drastically between alkaline and acid pH ranges. Special attention was given to intestinal alkaline phosphatase (IALP) and phytase on the BBM. Whole body fresh-frozen sections of young rats and their rapidly frozen and freeze-substituted small intestines, embedded in Technovit 7100, were processed for the histochemical demonstration of phosphatase activity at three different pH values (9.2, 7.3, and 5.2), representing the deviation of luminal pH in vivo. Either an azo-dye method or lead-salt method was employed using naphthol AS-MX phosphate and ATP as substrate, respectively. With the azo-dye method, intense phosphatase reactions were demonstrated along the BBM at all three pH ranges. Phosphatase reactions of the BBM at pH 9.2 and 7.3 were abolished by L(+)-phenylalanine, heat pre-treatment, and EDTA chelation although some reaction remained at pH 7.3 after the treatment with EDTA or L(+)-phenylalanine. Phosphatase reactions of the BBM at pH 5.2 were resistant to L(+)-phenylalanine, L(+)-tartrate, PCMB and EDTA chelation, implying that the characteristics of the enzyme responsible for phosphohydrolysis at acid pH values differed from those at higher pH values. The lead-salt method in which ATP was used as substrate revealed intense reactions--which were dependent on Mg++ and stimulated by Ca++ and resistant to L(+)phenylalanine--to be localized along the BBM at alkaline and neutral pH values, but not at acid pH values. In vitro experiments showed progressive hydrolysis of naphthol AS-MX phosphate by purified phytase at pH 5.2, in a dose-dependent manner, and suggested the possible involvement of phytase in the phosphatase reactions of the BBM at acid pH. These data indicate that the phosphatase reactions at alkaline and neutral pH values, associated with the BBM of the rat intestine, represent IALP and Mg++/ Ca++-ATPase, while those at acid pH appear to correspond to phytase activity, something which has not been demonstrated by histochemical methods despite the availability of extensive data based on biochemical analyses.
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PMID:Phosphatase activities of rat intestinal enterocytes and their relation to diverse luminal pH, with special references to the possible localization of phytase along the brush border membrane. 1183 8

The sequence in which a variety of enzymes and metabolites are affected by gibberellic acid after application of the hormone to aleurone layers of half seeds of barley (Hordeum vulgare var. Betzes) and half seeds of wheat (Triticum aestivum var. Gensee) was investigated. With barley aleurone layers the first hormonal effect observed was the increased secretion of soluble carbohydrate, some of which appears to be a glucan containing some beta-1,3 linkages. This was followed by increased oxygen consumption and increased secretion of ATPase, GTPase, phytase, phosphomonoesterase, phosphodiesterase, inorganic phosphate, carbohydrates other than amylase, peroxidase and amylase. Similar sequential effects were seen in wheat half seeds. Increased activity of alcohol dehydrogenase in barley seeds was elicited by the hormone but there was no effect on glucose-6-phosphate isomerase.
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PMID:A survey of the sequence of some effects of gibberellic Acid in the metabolism of cereal grains. 1665 95

The effect of dietary phytate and phytase on carbohydrase activity and hexose transport was investigated in broiler chickens. Diets containing phytate P (2.2 or 4.4 g/kg) with different phytase dose rates (0, 500, or 1,000 phytase units/kg) were fed to 504 female Cobb chicks for 3 wk. Diets containing high phytate concentrations depressed (P < 0.05) BW and G:F, whereas phytase supplementation improved (P < 0.05) the performance of birds. In the duodenum, phytate decreased (P < 0.05) the activities of disaccharidases, Na(+)K(+)-ATPase, and glucose concentrations by 5 to 11%, but phytase enhanced (P < 0.05) the concentrations of amylase, sucrase, maltase, Na(+)K(+)-ATPase, and glucose by 5 to 30%. In the jejunum, phytate decreased (P < 0.05) the concentrations of amylase, sucrase, Na(+)K(+)-ATPase, and glucose by 10 to 22%, and phytase alleviated the negative effect of phytate on the above variables. Ingestion of diets containing phytate also decreased (P < 0.05) serum amylase activity and glucose concentration, and phytase enhanced (P < 0.05) serum concentrations of amylase, sucrase, maltase, Na(+)K(+)-ATPase, and glucose. There were also interactions (P < 0.05) between phytate and phytase on the concentrations of serum amylase, duodenal amylase, sucrase, and jejunal glucose. Enzymatic analysis at a molecular level showed that neither phytate nor phytase influenced the mRNA expression of sucrase-isomaltase in the small intestine. Also, the investigation into the sodium glucose cotransporter gene may challenge the mechanism by which phytate interferes with glucose utilization, as partly indicated by bird performance, and transmembrane transport because diets containing increased phytate upregulated (P < 0.05) the mRNA expression of the sodium glucose cotransporter gene in duodenum and did not influence it in the jejunum. These results indicate that phytate can impair endogenous carbohydrase activity and digestive competence, and phytase can ameliorate these effects for chickens.
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PMID:Effect of diet containing phytate and phytase on the activity and messenger ribonucleic acid expression of carbohydrase and transporter in chickens. 1870 94

Protein-phytate interactions are fundamental to the detrimental impact of phytate on protein/amino acid availability. The inclusion of exogenous phytase in pig and poultry diets degrades phytate to more innocuous esters and attenuates these negative influences. The objective of the present review is to reappraise the underlying mechanisms of these interactions and reassess their implications in pig and poultry nutrition. Protein digestion appears to be impeded by phytate in the following manner. Binary protein-phytate complexes are formed at pH levels less than the isoelectric point of proteins and complexed proteins are refractory to pepsin digestion. Once the protein isoelectric points are exceeded binary complexes dissociate; however, the isoelectric point of proteins in cereal grains may be sufficiently high to permit these complexes to persist in the small intestine. Ternary protein-phytate complexes are formed at pH levels above the isoelectric point of proteins where a cationic bridge links the protein and phytate moieties. The molecular weights of protein and polypeptides in small-intestinal digesta may be sufficient to allow phytate to bind nutritionally important amounts of protein in ternary complexes. Thus binary and ternary complexes may impede protein digestion and amino acid absorption in the small intestine. Alternatively, phytate may interact with protein indirectly. Myo-inositol hexaphosphate possesses six phosphate anionic moieties (HPO(4)(2-)) that have strong kosmotropic effects and can stabilise proteins by interacting with the surrounding water medium. Phytate increases mucin secretions into the gut, which increases endogenous amino acid flows as the protein component of mucin remains largely undigested. Phytate promotes the transition of Na(+) into the small-intestinal lumen and this suggests that phytate may interfere with glucose and amino acid absorption by compromising Na(+)-dependent transport systems and the activity of the Na pump (Na(+)-K(+)-ATPase). Starch digestion may be depressed by phytate interacting with proteins that are closely associated with starch in the endosperm of cereal grains. While elucidation is required, the impacts of dietary phytate and exogenous phytase on the site, rate and synchrony of glucose and amino acid intestinal uptakes may be of importance to efficient protein deposition. Somewhat paradoxically, the responses to phytase in the majority of amino acid digestibility assays in pigs and poultry are equivocal. A brief consideration of the probable reasons for these inconclusive outcomes is included in this reappraisal.
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PMID:Protein-phytate interactions in pig and poultry nutrition: a reappraisal. 2230 81

Oligotropha carboxidovorans is characterized by the aerobic chemolithoautotrophic utilization of CO. CO oxidation by CO dehydrogenase proceeds at a unique bimetallic [CuSMoO2] cluster which matures posttranslationally while integrated into the completely folded apoenzyme. Kanamycin insertional mutants in coxE, coxF and coxG were characterized with respect to growth, expression of CO dehydrogenase, and the type of metal center present. These data along with sequence information were taken to delineate a model of metal cluster assembly. Biosynthesis starts with the MgATP-dependent, reductive sulfuration of [Mo(VI)O3] to [Mo(V)O2SH] which entails the AAA+-ATPase chaperone CoxD. Then Mo(V) is reoxidized and Cu(1+)-ion is integrated. Copper is supplied by the soluble CoxF protein which forms a complex with the membrane-bound von Willebrand protein CoxE through RGD-integrin interactions and enables the reduction of CoxF-bound Cu(2+), employing electrons from respiration. Copper appears as Cu(2+)-phytate, is mobilized through the phytase activity of CoxF and then transferred to the CoxF putative copper-binding site. The coxG gene does not participate in the maturation of the bimetallic cluster. Mutants in coxG retained the ability to utilize CO, although at a lower growth rate. They contained a regular CO dehydrogenase with a functional catalytic site. The presence of a pleckstrin homology (PH) domain on CoxG and the observed growth rates suggest a role of the PH domain in recruiting CO dehydrogenase to the cytoplasmic membrane enabling electron transfer from the enzyme to the respiratory chain. CoxD, CoxE and CoxF combine motifs of a DEAD-box RNA helicase which would explain their mutual translation.
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PMID:Insights into the posttranslational assembly of the Mo-, S- and Cu-containing cluster in the active site of CO dehydrogenase of Oligotropha carboxidovorans. 2537 94

This study was designed to investigate the effect of dietary phytate and phytase on proteolytic digestion and growth signalling in the gastrointestinal tract of broilers. Diets containing phytate phosphorus (2.2 or 4.4 g/kg) with phytase dose rates of 0, 500, or 1,000 FTU/kg were fed to 504 female Cobb chicks for three weeks. Diets containing high phytate reduced the activity of pepsin and trypsin, whereas the inclusion of microbial phytase increased the activity of pepsin, H(+)K(+)-ATPase, trypsin and alanyl aminopeptidase. In the intestine, phytate upregulated the mRNA expression of somatostatin, and down-regulated the mRNA expressions of ghrelin and target of rapamycin (TOR). Phytase down regulated the somatostatin gene, and upregulated the genes of ghrelin, TOR, p70 S6 kinase (S6K) and methionyl aminopeptidase. Significant interactions between phytate and phytase on the mRNA expressions of ghrelin, somatostatin and S6K in the jejunum were detected. The results suggest that dietary phytate and phytase can influence the gastrointestinal endocrine and exocrine systems, as well as the peripherally regulatory network of growth in broilers.
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PMID:Effect of dietary phytate and phytase on proteolytic digestion and growth regulation of broilers. 2696 99


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