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)

Phytases are a special class of phosphatase that catalyze the sequential hydrolysis of phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. Phytases are added to animal feedstuff to reduce phosphate pollution in the environment, since monogastric animals such as pigs, poultry, and fish are unable to metabolize phytate. Based on biochemical properties and amino acid sequence alignment, phytases can be categorized into two major classes, the histidine acid phytases and the alkaline phytases. The histidine acid phosphatase class shows broad substrate specificity and hydrolyzes metal-free phytate at the acidic pH range and produces myo-inositol monophosphate as the final product. In contrast, the alkaline phytase class exhibits strict substrate specificity for the calcium-phytate complex and produces myo-inositol trisphosphate as the final product. This review describes recent findings that present novel viewpoints concerning the molecular basis of phytase classification.
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PMID:Biochemical properties and substrate specificities of alkaline and histidine acid phytases. 1458 76

In order to understand the structural basis for the high thermostability of phytase from Aspergillus fumigatus, its crystal structure was determined at 1.5 A resolution. The overall fold resembles the structure of other phytase enzymes. Aspergillus niger phytase shares 66% sequence identity, however, it is much less heat-resistant. A superimposition of these two structures reveals some significant differences. In particular, substitutions with polar residues appear to remove repulsive ion pair interactions and instead form hydrogen bond interactions, which stabilize the enzyme; the formation of a C-terminal helical capping, induced by arginine residue substitutions also appears to be critical for the enzyme's ability to refold to its active form after denaturation at high temperature. The heat-resilient property of A.fumigatus phytase could be due to the improved stability of regions that are critical for the refolding of the protein; and a heat-resistant A.niger phytase may be achieved by mutating certain critical residues with the equivalent residues in A.fumigatus phytase. Six predicted N-glycosylation sites were observed to be glycosylated from the experimental electron density. Furthermore, the enzyme's catalytic residue His59 was found to be partly phosphorylated and thus showed a reaction intermediate, providing structural insight, which may help understand the catalytic mechanism of the acid phosphatase family. The trap of this catalytic intermediate confirms the two-step catalytic mechanism of the acid histidine phosphatase family.
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PMID:Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine. 1513 45

A gene, phoI, coding for a phosphatase from Enterobacter sp. 4 was cloned in Escherichia coli and sequenced. Analysis of the sequence revealed one open reading frame (ORF) that encodes a 269-amino acid protein with a calculated molecular mass of 29 kDa. PhoI belongs to family B acid phosphatase and exhibits 49.4% identity and 62.4% homology to the hel gene from Heamophilus influenzae, which encoded an outer membrane protein (P4). The optimum pH and temperature for phosphatase activity were pH 5.5 and 40 degrees C, respectively. Its specific activity on rho-nitrophenyl phosphatate was 70 U/mg at pH 5.5 and 40 degrees C. Enzyme activity was inhibited by Al3+, EDTA, and DTT, but fivefold activated by Cu2+ ion (350 U/mg). PhoI showed a strong synergistic effect when used with a purified E. coli phytase, AppA, to estimate combination effects.
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PMID:Cloning, sequencing and characterization of a novel phosphatase gene, phoI, from soil bacterium Enterobacter sp. 4. 1655 Apr 60

Phytic acid is the most abundant inositol phosphate in cells; it constitutes 1-5% of the dry weight of cereal grains and legumes. Phytases are the primary enzymes responsible for the hydrolysis of phytic acid and thus play important roles in inositol phosphate metabolism. A novel alkaline phytase in lily pollen (LlALP) was recently purified in our laboratory. In this paper, we describe the cloning and characterization of LlALP cDNA from lily pollen. Two isoforms of alkaline phytase cDNAs, LlAlp1 and LlAlp2, which are 1467 and 1533 bp long and encode proteins of 487 and 511 amino acids, respectively, were identified. The deduced amino acid sequences contains the signature heptapeptide of histidine phosphatases, -RHGXRXP-, but shares < 25% identity to fungal histidine acid phytases. Phylogenetic analysis reveals that LlALP is most closely related to multiple inositol polyphosphate phosphatase (MINPP) from humans (25%) and rats (23%). mRNA corresponding to LlAlp1 and LlAlp2 were expressed in leaves, stem, petals and pollen grains. The expression profiles of LlAlp isoforms in anthers indicated that mRNA corresponding to both isoforms were present at all stages of flower development. The expression of LlAlp2 cDNA in Escherichia coli revealed the accumulation of the active enzyme in inclusion bodies and confirmed that the cDNA encodes an alkaline phytase. In summary, plant alkaline phytase is a member of the histidine phosphatase family that includes MINPP and exhibits properties distinct from bacterial and fungal phytases.
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PMID:Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphosphate phosphatase (MINPP). 1686 Mar 50

Forty-one strains of lactic acid bacteria (LAB) isolated from Cornetto di Matera sourdoughs were screened for their enzymatic activities, to elucidate their possible roles during the fermentation process. Urease, peptidase, phytase, phosphatase and beta-glucosidase activities were measured spectrophotometrically using synthetic substrates. Proteolytic activities were examined in model doughs, using neutral and acidified sterile doughs as controls. All strains had low urease, glutamyl aminopeptidase and iminopeptidase activities, whereas differences within species were observed for the other enzymatic activities. Leuconostoc mesenteroides and Lactobacillus curvatus strains generally showed high aminopeptidase, X-prolyl dipeptidyl aminopeptidase, beta-glucosidase and phytase activities, while the enzymatic activities of Lactobacillus plantarum, Lactobacillus pentosus and Weissella cibaria varied between strains. In order to classify the strains on the basis of similar enzymatic profiles, a hierarchical cluster analysis was carried out. Several strains of L. plantarum, L. curvatus and Leuc. mesenteroides showed an interesting combination of proteolytic, peptidase, beta-glucosidase and phytase activities, suggesting their possible usefulness as a mixed starter culture in bread-making processes.
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PMID:Enzymatic activities of lactic acid bacteria isolated from Cornetto di Matera sourdoughs. 1717 29

Phytases are enzymes that catalyze liberation of inorganic phosphates from phytate, the major organic phosphorus in soil. Tobacco (Nicotiana tabacum) responds to phosphorus starvation with an increase in extracellular phytase activity. By a three-step purification scheme, a phosphatase with phytase activity was purified 486-fold from tobacco root exudates to a specific activity of 6,028 nkat mg(-1) and an overall yield of 3%. SDS-PAGE revealed a single polypeptide of 64 kDa, thus indicating apparent homogeneity of the final enzyme preparation. Gel filtration chromatography suggested that the enzyme was a ca. 56 kDa monomeric protein. De novo sequencing by tandem mass spectrometry resulted in a tryptic peptide sequence that shares high homology with several plant purple acid phosphatases. The identity of the enzyme was further confirmed by molybdate-inhibition assay and cDNA cloning. The purified enzyme exhibited pH and temperature optima at 5.0-5.5 and 45 degrees C, respectively, and were found to have high affinities for both p-nitrophenyl phosphate (pNPP; K(m)=13.9 microM) and phytate (K(m)=14.7 microM), but a higher kcat for pNPP (2,056 s(-1)) than phytate (908 s(-1)). Although a broad specificity of the enzyme was observed for a range of physiological substrates in soil, maximum activity was achieved using mononucleotides as substrates. We conclude that the phytase activity in tobacco root exudates is exhibited by a purple acid phosphatase and its catalytic properties are pertinent to its role in mobilizing organic P in soil.
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PMID:Phytase activity in tobacco (Nicotiana tabacum) root exudates is exhibited by a purple acid phosphatase. 1789 89

Lately, whole wheat products are highly recommended from their healthy properties. However, the presence of phytic acid (InsP(6)) could partly limit their benefits because it decreases the mineral bioavailability due to its chelating properties. The objective of this work was to select strains with high phytate-degrading activity from human feces, and evaluate their suitability for the bread making process. Twenty-three different bifidobacterial strains (13 from infants and 10 from adults) were isolated, belonging to the species Bifidobacterium longum, Bifidobacterium breve and Bifidobacterium catenulatum. The phosphatase and phytase activities of these strains were evaluated as well as their ability to degrade InsP(6) during growth. Then, the fermentative ability of the strain showing the highest phytate-degrading activity (B. longum. BIF307) was determined in whole wheat breadmaking. The use of the selected bifidobacterial strain as starter during whole wheat fermentation resulted in bread with similar technological quality than the control (in absence of bifidobacteria) and crumb with lower levels of inositol phosphates. Therefore, the used of the selected Bifidobacterium strain in whole wheat breadmaking process could provide potential nutritional benefits by decreasing the antinutrient content of the product.
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PMID:Selection of phytate-degrading human bifidobacteria and application in whole wheat dough fermentation. 1799 91

A protocol to assess the potential release of dissolved reactive phosphorus (DRP) by enzymatic hydrolysis of dissolved organic phosphorus (DOP) in waters (sediment porewater and sewage liquors in this study) under environmental conditions is presented. This protocol enables the quantification of different classes of DOP compounds using a variety of phosphatase enzymes, i.e., alkaline phosphatase, phosphodiesterase, and phytase. All experiments were carried out within the pH range of most natural waters, i.e., at neutral (pH 7) or slightly alkaline pH (pH 9). Tri-sodium citrate and sodium dodecyl sulfate (SDS) were used in the assays to prevent interferences due to adsorption processes in the presence of multivalent metallic cations and to minimize protein binding. Applying this protocol revealed that labile phosphate monoesters always represented the largest fraction of enzymatically hydrolyzed P in sewage liquors and sediment porewater. Total enzymatically hydrolyzable P (EHP) represented only 16% of the TDP in the sediment porewater but up to 43% in sewage liquors. Because most of the enzymes used in this study are likely to exist in aquatic ecosystems, the EHP fraction might represent a source of potentially bioavailable P of similar magnitude to DRP.
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PMID:A protocol to assess the enzymatic release of dissolved organic phosphorus species in waters under environmentally relevant conditions. 1804 29

The production of phytase and associated feed enzymes (phosphatase, xylanase, CMCase, alpha-amylase and beta-glucosidase) was determined in a thermotolerant fungus Mucor indicus MTCC 6333, isolated from composting soil. Solid-substrate culturing on wheat bran and optimizing other culture conditions (C and N sources, level of N, temperature, pH, culture age, inoculum level), increased the yield of phytase from 266 +/- 0.2 to 513 +/- 0.4 nkat/g substrate dry mass. The culture extract also contained 112, 194, 171, 396, and 333 nkat/g substrate of phosphatase, xylanase, CMCase, beta-glucosidase and alpha-amylase activities, respectively. Simple 2-step purification employing anion exchange and gel filtration chromatography resulted in 21.9-fold purified phytase. The optimum pH and temperature were pH 6.0 and 70 degrees C, respectively. The phytase was thermostable under acidic conditions, showing 82% residual activity after exposure to 60 degrees C at pH 3.0 and 5.0 for 2 h, and displayed broad substrate specificity. The Km was 200 nmol/L and v(lim) of 113 nmol/s per mg protein with dodecasodium phytate as substrate. In vitro feed trial with feed enzyme resulted in the release of 1.68 g inorganic P/kg of feed after 6 h of incubation at 37 degrees C.
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PMID:Production of feed enzymes (phytase and plant cell wall hydrolyzing enzymes) by Mucor indicus MTCC 6333: purification and characterization of phytase. 1829 46

The presence of phytase activity was demonstrated in 26 strains of rabbit cecal bacteria. In 25 strains a low phytase activity, 0.10-0.62 micromol phosphate released per min per mg protein, was found. High activity (2.61 micromol/min per mg protein) was found in the strain PP2 identified as Enterococcus hirae. Phytase activity was cell-associated, being higher in the cell extract than in the cell walls. Extracellular phytase activity and cell-associated phosphatase activity were not detected. Phytase activity was optimal around pH 5.0, which is below the physiological cecal pH range. The K (m) determined using the Lineweaver-Burk plot was 0.19 micromol/mL. Cations Fe(3+), Cu(2+) and Zn(2+) at 0.5 mmol/L decreased phytase activity in sonicated cells of E. hirae by 99.4, 90.7 and 96.5 %, respectively. In contrast, Mg(2+) increased activity by 11.0 %. Characteristics of E. hirae phytase (pH optimum, K (m), cation sensitivity) were similar to those of other bacterial phytases reported in the literature. Other bacteria with a high phytase activity may be present in the rabbit cecum but remain to be identified.
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PMID:Phytase activity in rabbit cecal bacteria. 1941 47


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