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metabolism
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release of phosphate by stepwise hydrolysis of phosphomonoester bonds in phytate. Phytate is the major storage form of phosphate and inositol, predominantly occurring in cereal grains, legumes, and oilseeds
evolution
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dual-domain beta-propeller phytases have succeeded evolutionarily because they can increase the amount of available phosphate by interacting together
evolution
the two phytases, an acidic histidine acid phosphatase, PhyH49, and an alkaline beta-propeller phytase, PhyB49, share low identities with known phytases, 61% at most
evolution
enzyme rStPhy belongs to the histidine acid phosphatase (HAP) phytases family
evolution
molecular modeling of PHY US42 indicates that this phytase belongs to the group of beta-propeller phytases that are usually calcium-dependent
evolution
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on the basis of the site at which phytate dephosphorization begins, phytases can be grouped into three classes: 3-phytases (EC 3.1.3.8), 6-phytases (EC 3.1.3.26), and 5-phytases (EC 3.1.3.72). The fungal phytases are included in the 3-phytases class, in which the dephosphorization starts at the third phosphate group. Because of their catalytic mechanism, the fungal phytases belong to the histidine acid phosphatase class
evolution
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the consensus sequence RHGXRXP and HD, typical of histidine acid phosphatases
evolution
the enzyme AgpP from Pantoea sp. 3.5.1. belongs to the Agp subfamily of histidine acid phosphatases with 3-phytase specificity. The amino acid sequence of the Pantoea sp. 3.5.1 AgpP phytase harbors an N-terminal RHNLRAP motif (where the italicized residues are variable) and a C-terminal HD motif, which are the structural hallmarks of the highly conserved catalytic core of histidine acid phosphatases (HAPs) [consensus sequence RH(G/N)XRXP/HD, where the slash separates the N- and C-terminal sequences]
evolution
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the enzyme belongs to the histidine acid phosphatase (HAP) family
evolution
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the enzyme belongs to the histidine acid phosphatase (HAP) family
evolution
KM873028
the enzyme belongs to the histidine acid phosphatase (HAP) family phytases present in insect-cultivated fungus gardens
evolution
the enzyme belongs to the histidine acid phosphatase (HAP) family, it possesses typical conserved motifs of HAP phytases: RHGERFP in AA125-131 and HD in AA394-395
evolution
the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP
evolution
the enzyme belongs to the histidine acid phosphatases
evolution
the enzyme sequence contains histidine acid phosphatase (HAP) motifs (RHGXRXP and HD), indicating the classification of this enzyme in the HAP phytase family
evolution
the phytase of the yeast Pichia anomala is a histidine acid phosphatase based on signature sequences and catalytic amino acids
evolution
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the enzyme belongs to the histidine acid phosphatases
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evolution
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the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP
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evolution
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the enzyme belongs to the histidine acid phosphatases
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evolution
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dual-domain beta-propeller phytases have succeeded evolutionarily because they can increase the amount of available phosphate by interacting together
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evolution
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the enzyme sequence contains histidine acid phosphatase (HAP) motifs (RHGXRXP and HD), indicating the classification of this enzyme in the HAP phytase family
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evolution
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the consensus sequence RHGXRXP and HD, typical of histidine acid phosphatases
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evolution
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the enzyme belongs to the histidine acid phosphatases
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evolution
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the enzyme belongs to the histidine acid phosphatases
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evolution
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the enzyme belongs to the histidine acid phosphatase (HAP) family
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evolution
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the two phytases, an acidic histidine acid phosphatase, PhyH49, and an alkaline beta-propeller phytase, PhyB49, share low identities with known phytases, 61% at most
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evolution
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the enzyme belongs to the histidine acid phosphatase (HAP) family, it possesses typical conserved motifs of HAP phytases: RHGERFP in AA125-131 and HD in AA394-395
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evolution
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the enzyme belongs to the histidine acid phosphatases
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evolution
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molecular modeling of PHY US42 indicates that this phytase belongs to the group of beta-propeller phytases that are usually calcium-dependent
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malfunction
activity and catalytic efficiency at low temperature are reduced in a recombinant protein from which the N-terminal domain is removed
malfunction
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activity and catalytic efficiency at low temperature are reduced in a recombinant protein from which the N-terminal domain is removed
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physiological function
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gene disruption mutants show a lower phytase and phophatase activity in seedlings and germinating pollen and lower pollen germination rate
physiological function
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cysteine phytase is the major phytate-degrading enzyme in the anaerobic ruminal environment
physiological function
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cysteine phytase is the major phytate-degrading enzyme in the anaerobic ruminal environment
physiological function
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importance of enzyme domain PhyH-DI in phytate degradation
physiological function
phytase activity in grain is essential to make phosphate available to cell metabolism, and in food and feed
physiological function
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phytate is an antinutritional factor that influences the bioavailability of essential minerals by forming complexes with them and converting them into insoluble salts. beta-Propeller phytase hydrolyzes insoluble Ca2+-phytate salts and completely abrogates the ability of phytate to chelate metal ions, stoichiometry, affinity, and thermodynamics of these interactions by isothermal titration calorimetry, overview. Ins(2,4,6)P3 is unable to bind Ca2+ or any other cation tested, including Co2+, Cu2+, Fe3+, Mg2+, Mn2+, Sr2+, and Zn2+
physiological function
transgenic expression in Brassica napus with a signal peptide sequence. Transgenic lines exhibit significantly higher exuded phytase activity when compared to wild-type controls. Transgenic Brassica napus has significantly improved phosphate uptake and plant biomass. Seed yields of transgenic increase by 20.9% when compared to wild-type. When phytate is used as the sole phosphate source, phosphate accumulation in seeds increases by 20.6. Phytase activities in transgenic canola seeds range from 1,138 to 1,605 U/kg seeds, while no phytase activity is detected in wild-type seeds. Phytic acid content in seeds is significantly lower than in wild-type
physiological function
AgpP phytase and its unusual regulation by metal ions highlight the remarkable diversity of phosphorus metabolism regulation in soil bacteria
physiological function
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phytase degrades phytates to release phosphate and other essential ions. It is widespread in nature, found in plants, animals and microorganisms. The use of phytase reduces phosphate excretion in monogastric animals and avoids supplementation of feeds with inorganic phosphate. Animal stomach is the main functional site for phytase-mediated dephosphorylation in the gastrointestinal tract
physiological function
phytase hydrolyzes phytate (myo-inositol 1,2,3,4,5,6-hexakisphosphate, IP6) and its salts present in cereals and legumes to release inorganic phosphate. It contributes to the removal of phytate, an anti-nutritional factor in feed, and thereby increases the bioavailability of phosphate, minerals, protein, and starch
physiological function
phytase hydrolyzes phytic acid (myo-inositol-hexakisphosphate), which is the major storage form of phosphorus in cereals, legumes, and oilseed crops
physiological function
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phytases (myo-inositol hexakisphosphate phosphohydrolases) are enzymes that compose a special class of phosphatases. Phytases catalyze the hydrolysis of the phosphomonoester bonds of phytate (salts of myo-inositol 1,2,3,4,5,6-hexakis dihydrogen phosphate), releasing lower forms of myo-inositol and inorganic phosphates. Regulation of enzymatic synthesis by phosphate is coordinated by the PHO pathwa
physiological function
phytases are a special class of phosphatases that sequentially hydrolyse phytic acid to less-phosphorylated myo-inositol which release inorganic phosphates. This class of enzyme is widely distributed in nature and has been isolated from several sources, including plants, animals, and microorganisms
physiological function
phytate present in cereals lowers bioavailability of minerals. The reduction of phytic acid content can lead to improvement in mineral availability, and thus mitigate antinutrient effects of phytic acid
physiological function
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the enzyme promotes plant growth showing a significant effect, with an increase of 10% of root and 25% of shoot length, resulting in a 2.2fold increase in biomass
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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the phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface
physiological function
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phytase hydrolyzes phytic acid (myo-inositol-hexakisphosphate), which is the major storage form of phosphorus in cereals, legumes, and oilseed crops
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physiological function
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phytase hydrolyzes phytate (myo-inositol 1,2,3,4,5,6-hexakisphosphate, IP6) and its salts present in cereals and legumes to release inorganic phosphate. It contributes to the removal of phytate, an anti-nutritional factor in feed, and thereby increases the bioavailability of phosphate, minerals, protein, and starch
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physiological function
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importance of enzyme domain PhyH-DI in phytate degradation
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physiological function
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phytases are a special class of phosphatases that sequentially hydrolyse phytic acid to less-phosphorylated myo-inositol which release inorganic phosphates. This class of enzyme is widely distributed in nature and has been isolated from several sources, including plants, animals, and microorganisms
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physiological function
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the enzyme promotes plant growth showing a significant effect, with an increase of 10% of root and 25% of shoot length, resulting in a 2.2fold increase in biomass
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additional information
catalytic efficiency of the HAP phytase is determined by key residue Arg79 located in close proximity to the active site
additional information
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catalytic efficiency of the HAP phytase is determined by key residue Arg79 located in close proximity to the active site
additional information
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conformational dynamics of the active site loop, structure analysis, overview. Molecular dynamic studies indicate that the movement in the active site is mainly confined by the active site loop resulted in wider opening of the loop in absence of phytate, possible role of loop residues as prerequisite for highly active phytases
additional information
phytase ASR1 is a member of the histidine-acid-phosphatase family, that shares two conserved active-site motifs, RHGXRXP and HD, and hydrolyzes metal-free phytate with pH optima in the acidic range. Histidine-acid-phosphatases share a common two-step mechanism for catalysis. The reaction starts with a nucleophilic attack on the phosphoester bond by a conserved histidine in the long active-site motif. The histidine side chain from the conserved HD motif protonates the leaving group. The second step comprises hydrolysis of the resulting covalent phospho-histidine intermediate. Comparison of substrate binding of Klebsiella sp. ASR1 PhyK with Escherichia coli AppA phytase
additional information
replacements of G56E, L65F, Q144H, and L151S improve the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures
additional information
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replacements of G56E, L65F, Q144H, and L151S improve the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures
additional information
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the enzyme adsorbs to and interacts with pure minerals and oxisol clays also releasing orthophosphate from InsP6-saturated minerals, overview
additional information
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the enzyme can also act as a vanadate haloperoxidase, EC 1.11.1.10
additional information
the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP- , near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen
additional information
the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP- , near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen
additional information
the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP-, near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen
additional information
the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP-, near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen
additional information
the enzyme is resistant to shrimp digestive enzymes and porcine trypsin
additional information
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the enzyme is resistant to shrimp digestive enzymes and porcine trypsin
additional information
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the enzyme shows strong resistance toward pepsin and trypsin
additional information
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the tandemly repeated domains of a beta-propeller phytase act synergistically to increase catalytic efficiency. The intact domain is responsible for phytate hydrolysis. Enzyme domain PhyH-DI also hydrolyzes the phytate intermediate D-Ins(1,4,5,6)P4, and acts synergistically, causing a 1.2-2.5fold increase in phosphate release, with domain PhyH-DII, other beta-propeller phytases, PhyP and 168PhyA, and a histidine acid phosphatase. Fusion of PhyH-DI with PhyP or 168PhyA significantly enhanced their catalytic efficiencies
additional information
two types of phytases in Serratia sp. TN49
additional information
two types of phytases in Serratia sp. TN49
additional information
amino acid sequence analysis and homology structure modeling
additional information
Bacillus phytases exhibit their desirable activity profile at neutral pH. They have higher thermal stability, and strict substrate specificity for the calcium-phytate complex than that of acidic phytase. Molecular model of phytase constructed by homology modeling method using the structure with PDB ID 2POO as template, overview
additional information
catalytic center structures of wild-type YkAPPA and its mutants E230G and L162G, catalytic sites are catalytic sites R44, R48, D115, R119, H333, and D334, overview
additional information
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catalytic center structures of wild-type YkAPPA and its mutants E230G and L162G, catalytic sites are catalytic sites R44, R48, D115, R119, H333, and D334, overview
additional information
homology modeling and computational analysis of Penicillium oxalicum strain KCTC6440 PhyA, comparison to the structure of phytase PhyA from Penicillium oxalicum strain PJ3
additional information
homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
additional information
molecular docking of wild-type and mutant enzymes, homology modelling using the enzyme structure of the phytase from Bacillus amyloliquefaciens (PDB ID 2POO) as the template, overview. Residues D24, S51 and K70 have a relatively large influence on the catalytic activity probably because they are adjacent to the active site cleft. The enzyme is composed of six beta-sheets and possesses six calcium binding sites. The 25 amino acid residues except V60, involved in calcium binding, are highly conserved
additional information
requirement of a thiol group for the activity
additional information
KM873028
structural model of rPhyXT52 is deduced by homology modeling using the Yersinia kristensenii phytase (PDB ID 4ARV) structure as template, overview
additional information
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structure of the active site pocket of phytase protein, homology modeling of HAP-phytase, overview
additional information
the catalytically important amino acids Arg74, His75, Arg78, His368, and Asp369 are identified by docking and site-directed mutagenesis, molecular surface analysis, and three-dimensional modeling
additional information
the deduced amino acid sequence of phyC harbors a putative -35 and -10 sequences, a ribosomal binding site, and a transcription terminator
additional information
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the deduced amino acid sequence of phyC harbors a putative -35 and -10 sequences, a ribosomal binding site, and a transcription terminator
additional information
the enzyme has an active-site motif RHGXRXP and a remote C-teminal His-Asp (HD motif) which takes part in the catalysis
additional information
the enzyme structure possesses a phosphate-binding pocket with residues R54, H55, R58, I61, R146, W272, H315, E316, and V317 involved in phosphate ligand binding
additional information
the N-terminal domain is required for the low temperature activity and high catalytic efficiency of PSphy
additional information
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the N-terminal domain is required for the low temperature activity and high catalytic efficiency of PSphy
additional information
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the phytase seems to possess improved adaptability to the low pH condition caused by the gastric acid in livestock and poultry stomachs
additional information
three-dimensional model of recombinant PPHY by homology modeling using the crystal structure of phytase chain A from Debaryomyces castellii (PDB ID 2gfiA) as template, inhibitor docking of sodium phytate, vanadate, and tartrate
additional information
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
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three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
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threedimensional structural model, overview
additional information
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homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
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additional information
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homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
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additional information
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molecular docking of wild-type and mutant enzymes, homology modelling using the enzyme structure of the phytase from Bacillus amyloliquefaciens (PDB ID 2POO) as the template, overview. Residues D24, S51 and K70 have a relatively large influence on the catalytic activity probably because they are adjacent to the active site cleft. The enzyme is composed of six beta-sheets and possesses six calcium binding sites. The 25 amino acid residues except V60, involved in calcium binding, are highly conserved
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additional information
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the enzyme shows strong resistance toward pepsin and trypsin
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additional information
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Bacillus phytases exhibit their desirable activity profile at neutral pH. They have higher thermal stability, and strict substrate specificity for the calcium-phytate complex than that of acidic phytase. Molecular model of phytase constructed by homology modeling method using the structure with PDB ID 2POO as template, overview
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additional information
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the tandemly repeated domains of a beta-propeller phytase act synergistically to increase catalytic efficiency. The intact domain is responsible for phytate hydrolysis. Enzyme domain PhyH-DI also hydrolyzes the phytate intermediate D-Ins(1,4,5,6)P4, and acts synergistically, causing a 1.2-2.5fold increase in phosphate release, with domain PhyH-DII, other beta-propeller phytases, PhyP and 168PhyA, and a histidine acid phosphatase. Fusion of PhyH-DI with PhyP or 168PhyA significantly enhanced their catalytic efficiencies
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additional information
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homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
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additional information
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homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
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additional information
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the enzyme is resistant to shrimp digestive enzymes and porcine trypsin
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additional information
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the N-terminal domain is required for the low temperature activity and high catalytic efficiency of PSphy
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additional information
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homology modeling and computational analysis of Penicillium oxalicum strain KCTC6440 PhyA, comparison to the structure of phytase PhyA from Penicillium oxalicum strain PJ3
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additional information
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two types of phytases in Serratia sp. TN49
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additional information
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three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
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additional information
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homology structure modeling of Yersinia mollaretii phytase using the Yersinia kristensenii phytase apo-form structure (PDB ID 4ARV), Hafnia alvei phytase in complex with tartrate (PDB ID 4ARU), Hafnia alvei phytase in complex with myo-inositol hexakissulphate (PDB ID 4ARO), Hafnia alvei phytase apo-form (PDB ID 4ARS), and Escherichia coli phytase with bound phytate in the active site (PDB ID 1DKQ) as templates, location of active site loop
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additional information
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the deduced amino acid sequence of phyC harbors a putative -35 and -10 sequences, a ribosomal binding site, and a transcription terminator
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additional information
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amino acid sequence analysis and homology structure modeling
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