Phytase (myo-inositol-hexakisphosphate phosphohydrolase), extracellular enzyme that hydrolyzes myo-inositol hexakisphosphate (phytate) to myo-inositol and inorganic phosphate
about
P688
Overexpression of phyA and appA genes improves soil organic phosphorus utilisation and seed phytase activity in Brassica napusShifting the pH profile of Aspergillus niger PhyA phytase to match the stomach pH enhances its effectiveness as an animal feed additiveThe structure of Aspergillus niger phytase PhyA in complex with a phytate mimeticA simple and accurate two-step long DNA sequences synthesis strategy to improve heterologous gene expression in pichiaDigital gene expression analysis of mature seeds of transgenic maize overexpressing Aspergillus niger phyA2 and its non-transgenic counterpart.Identification and cloning of a second phytase gene (phyB) from Aspergillus niger (ficuum).The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila.Absorption studies show that phytase from Aspergillus niger significantly increases iron and zinc bioavailability from phytate-rich foods.Molecular characterization and expression of a phytase gene from the thermophilic fungus Thermomyces lanuginosus.Expression of an Aspergillus niger phytase gene (phyA) in Saccharomyces cerevisiaePhytase.Overexpression and functional characterization of an Aspergillus niger phytase in the fat body of transgenic silkworm, Bombyx mori.Adopting selected hydrogen bonding and ionic interactions from Aspergillus fumigatus phytase structure improves the thermostability of Aspergillus niger PhyA phytaseCloning, characterization and overexpression of the phytase-encoding gene (phyA) of Aspergillus niger.[Expression of phytase gene phyA in Yarrowia lipolytica po1h].Extracellular secretion of Aspergillus phytase from Arabidopsis roots enables plants to obtain phosphorus from phytate.Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0.PhyA gene product of Aspergillus ficuum and Peniophora lycii produces dissimilar phytases.Fungal phyA gene expressed in potato leaves produces active and stable phytase.Cloning and expression of fungal phytases in genetically modified strains of Aspergillus awamori.Isolation, characterization, and molecular cloning of the cDNA encoding a novel phytase from Aspergillus niger 113 and high expression in Pichia pastoris.Monitoring of unfolding and refolding in fungal phytase (phyA) by dynamic light scattering.Site-directed mutagenesis of disulfide bridges in Aspergillus niger NRRL 3135 phytase (PhyA), their expression in Pichia pastoris and catalytic characterization.Impact of assay conditions on activity estimate and kinetics comparison of Aspergillus niger PhyA and Escherichia coli AppA2 phytases.Vanadate inhibition of fungal PhyA and bacterial AppA2 histidine acid phosphatases.Site-directed mutagenesis improves the thermostability and catalytic efficiency of Aspergillus niger N25 phytase mutated by I44E and T252R.Effects of combining three fungal phytases with a bacterial phytase on plasma phosphorus status of weanling pigs fed a corn-soy diet.Degradation of phytates in distillers' grains and corn gluten feed by Aspergillus niger phytase.Role of glycosylation in the functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris.Expression of a fungal phytase gene in Nicotiana tabacum improves phosphorus nutrition of plants grown in amended soils.Cumulative improvements of thermostability and pH-activity profile of Aspergillus niger PhyA phytase by site-directed mutagenesis.Improving phytase enzyme activity in a recombinant phyA mutant phytase from Aspergillus niger N25 by error-prone PCR.Screening, cloning and overexpression of Aspergillus niger phytase (phyA) in Pichia pastoris with favourable characteristics.[Cloning and sequence analysis of the phytase phyA gene of Aspergillus niger N25][Cloning of a phyA gene and its over expression in E. coli].High level expression of a recombinant acid phytase gene in Pichia pastoris.Different sensitivity of recombinant Aspergillus niger phytase (r-PhyA) and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro[Improving thermostability of Aspergillus niger phytase by elongation mutation]Gene cloning and soluble expression of Aspergillus niger phytase in E. coli cytosol via chaperone co-expression[Overexpression of artificial synthetic gene of Aspergillus niger NRRL3135 phytase in Pichia pastoris]
P921
Q21089795-F9126F51-6C1D-4C65-A861-9DDAE702870BQ24549345-0DB8C9F0-6644-440A-BD63-BA7E50F863BBQ27662187-81B7B824-8D66-4ACF-97C6-C9C9135AA442Q28483394-90CC7434-CD7D-4612-9F12-DA650E2BA976Q34803015-008F4B84-4D48-4947-A428-60FC3493D8BDQ36722279-45F2B4CD-DA7E-480B-B511-F97C8B8CE6BAQ36845603-DF0FD1D5-D349-4306-9328-55A7674EA484Q38139457-D875B69B-DB22-42AD-813C-EBB15C7B1BF3Q38331817-FCB5EF68-9A61-4597-837E-022E3801BBDEQ39481536-1816A3B0-E46F-4D74-B06D-D1735FC80A40Q40957312-F8B4C5D4-31AC-459E-9D10-69D0C8EB5C6DQ42004030-4EB399AF-8190-415C-9A9F-0DEF7784C5E6Q42089684-CD610DA4-8CC7-439D-9478-2763E7183EE9Q42616282-BBA5E542-0752-4C54-95DC-E7D546647D3AQ42947088-CA7FCC50-1A83-44BE-BEF5-9761E5AFBE0CQ43586188-D8911701-B424-4839-9C89-45049DD145C4Q44164031-F6023036-4A43-47CC-A36A-8D3B83867423Q44378362-ECAF372C-0C45-40C0-B921-512A903C07B7Q44476776-E4FE84D0-E4EF-41E7-A777-0761F06F679CQ44598888-DBCF912D-B057-4720-ACA6-6A8A819C8A1AQ45094427-06D612A3-C461-46D1-BF05-513FA40FF512Q45225629-C814E5B3-9A8D-4A52-9993-5E9F55601FFFQ45339816-11F4C5E3-42C5-4B93-A589-32813758D751Q45967444-4C76586C-7A8F-4998-ADCF-319F29AB576BQ46152558-B4E9B694-2B6C-4178-AA10-FDA28A0B0D1BQ46177240-71F09D64-DD9F-42B4-BF78-183307165545Q46317576-FFFCC43F-C704-4735-95AB-54CA3E358506Q46348221-B3B1F90E-63CF-4956-8CD1-91E83562FFE0Q46560916-992402FF-BD17-4033-944F-468E806399F6Q46671786-E24FD1E4-D74E-43DF-9481-CB17EE0D8829Q46692451-7CDEEE1F-9C6D-463E-B38C-B067D959FE41Q46817910-E9860BA0-6074-4A76-908E-27B01974CE2EQ46933759-93DCCB36-985A-4699-BEAE-AEF07D0BB26CQ48261787-65DDCE47-9F3C-4554-BD41-73D11414715FQ54445867-3060F675-29F9-4EE4-B539-8A711D970BCCQ54684571-12BD9FF0-B81A-4721-9811-E10B1EE37238Q61522135-36C59FDC-7D9B-4F5D-A296-83AE8469AB64Q61522141-0935578C-B8B2-4D5F-B5CF-C3509582F3D2Q61522144-E6759A79-AB44-44AC-B0C3-83AF044D8879Q61522148-61B97731-A5E2-4506-893D-00857266560A
P921
Phytase (myo-inositol-hexakisphosphate phosphohydrolase), extracellular enzyme that hydrolyzes myo-inositol hexakisphosphate (phytate) to myo-inositol and inorganic phosphate
description
protein
@id
proteïne in An04g03460-T
@nl
protèin
@ace
name
An04g03460-T
@nl
Phytase (myo-inositol-hexakisp ...... ositol and inorganic phosphate
@en
type
label
An04g03460-T
@nl
Phytase (myo-inositol-hexakisp ...... ositol and inorganic phosphate
@en
prefLabel
An04g03460-T
@nl
Phytase (myo-inositol-hexakisp ...... ositol and inorganic phosphate
@en
P279
P31
P3382
An04g03460-T