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3.1.3.8: 3-phytase

This is an abbreviated version!
For detailed information about 3-phytase, go to the full flat file.

Word Map on EC 3.1.3.8

Reaction

myo-inositol hexakisphosphate
+
H2O
=
1D-myo-inositol 1,2,4,5,6-pentakisphosphate
 +
phosphate

Synonyms

1-phytase, 168phyA, 3'-phytase, 3-phytase, 3-phytase A, 3-phytase B, acid phytase, acidic histidine acid phosphatase, Afp, agpP, AgpP phytase, alkaline beta-propeller phytase, alkaline phytase, Allzyme, Allzyme phytase, AppA, appA phytase, AppA2, AppA2 phytase, AppAS, appA_Gw, Aspergillus niger N25 phytase, ASR1, AtPAP15, beta-propeller phytase, BIFPSEUDO_03792, Blon_0263, BPP, cell-bound phytase, cysteine phytase, dual-domain BPP, experimental phytase SP 1002, HAP, HAP phytase, HAP-phytase, histidine acid phosphatase, histidine acid phosphatase phytase, histidine acid phytase, HvPAPhy_a, LlALP1, LlALP2, microbial phytase, MiPhyA, MOK1 phytase, More, MYCTH_2306203, myo-inositol 1,2,3,4,5,6-hexakisphosphate phosphohydrolase, myo-inositol hexakiphosphate phosphohydrolase, myo-inositol hexakis phosphohydrolase, myo-inositol hexakisphosphate 3-phosphohydrolase, myo-inositol hexakisphosphate hydrolase, myo-inositol hexakisphosphate phosphohydrolase, myo-inositol hexaphosphate phosphohydrolase, myo-inositol-hexakisphosphate phosphohydrolase, MYO-inositol-hexaphosphate 3-phosphohydrolase, myo-inositol-hexaphosphate phosphohydrolase, myo-inositolhexakisphosphate phosphohydrolase, Natuphos, neutral phytase, NLP_0515, PAP, PAP type I, PAPhy, PAPhys, PAPhy_a1.1, pGF11 phytase, pGP209 phytase, pH 2.5 optimum acid phosphatase, Phy, PHY US42, PHY US573, phy168, PhyA, PhyA phytase, PhyA115, PhyA2, PhyB, PhyB49, PhyC, PhyCm, PhyH, PhyH49, PhyK, phyL, PhyP, phyS, phytase, phytase A, phytase C, phytate 1-phosphatase, Phytate 3-phosphatase, phytate 6-phosphatase, PhyTX52, PJ3 phytase, PPHY, protease-resistant phytase, PSphy, purple acid phosphatase, RMPhy1, RO1, RO2, Ronozyme P, RPHY1, ruminant microbial phytase, St-Phy, StPhy, tfphyA, YeAPPA, YkAPPA, YmPh

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.8 3-phytase

Crystallization

Crystallization on EC 3.1.3.8 - 3-phytase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at resolution higher than 1.7 A, native enzyme and enzyme in complex with P=4 at pH 5.5 and at pH 7.5. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
hanging-drop vapour diffusion method at 22°C, crystal structure determined at 1.5 A resolution. The crystal structure clearly shows a partially occupied phosphohistidine residue, the transient reaction intermediate of the enzyme, at the active site
-
deglycosylated PhyA free or in complex with inhibitor myo-inositol-1,2,3,4,5,6-hexakis sulfate, vapour-diffusion hanging drop technique, reservoirs contain 1 ml of PEG 3350 at 15-30% w/v, and ammonium nitrate a t0.1-0.4 M, siliconized coverslips are used to suspend a drop containing 0.002 ml of phytase at 13 mg/ml protein concetration and 0.002 ml of reservoir solution over the reservoir, X-ray diffraction structure determination and analysis at 2.2-2.4 A resolution
-
molecular dynamics simulation and comparison between wild-type and thermostable mutant A35E/P42S/Q168R/T248R show that among secondary structure elements, loops have the most impact on the thermal stability of Aspergillus niger phytase. In addition, the location rather than the number of hydrogen bonds has an important contribution to thermostability. Salt bridges may have stabilizing or destabilizing effect on the enzyme and influence its thermostability accordingly
the crystal structure of the enzyme in complex with phosphate reveals that two phosphates and four calcium ions are tightly bound at the active site
-
to 2.3 A resolution. The structure can be divided into two parts: a large alpha/beta-domain with a six-stranded beta-sheet and a small alpha-domain. The four active sites of the tetramer are solvent-exposed and are accessible to substrate
analysis of crystal structure of the phytate complex of Escherichia coli phytase at pH 6.6 with phytate bound via its 3-phosphate to the active site with Hg2+ as intermolecular bridge, X-ray diffraction structure at 2.28 A resolution, analysis of active site loops, overview
-
apo-enzyme, to 1.9 A resolution, and in complex with substrate analogue myo-inositiol hexakissulfate, to 1.59 A resolution. The substrate analogue is coordinated by residues Arg18, His19, Arg22, Thr25, Lys26, His128, Thr219, His306, Asp307 and a number of water molecules. The Nepsilon2 atom of the catalytic nucleophile, His19, lies 3.2 A from S6 of the analogue and is in-line with the S-O bond from the inositol ring. The OD1 atom of Asp307, the proton donor, forms an H-bond with the oxygen at position 6 of the inositol ring
native PhyK and inactive mutant H25A phytase PhyK, the latter with bound sulfate ions, hanging-drop vapor diffusion at 18°C, 5-6 weeks, for the wild-type enzyme: mixing of 6 mg/ml protein in 20 mM sodium acetate (pH 5.0), 50 mm NaCl with an equal volume of 4.0 M sodium formate, for mutant H25A: mixing of 0.0015 ml of protein in 25 mM sodium acetate pH 5.0, 60 mM NaCl and 1 mM tris-(2-carboxyethyl)phosphine with 0.0015 ml of 12% PEG 8000, 0.08 M (NH4)2SO4, 0.1 M sodium acetate and 1.5 mM phytate, 1 week, 22°C, X-ray diffraction structure determination and analysis at 1.7 A resolution, single-wavelength anomalous-diffraction phasing
recombinant phytase contains the active site RHGXRXP and HD sequence motifs, a large alpha/beta-domain and a small alpha-domain
-
phytase in complex with persulfated phytate, determination of three different structures from three crystal forms: phytase alone, phytase bound with myo-inositol hexasulfate at a location slightly away from the active site and phytase bound with myo-inositol hexosulfate at the active site. The crystal structures reveal a phytase fold of the dual-specificity phosphatase type. The active site is locatewd near a conserved Cys241-containing P loop. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
molecular modeling of structure
-
in complex with phosphate, to 1.9 A resolution