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Literature summary extracted from

  • Correia, I.; Aksu, S.; Adao, P.; Pessoa, J.C.; Sheldon, R.A.; Arends, I.W.
    Vanadate substituted phytase: Immobilization, structural characterization and performance for sulfoxidations (2008), J. Inorg. Biochem., 102, 318-329.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.3.8 biotechnology a cross-linked enzyme aggregate (CLEA) of 3-phytase is synthesised, which is incubated with vanadate and tested as a biocatalyst in the asymmetric sulfoxidation of thioanisole using hydrogen peroxide as the oxidant. The results show that the 3-phytase-CLEA demonstrates a similar efficiency (ca. 95% conversion) and asymmetric induction (ca. 60%) as the free enzyme. Moreover, the 3-phytase-CLEA can be reused at least three times without significant loss of activity Aspergillus niger
3.1.3.8 synthesis immobilization of enzyme via a cross-linked enzyme aggregate. The immobilized enzyme incubated with vanadate shows a similar efficiency and asymmetric induction as the free enzyme and can be used at least three times without significant loss of activity. In presence of organic solvents, the activtiy is still limited. Vanadate is coordinatecd to oxygen functions at two different binding sites, and the alpha-helical content decreases upon coordination of vanadate Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 vanadate 51V-NMR studies show that vanadate is incorporated in the active site. Enzyme shows higher affinity for vanadate at pH 5.0 than at pH 7.6. vanadium is covalently coordinated in the active site of the enzyme to an apical histidine and to oxygen donors. Two sites are available for coordination. Upon addition of H2O2 two peroxide-vanadate-phytase complexes are formed at pH 5.0 in the case of 3-phytase Aspergillus niger
3.1.3.26 vanadate 51V-NMR studies show that vanadate is incorporated in the active site of the enzyme. The 6-phytase, which is inactive in the sulfoxidation of thioanisole, show higher affinity for vanadate at pH 7.6 than at pH 5.0. Vanadium is covalently coordinated in the active site of the enzyme to an apical histidine and to oxygen donors. Two sites are available for coordination. Upon addition of H2O2 no peroxide-vanadate-phytase complexes are observed for the 6-phytase as seen for 3-phytase, in agreement with the inactivity of the 6-phytase for the oxidation of thioanisole Peniophora lycii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.8 vanadate incubation with vanadate to obtain a biocatalyst in the asymmetric sulfoxidation of thioanisole using hydrogen peroxide. Vanadate is coordinatecd to oxygen functions at two different binding sites, and the alpha-helical content decreases upon coordination of vanadate Aspergillus niger

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.1.3.8 1,2-dimethoxyethane presence of 30% increases the alpha-helical content of the phytase Aspergillus niger
3.1.3.8 acetonitrile presence decreases the alpha-helical content of the phytase Aspergillus niger
3.1.3.8 Ethanol presence of 30% increases the alpha-helical content of the phytase Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Aspergillus niger
-
-
-
3.1.3.8 Aspergillus niger
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 the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
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3.1.3.26 Peniophora lycii
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 the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.8 commercial preparation
-
 Aspergillus niger
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 4-nitrophenyl phosphate + H2O The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate Aspergillus niger 4-nitrophenol + phosphate
-
 ?
3.1.3.26 4-nitrophenyl phosphate + H2O The enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate Peniophora lycii 4-nitrophenol + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.8 3-phytase
-
 Aspergillus niger
3.1.3.26 6-phytase
-
 Peniophora lycii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.8 37
-
 assay at Aspergillus niger
3.1.3.26 37
-
 assay at Peniophora lycii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 4.5
-
 assay at Aspergillus niger
3.1.3.26 4.5
-
 assay at Peniophora lycii