Literature summary for 3.1.3.8 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.

Search for more literature for 3.1.3.8

Application

Application	Comment	Organism
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
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

Inhibitors	Comment	Organism	Structure
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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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

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

Organism

Organism	UniProt	Comment	Textmining
Aspergillus niger	-	-	-
Aspergillus niger	-	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	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
commercial preparation	-	Aspergillus niger	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?

Synonyms

Synonyms	Comment	Organism
3-phytase	-	Aspergillus niger

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Aspergillus niger

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.5	-	assay at	Aspergillus niger

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Release 2023.1 (January 2023)