Literature summary for 3.1.3.8 extracted from

Tomschy, A.; Tessier, M.; Wyss, M.; Brugger, R.; Broger, C.; Schnoebelen, L.; van Loon, A.P.; Pasamontes, L.
Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure (2000), Protein Sci., 9, 1304-1311.

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Protein Variants

Protein Variants	Comment	Organism
Q27A	1.1fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. The pH-activity profile resembles that of wild-type enzyme with slight increases below pH 4.0 and around pH 6.5	Aspergillus fumigatus
Q27G	2.3fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme.Increase in specific activity is almost constant over entire pH-range, pH 4-8	Aspergillus fumigatus
Q27I	3.1fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Remarkable increase in specific activity around pH 6.5, while having no or only a modest effect in the more acidic pH range. The shape of the pH-profile strongly resembles that of Aspergillus terreus - which also has Leu at postion 27	Aspergillus fumigatus
Q27L	3.4fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Remarkable increase in specific activity around pH 6.5, while having no or only a modest effect in the more acidic pH range. The shape of the pH-profile strongly resembles that of Aspergillus terreus - which also has Leu at postion 27	Aspergillus fumigatus
Q27N	1.7fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Increase in specific activity is almost constant over entire pH-range, pH 4-8	Aspergillus fumigatus
Q27P	1.7fold decrease in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Mutant enzyme has a pronounced tendency to aggregate and precipitate	Aspergillus fumigatus
Q27S	1.9fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme	Aspergillus fumigatus
Q27T	2.8fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme. Increase in specific activity over the entire pH-range, pH 4-8	Aspergillus fumigatus
Q27V	1.3fold increase in specific activity with phytate at pH 5.0 compared to wild-type enzyme	Aspergillus fumigatus

Organism

Organism	UniProt	Comment	Textmining
Aspergillus fumigatus	-	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 or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-phosphoglycerate + H2O	-	Aspergillus fumigatus	glycerate + phosphate	-	?
4-nitrophenylphosphate + H2O	-	Aspergillus fumigatus	4-nitrophenol + phosphate	-	?
ATP + H2O	-	Aspergillus fumigatus	?	-	?
beta-glycerophosphate + H2O	-	Aspergillus fumigatus	glycerol + phosphate	-	?
fructose 1,6-bisphosphate + H2O	-	Aspergillus fumigatus	?	-	?
myo-inositol hexakisphosphate + H2O	-	Aspergillus fumigatus	? + phosphate	-	?
phenyl phosphate	-	Aspergillus fumigatus	phenol + phosphate	-	?
phosphoenolpyruvate + H2O	-	Aspergillus fumigatus	pyruvate + phosphate	-	?

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Release 2023.1 (January 2023)