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Literature summary extracted from

  • Tomschy, A.; Brugger, R.; Lehmann, M.; Svendsen, A.; Vogel, K.; Kostrewa, D.; Lassen, S.F.; Burger, D.; Kronenberger, A.; van Loon, A.P.; Pasamontes, L.; Wyss, M.
    Engineering of phytase for improved activity at low pH (2002), Appl. Environ. Microbiol., 68, 1907-1913.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.1.3.8 agriculture since monogastric animals virtually lack phytase activity in their digestive tract, phytic acid phosphorus is metabolically unavailable to these animals. The problem can be circumvented by supplementation of the feed with a recombinantly produced phytase that has a pH activity profile ideally suited for maximal activity in the digestive tract of either pigs or poultry Aspergillus fumigatus
3.1.3.26 agriculture since monogastric animals virtually lack phytase activity in their digestive tract, phytic acid phosphorus is metabolically unavailable to these animals. The problem can be circumvented by supplementation of the feed with a recombinantly produced phytase that has a pH activity profile ideally suited for maximal activity in the digestive tract of either pigs or poultry Aspergillus fumigatus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.8 G277K mutation increases the activity of the enzyme at pH 2.8-3.4. Mutation decreases the relative activity at pH values of above 6.3 Aspergillus fumigatus
3.1.3.8 K68A mutation decreases the pH optimum with phytate as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity Aspergillus fumigatus
3.1.3.8 Q27L mutation increases the specific activity mainly around pH 6.5, while the increase is much smaller in the pH range 2 to 5, the pH that seems most relevant for maximal performance of the enzyme in animals. Decreasing the negative surface charge of the Aspergillus fumigatus Q27L phytase mutant by glycinamidylation of the surface carboxy groups (of Asp and Glu residues) lowers the pH-optimum by ca. 0.5 unit but also results in 70-75% inactivation of the enzyme Aspergillus fumigatus
3.1.3.8 S140Y/D141G mutation decreases the pH optimum with phytate as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity Aspergillus fumigatus
3.1.3.8 Y282H mutation increases the activity of the enzyme at pH 2.8-3.4. Mutation decreases the relative activity at pH values of above 6.3 Aspergillus fumigatus
3.1.3.26 G277K mutation increases the activity of the enzyme at pH 2.8-3.4. Mutation decreases the relative activity at pH values of above 6.3 Aspergillus fumigatus
3.1.3.26 K68A mutation decreases the pH optimum with phytate as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity Aspergillus fumigatus
3.1.3.26 Q27L mutation increases the specific activity mainly around pH 6.5, while the increase is much smaller in the pH range 2 to 5, the pH that seems most relevant for maximal performance of the enzyme in animals. Decreasing the negative surface charge of the Aspergillus fumigatus Q27L phytase mutant by glycinamidylation of the surface carboxy groups (of Asp and Glu residues) lowers the pH-optimum by ca. 0.5 unit but also results in 70-75% inactivation of the enzyme Aspergillus fumigatus
3.1.3.26 S140Y/D141G mutation decreases the pH optimum with phytate as substrate by 0.5 to 1.0 unit, with either no change or even a slight increase in maximum specific activity Aspergillus fumigatus
3.1.3.26 Y282H mutation increases the activity of the enzyme at pH 2.8-3.4. Mutation decreases the relative activity at pH values of above 6.3 Aspergillus fumigatus

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 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.
-
3.1.3.26 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.
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 3-phosphoglycerate + H2O
-
Aspergillus fumigatus glycerate + phosphate
-
?
3.1.3.8 4-nitrophenylphosphate + H2O
-
Aspergillus fumigatus 4-nitrophenol + phosphate
-
?
3.1.3.8 beta-glycerophosphate + H2O
-
Aspergillus fumigatus glycerol + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus fumigatus ? + phosphate
-
?
3.1.3.8 phenyl phosphate
-
Aspergillus fumigatus phenol + phosphate
-
?
3.1.3.8 phosphoenolpyruvate + H2O
-
Aspergillus fumigatus pyruvate + phosphate
-
?
3.1.3.26 3-phosphoglycerate + H2O
-
Aspergillus fumigatus glycerate + phosphate
-
?
3.1.3.26 4-nitrophenylphosphate + H2O
-
Aspergillus fumigatus 4-nitrophenol + phosphate
-
?
3.1.3.26 beta-glycerophosphate + H2O
-
Aspergillus fumigatus glycerol + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O
-
Aspergillus fumigatus ? + phosphate
-
?
3.1.3.26 phenyl phosphate
-
Aspergillus fumigatus phenol + phosphate
-
?
3.1.3.26 phosphoenolpyruvate + H2O
-
Aspergillus fumigatus pyruvate + phosphate
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 4.5
-
Q27T mutant enzyme, 4-nitrophenyl phosphate as substrate Aspergillus fumigatus
3.1.3.8 5
-
Y27T/K68A mutant enzyme, 4-nitrophenyl phosphate as substrate, mutant enzyme Q27T/K68A with phytate as substrate Aspergillus fumigatus
3.1.3.8 5.5
-
Y27T/K68A mutant enzyme, phytate as substrate, mutant enzyme Q27T with phytate as substrate Aspergillus fumigatus
3.1.3.8 6.5
-
Q27T mutant enzyme, phytate as substrate Aspergillus fumigatus
3.1.3.26 4.5
-
Q27T mutant enzyme, 4-nitrophenyl phosphate as substrate Aspergillus fumigatus
3.1.3.26 5
-
Y27T/K68A mutant enzyme, 4-nitrophenyl phosphate as substrate, mutant enzyme Q27T/K68A with phytate as substrate Aspergillus fumigatus
3.1.3.26 5.5
-
Y27T/K68A mutant enzyme, phytate as substrate, mutant enzyme Q27T with phytate as substrate Aspergillus fumigatus
3.1.3.26 6.5
-
Q27T mutant enzyme, phytate as substrate Aspergillus fumigatus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.8 3.5 5.5 pH 3.5: about 65% of maximal activity, pH 5.5: about 60% of maximal activity, Y27T/K68A mutant enzyme, 4-nitrophenyl phosphate as substrate Aspergillus fumigatus
3.1.3.8 3.5 5.5 pH 3.5: about 75% of maximal activity, pH 5.5: about 45% of maximal activity, Q27T mutant enzyme, 4-nitrophenyl phosphate as substrate Aspergillus fumigatus
3.1.3.8 4 7 pH 4.0: about 50% of maximal activity, pH 7.0: about 45% of maximal activity, Y27T/K68A mutant enzyme, phytate as substrate Aspergillus fumigatus
3.1.3.8 4 7.5 pH 4.0: about 45% of maximal activity, pH 7.5: about 45% of maximal activitry, Q27T mutant enzyme, phytate as substrate Aspergillus fumigatus
3.1.3.26 3.5 5.5 pH 3.5: about 65% of maximal activity, pH 5.5: about 60% of maximal activity, Y27T/K68A mutant enzyme, 4-nitrophenyl phosphate as substrate Aspergillus fumigatus
3.1.3.26 3.5 5.5 pH 3.5: about 75% of maximal activity, pH 5.5: about 45% of maximal activity, Q27T mutant enzyme, 4-nitrophenyl phosphate as substrate Aspergillus fumigatus
3.1.3.26 4 7 pH 4.0: about 50% of maximal activity, pH 7.0: about 45% of maximal activity, Y27T/K68A mutant enzyme, phytate as substrate Aspergillus fumigatus
3.1.3.26 4 7.5 pH 4.0: about 45% of maximal activity, pH 7.5: about 45% of maximal activitry, Q27T mutant enzyme, phytate as substrate Aspergillus fumigatus