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 |
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 |
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. | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
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 | - |
? |
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 |
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 |