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Literature summary extracted from

  • Jermutus, L.; Tessier, M.; Pasamontes, L.; van Loon, A.P.; Lehmann, M.
    Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case (2001), J. Biotechnol., 85, 15-24.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 expression of mutant enzymes in Aspergillus niger Aspergillus terreus
3.1.3.26 expression of mutant enzymes in Aspergillus niger Aspergillus terreus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.8 A68S/A72E/A73E/S77N t1/2 at 49°C decreases from 53 min for the wild-type enzyme to 20 min for the mutant enzyme Aspergillus terreus
3.1.3.8 E41A/D42G t1/2 at 49°C increases from 53 min for the wild-type enzyme to 76 min for the mutant enzyme Aspergillus terreus
3.1.3.8 H61E t1/2 at 49°C increases from 53 min for the wild-type enzyme to 54 min for the mutant enzyme Aspergillus terreus
3.1.3.8 additional information replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme Aspergillus terreus
3.1.3.26 A68S/A72E/A73E/S77N t1/2 at 49°C decreases from 53 min for the wild-type enzyme to 20 min for the mutant enzyme Aspergillus terreus
3.1.3.26 E41A/D42G t1/2 at 49°C increases from 53 min for the wild-type enzyme to 76 min for the mutant enzyme Aspergillus terreus
3.1.3.26 H61E t1/2 at 49°C increases from 53 min for the wild-type enzyme to 54 min for the mutant enzyme Aspergillus terreus
3.1.3.26 additional information replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme Aspergillus terreus

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 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 or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
3.1.3.8 Aspergillus terreus
-
 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.
-
3.1.3.8 Aspergillus terreus 9A-1
-
 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 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 or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
3.1.3.26 Aspergillus terreus
-
 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 terreus 9A-1
-
 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.
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.8
-
 Aspergillus terreus
3.1.3.26
-
 Aspergillus terreus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.8 additional information
-
 replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme Aspergillus terreus
3.1.3.8 49
-
 t1/2: 138 min, wild-type enzyme Aspergillus niger
3.1.3.8 49
-
 t1/2: 53 min, wild-type enzyme Aspergillus terreus
3.1.3.26 additional information
-
 replacement of one alpha-helix on the surface of the Aspergillus terreus phytase by the corresponding stretch of Aspergillus niger phytase results in an enzyme with improved thermostability and unaltered enzymatic activity. The thermostability of this hybrid protein is very similar to that of Aspergillus niger phytase, although the fusion protein contains only a 31 amino acid stretch of the more stable parent enzyme Aspergillus terreus
3.1.3.26 49
-
 t1/2: 138 min, wild-type enzyme Aspergillus niger
3.1.3.26 49
-
 t1/2: 53 min, wild-type enzyme Aspergillus terreus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 4.5
-
-
 Aspergillus terreus
3.1.3.26 4.5
-
-
 Aspergillus terreus