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Literature summary for 3.1.3.8 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
Search for more literature for 3.1.3.8

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutant enzymes in Aspergillus niger Aspergillus terreus

Protein Variants

Protein Variants Comment Organism
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
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
H61E t1/2 at 49°C increases from 53 min for the wild-type enzyme to 54 min for the mutant enzyme Aspergillus terreus
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

Organism UniProt Comment Textmining
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.
-
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.
-
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)

Purification (Comment) Organism
-
 Aspergillus terreus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
49
-
 t1/2: 138 min, wild-type enzyme Aspergillus niger
49
-
 t1/2: 53 min, wild-type enzyme Aspergillus terreus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
-
 Aspergillus terreus