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Literature summary extracted from

  • Zhang, W.; Lei, X.G.
    Cumulative improvements of thermostability and pH-activity profile of Aspergillus niger PhyA phytase by site-directed mutagenesis (2008), Appl. Microbiol. Biotechnol., 77, 1033-1040.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 expressed in Pichia pastoris strain X33 Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.8 A58E/P65S/Q191R/T271R retains 20% greater activity after being heated at 80°C for 10 min and has 7°C higher melting temperature than that of the wild type enzyme Aspergillus niger
3.1.3.8 A58E/P65S/Q191R/T271R/E228K pH-activity profile-improved mutant, optimum shift to pH 4.0, 64% increased specific activity at pH 3.5 Aspergillus niger
3.1.3.8 A58E/P65S/Q191R/T271R/E228K/K300E pH-activity profile-improved mutant, eliminates the activity dip at pH 3.5 shown in the wild type Aspergillus niger
3.1.3.8 A58E/P65S/Q191R/T271R/E228K/S149P improved thermostability Aspergillus niger
3.1.3.8 A58E/P65S/Q191R/T271R/E228K/S149P/F131L improved thermostability Aspergillus niger
3.1.3.8 A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R Although the substitution of K112R is supposed to create a new hydrogen bond with Y113 at a distance of 2.56 A, it does not offer extra benefit to thermostability Aspergillus niger
3.1.3.8 A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R 27% increased specific activity at pH 5.5, 100% increased specific activity at pH 3.5 Aspergillus niger
3.1.3.8 A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R/K300E 33% decreased activity at pH 5.5, wild type specific activity at pH 3.5 Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.8 0.0827
-
 myo-inositol hexakisphosphate mutant enzyme A58E/P65S/Q191R/T271R/E228K, at pH 4.0 Aspergillus niger
3.1.3.8 0.0864
-
 myo-inositol hexakisphosphate mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P, at pH 4.0 Aspergillus niger
3.1.3.8 0.0934
-
 myo-inositol hexakisphosphate mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R, at pH 4.0 Aspergillus niger
3.1.3.8 0.1076
-
 myo-inositol hexakisphosphate mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P, at pH 5.5 Aspergillus niger
3.1.3.8 0.1083
-
 myo-inositol hexakisphosphate mutant enzyme A58E/P65S/Q191R/T271R/E228K, at pH 5.5 Aspergillus niger
3.1.3.8 0.1224
-
 myo-inositol hexakisphosphate wild type enzyme, at pH 4.0 Aspergillus niger
3.1.3.8 0.1719
-
 myo-inositol hexakisphosphate wild type enzyme, at pH 5.5 Aspergillus niger
3.1.3.8 0.3847
-
 myo-inositol hexakisphosphate mutant enzyme A58E/P65S/Q191R/T271R/E228K/S149P/F131L/K112R/K195R, at pH 5.5 Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Aspergillus niger
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.8 DEAE cation exchange chromatography and Sephadex100 gel filtration Aspergillus niger

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 myo-inositol hexakisphosphate + H2O
-
 Aspergillus niger 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.8 PhyA
-
 Aspergillus niger