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Literature summary for 3.1.3.8 extracted from

  • Wyss, M.; Pasamontes, L.; Remy, R.; Kohler, J.; Kusznir, E.; Gadient, M.; Muller, F.; van Loon, A.P.G.M.
    Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase, and A. niger PH 2.5 acid phosphatase (1998), Appl. Environ. Microbiol., 64, 4446-4451.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.8

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus
-
-
-
Aspergillus niger
-
-
-
Aspergillus niger T213
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
after heat denaturation at temperatures up to 90°C the enzyme refolds completely into a nativelike, fully active conformation. Capacity of the enzyme to refold properly after heat denaturation may favorably affect its pelleting stability Aspergillus fumigatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
myo-inositol hexakisphosphate + H2O
-
 Aspergillus niger 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O
-
 Aspergillus fumigatus 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O
-
 Aspergillus niger T213 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 20 min, about 15% loss of activity Aspergillus niger
55
-
 irreversible conformational change with loss in enzymatic activity of 70-80% Aspergillus niger
70
-
 about 75% loss of activity Aspergillus niger