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Literature summary for 3.1.3.8 extracted from

  • Tu, S.; Ma, L.; Rathinasabapathi, B.
    Characterization of phytase from three ferns with differing arsenic tolerance (2011), Plant Physiol. Biochem., 49, 146-150.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
arsenate
-
Nephrolepis exaltata
arsenate
-
Pteris ensiformis
arsenate the enzyme of Pteris vittata shows partial resistance to arsenate in contrast to enzymes from other ferns, e.g. Pteris ensiformis and Nephrolepis exaltata Pteris vittata
additional information no inhibition by arsenite Nephrolepis exaltata
additional information no inhibition by arsenite Pteris ensiformis
additional information no inhibition by arsenite Pteris vittata

Organism

Organism UniProt Comment Textmining
Nephrolepis exaltata
-
-
-
Pteris ensiformis
-
-
-
Pteris vittata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial purification of native enzyme by ammonium sulfate fractionation Nephrolepis exaltata
partial purification of native enzyme by ammonium sulfate fractionation Pteris vittata
partial purification of native enzyme by ammonium sulfate fractionation Pteris ensiformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
Nephrolepis exaltata
40
-
-
Pteris ensiformis
40 70
-
Pteris vittata

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
partially purified enzyme, 240 min, no loss of activity Pteris vittata

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
Nephrolepis exaltata
5
-
-
Pteris vittata
5
-
-
Pteris ensiformis

pH Range

pH Minimum pH Maximum Comment Organism
3.5 6 activity range, profile, overview Nephrolepis exaltata
3.5 6 activity range, profile, overview Pteris vittata
3.5 6 activity range, profile, overview Pteris ensiformis