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Literature summary for 3.4.23.40 extracted from

  • Belozersky, M.A.; Sarbakanova, S.T.; Dunaevsky, Y.A.
    Aspartic proteinase from wheat seeds: isolation, properties and action on gliadin (1998), Planta, 177, 321-326.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
pepstatin A
-
Triticum aestivum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
seeds, gel filtration Triticum aestivum

Organism

Organism UniProt Comment Textmining
Triticum aestivum
-
wheat
-

Purification (Commentary)

Purification (Comment) Organism
-
Triticum aestivum

Source Tissue

Source Tissue Comment Organism Textmining
seed endosperm Triticum aestivum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.703
-
substrate gliadin Triticum aestivum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Albumin + H2O
-
Triticum aestivum ?
-
?
Gliadin + H2O gliadin subunits with MW of 66800-9500 and 31000 are processed to fragemnts of 57000-63000 and 24000-26600, respectively Triticum aestivum ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Triticum aestivum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
pH 4.0-8.0, at least 24 h stable Triticum aestivum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
substrate bovine serum albumin Triticum aestivum
4.5
-
substrate gliadin Triticum aestivum

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 8 at least 24 h at 37°C Triticum aestivum