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Literature summary for 3.4.24.39 extracted from

  • Nakadai, T.; Nasuno, S.; Iguchi, N.
    Purification and properties of neutral proteinase II from Aspergillus oryzae (1973), Agric. Biol. Chem., 37, 2703-2708.
No PubMed abstract available
Search for more literature for 3.4.24.39

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Aspergillus oryzae
NaCl
-
 Aspergillus oryzae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19300
-
 Aspergillus oryzae, gel filtration Aspergillus oryzae

Organism

Organism UniProt Comment Textmining
Aspergillus oryzae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aspergillus oryzae

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
 Aspergillus oryzae
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Aspergillus oryzae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carboxybenzyl-Gly-Phe amide + H2O
-
 Aspergillus oryzae carboxybenzyl-Gly + Phe amide
-
 ?
casein + H2O
-
 Aspergillus oryzae hydrolyzed casein
-
 ?
additional information neither aminopeptidase nor carboxypeptidase activity Aspergillus oryzae ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
 10 min, less than 30% loss of activity Aspergillus oryzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 6 casein Aspergillus oryzae