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Literature summary for 3.4.23.18 extracted from

  • Takeuchi, M.; Ueno, Y.; Ichishima, E.
    Fluorogenic substrate of Aspergillus aspartic proteinase (1988), Agric. Biol. Chem., 52, 1279-1280.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
1,2-epoxy-3-(4-nitrophenoxy)propane not Aspergillus phoenicis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Aspergillus phoenicis
-
-
soluble
-
Aspergillus phoenicis
-
-

Organism

Organism UniProt Comment Textmining
Aspergillus phoenicis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
from Molsin, a commercial crude enzyme extract Aspergillus phoenicis

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation Molsin, commercial crude enzyme Aspergillus phoenicis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tert-Butoxycarbonyl-Ile-Glu-Gly-Arg 4-methylcoumarin 7-amide + H2O
-
Aspergillus phoenicis tert-Butoxycarbonyl-Ile-Glu-Gly + Arg 4-methylcoumarin 7-amide
-
?
tert-Butoxycarbonyl-Leu-Ser-Thr-Arg 4-methylcoumarin 7-amide + H2O
-
Aspergillus phoenicis tert-Butoxycarbonyl-Leu-Ser-Thr + Arg 4-methylcoumarin 7-amide
-
?
Trypsinogen + H2O
-
Aspergillus phoenicis ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Aspergillus phoenicis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5
-
tert-butoxycarbonyl-Leu-Ser-Thr-Arg 4-methylcoumarin 7-amide Aspergillus phoenicis