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Literature summary for 3.4.21.25 extracted from

  • Kaneda, M.; Ohmine, H.; Yonezawa, H.; Tominaga, N.
    Amino acid sequence around the reactive serine of cucumisin from melon fruit (1984), J. Biochem., 95, 825-829.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
diisopropyl fluorophosphate synthesis of denatured diisopropyl phosphorylcucumisin derivatives, which are hydrolyzed by chymotrypsin, to get peptides for amino acid sequence analysis around the reactive serine of the active site Cucumis melo

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Protein + H2O Cucumis melo
-
?
-
?

Organism

Organism UniProt Comment Textmining
Cucumis melo
-
L. var Prince
-

Source Tissue

Source Tissue Comment Organism Textmining
fruit
-
Cucumis melo
-

Storage Stability

Storage Stability Organism
lyophilization causes a loss of activity of more than 10% Cucumis melo
very stable in a frozen solution, no loss of activity after one year Cucumis melo

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
Cucumis melo ?
-
?
Protein + H2O
-
Cucumis melo ?
-
?
protein + H2O
-
Cucumis melo hydrolyzed protein
-
?