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Literature summary extracted from

  • Abe, Y.; Shirane, K.; Yokosawa, H.; Matsushita, H.; Mitta, M.; Kato, I.; Ishii, S.
    Asparaginyl endopeptidase of jack bean seeds. Purification, characterization, and high utility in protein sequence analysis (1993), J. Biol. Chem., 268, 3525-3529.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.4.22.34 2-mercaptoethanol stabilizes Canavalia ensiformis
3.4.22.34 Brij 35, 0.005-0.05%, stabilizes Canavalia ensiformis
3.4.22.34 DTT stabilizes Canavalia ensiformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.34 cystatin EW Canavalia ensiformis
3.4.22.34 diisopropyl fluorophosphate
-
 Canavalia ensiformis
3.4.22.34 leupeptin
-
 Canavalia ensiformis
3.4.22.34 p-chloromercuribenzene sulfonic acid
-
 Canavalia ensiformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.22.34 0.023
-
 Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 pH 5.0 Canavalia ensiformis
3.4.22.34 0.033
-
 Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 pH 5.9 Canavalia ensiformis

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.34 Canavalia ensiformis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.22.34
-
 Canavalia ensiformis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.34 seed mature Canavalia ensiformis
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.22.34 additional information
-
-
 Canavalia ensiformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.34 Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 + H2O
-
 Canavalia ensiformis Dinitrophenyl-Pro-Glu-Ala-Asn + NH4OH
-
 ?
3.4.22.34 additional information almost all the peptide bonds on the carboxyl side of Asn residues are susceptible to the enzyme. The exceptions are cases where the residue is at the NH2 terminus or the second position from the NH2 terminus of the substrates and where it is N-glycosylated Asn Canavalia ensiformis ?
-
 ?

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.22.34 7.5
-
 even with additives the enzyme is labile above Canavalia ensiformis