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Literature summary for 3.4.22.34 extracted from
- Asparaginyl endopeptidase of jack bean seeds. Purification, characterization, and high utility in protein sequence analysis (1993), J. Biol. Chem., 268, 3525-3529.
General Stability
| General Stability | Organism |
|---|---|
| 2-mercaptoethanol stabilizes | Canavalia ensiformis |
| Brij 35, 0.005-0.05%, stabilizes | Canavalia ensiformis |
| DTT stabilizes | Canavalia ensiformis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| cystatin | EW | Canavalia ensiformis | |
| diisopropyl fluorophosphate | - |
Canavalia ensiformis |  |
| leupeptin | - |
Canavalia ensiformis | |
| p-chloromercuribenzene sulfonic acid | - |
Canavalia ensiformis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.023 | - |
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 | pH 5.0 | Canavalia ensiformis | |
| 0.033 | - |
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 | pH 5.9 | Canavalia ensiformis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Canavalia ensiformis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Canavalia ensiformis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| seed | mature | Canavalia ensiformis | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Canavalia ensiformis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 + H2O | - |
Canavalia ensiformis | Dinitrophenyl-Pro-Glu-Ala-Asn + NH4OH | - |
? | |
| 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
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
even with additives the enzyme is labile above | Canavalia ensiformis |
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