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Literature summary extracted from

  • Dando, P.M.; Fortunato, M.; Smith, L.; Knight, C.G.; McKendrick, J.E.; Barrett, A.J.
    Pig kidney legumain: an asparaginyl endopeptidase with restricted (1999), Biochem. J., 339, 743-749.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.34 additional information glycosylation of asparaginyl residues totally prevents cleavage by the enzyme, no binding to human alpha2-macroglobulin Sus scrofa
3.4.22.34 rat alpha1-macroglobulin
-
 Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.22.34 lysosome
-
 Sus scrofa 5764
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.34 protein + H2O Sus scrofa
-
 peptides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.34 Sus scrofa
-
 purified enzyme
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.34 kidney cortex Sus scrofa
-

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 7
-
 purified enzyme Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.34 AGTHNGQIGA + H2O the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived, low activity Sus scrofa AGTHN + GQIGA
-
 ?
3.4.22.34 AHIDNEEDIA + H2O low activity, the peptide sequence is also cleaved in tetanus toxoid C fragment of which it is derived Sus scrofa AHIDN + EEDIA
-
 ?
3.4.22.34 AHIDNESDIA + H2O low activity Sus scrofa AHIDN + ESDIA
-
 ?
3.4.22.34 ALKGNNLIWA + H2O the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived Sus scrofa ALKGN + NLIWA
-
 ?
3.4.22.34 AQLKNITDYA + H2O the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived Sus scrofa AQLKN + ITDYA
-
 ?
3.4.22.34 AREDNNITLA + H2O low activity, the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived Sus scrofa AREDN + NITLA
-
 ?
3.4.22.34 ARLYNGLKFA + H2O the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived Sus scrofa ARLYN + GLKFA
-
 ?
3.4.22.34 ASGFNSSVIA + H2O the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived Sus scrofa ASGFN + SSVIA
-
 ?
3.4.22.34 ATITNDRLSA + H2O the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived Sus scrofa ATITN + DLRSA
-
 ?
3.4.22.34 AYGTNEYSIA + H2O the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived Sus scrofa AYGTN + EYSIA
-
 ?
3.4.22.34 benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
-
 Sus scrofa benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
 ?
3.4.22.34 benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
-
 Sus scrofa benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
 ?
3.4.22.34 benzyloxycarbonyl-Gly-Ala-Asn-4-methylcoumarin-7-amide + H2O
-
 Sus scrofa benzyloxycarbonyl-Gly-Ala-Asn + 7-amino-4-methylcoumarin
-
 ?
3.4.22.34 benzyloxycarbonyl-Leu-Ala-Asn-4-methylcoumarin-7-amide + H2O
-
 Sus scrofa benzyloxycarbonyl-Leu-Ala-Asn + 7-amino-4-methylcoumarin
-
 ?
3.4.22.34 benzyloxycarbonyl-Phe-Ala-Asn-4-methylcoumarin-7-amide + H2O
-
 Sus scrofa benzyloxycarbonyl-Phe-Ala-Asn + 7-amino-4-methylcoumarin
-
 ?
3.4.22.34 benzyloxycarbonyl-Pro-Ala-Asn-4-methylcoumarin-7-amide + H2O
-
 Sus scrofa benzyloxycarbonyl-Pro-Ala-Asn + 7-amino-4-methylcoumarin
-
 ?
3.4.22.34 benzyloxycarbonyl-Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
-
 Sus scrofa benzyloxycarbonyl-Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
 ?
3.4.22.34 benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
-
 Sus scrofa benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
-
 ?
3.4.22.34 bovine serum albumin + H2O SDS-denatured substrate, cleavage site are at positions 324 and 404 Sus scrofa 3 fragments
-
 ?
3.4.22.34 casein 1 + H2O cleavage site is at position 95 Sus scrofa 2 fragments
-
 ?
3.4.22.34 concanavalin A A-chain + H2O cleavage site are at positions 159 and 163 Sus scrofa 3 fragments
-
 ?
3.4.22.34 lysozyme C + H2O cleavage site are at positions 62 and 64 Sus scrofa 3 fragments
-
 ?
3.4.22.34 additional information substrate specificity, overview, activity with oligopeptides derived from several protein substrates, overview, no activity with peptides AWYFNHLKDA, and ANDPNRDILA, no activity with substrate analogues containing mono-or di-N-methylasparagines, L-2-amino-3-ureidopropionic acid or citrulline in the P1 position Sus scrofa ?
-
 ?
3.4.22.34 protein + H2O
-
 Sus scrofa peptides
-
 ?
3.4.22.34 protein + H2O strong specificity for asparaginyl residues located at the protein surface Sus scrofa peptides
-
 ?
3.4.22.34 rat alpha1-macroglobulin + H2O cleavage site are at positions 721 and 899 Sus scrofa 3 fragments
-
 ?
3.4.22.34 tetanus toxoid C fragment + H2O cleavage site are at positions 26, 337, and 372 Sus scrofa ?
-
 ?
3.4.22.34 transferrin + H2O cleavage site are at positions 95, 529, 574, and 603 Sus scrofa 5 fragments
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.22.34 Asparaginyl endopeptidase
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.22.34 30
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.22.34 5.8
-
 assay at Sus scrofa