3.4.22.34: Legumain
This is an abbreviated version!
For detailed information about Legumain, go to the full flat file.
Word Map on EC 3.4.22.34
-
3.4.22.34
-
cathepsins
-
phaseolus
-
vulgaris
-
vacuole
-
cystatins
-
proteinases
-
metastasis
-
papain
-
cotyledon
-
plasmodium
-
globulin
-
falciparum
-
vicilins
-
schistosoma
-
papain-like
-
tau
-
legume
-
endopeptidases
-
seed-specific
-
mesoamerican
-
phytohemagglutinin
-
falcipain-2
-
clan
-
mansoni
-
andean
-
leguminous
-
procathepsins
-
lunatus
-
cyclotides
-
jack
-
caspase-1-like
-
drug development
-
biotechnology
-
medicine
-
diagnostics
- 3.4.22.34
- cathepsins
- phaseolus
- vulgaris
- vacuole
- cystatins
- proteinases
- metastasis
- papain
- cotyledon
- plasmodium
- globulin
- falciparum
- vicilins
- schistosoma
-
papain-like
- tau
-
legume
- endopeptidases
-
seed-specific
-
mesoamerican
- phytohemagglutinin
- falcipain-2
-
clan
- mansoni
-
andean
-
leguminous
-
procathepsins
- lunatus
-
cyclotides
-
jack
-
caspase-1-like
- drug development
- biotechnology
- medicine
- diagnostics
Reaction
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds =
Synonyms
AEP, Antigen Sj32, Antigen SM32, As-specific vacuolar cysteine proteinase, Asn-specific vacuolar cysteine proteinase, asparagine endopeptidase, asparaginly endopeptidase, asparaginyl endopepidase, Asparaginyl endopeptidase, asparaginyl endopeptidase legumain, asparaginyl endopeptidase,, asparaginyl proteinase, asparaginyl-specific cysteine endopeptidase, asparagyl-endopeptidase, aspartate-specific endopeptidase, AtLEGgamma, Bean endopeptidase, C197 legumain, c197 Sm32, cysteine protease 1, hemoglobinase, HlLgm, HlLgm2, IrAE, IrAE protein, isae1, isae2, LeG, LEG-1, Leg-2, Leg-4, Leg1, Leg2, Leg3, Leg4, Leg5, legumain, legumain-1, LGMN, lysosomal asparaginycysteine endopeptidase, lysosomal asparaginyl endopeptidase, lysosomal cysteine proteinase, More, N197 legumain, osteoclast inhibitory peptide 2, Ov-aep-1, Phaseolin, Proteinase B, PrVPE1, schistosome legumain, Sj32, Sm32, SmAE, SmAE protein, SPAE, TcLEG3, TcLEG6, TcLEG9, TvAE1, vacuolar processing enzyme, vacuolar processing enzyme 1a, vacuolar processing enzyme 1b, vacuolar processing enzyme 2, vacuolar processing enzyme 3, Vicilin peptidohydrolase, VPE, VPE1a, VPE1b, VPE2, VPE3
ECTree
3.4.22.34 LegumainAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.22.34 - Legumain
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-Asp-Asn-Leu-Asp alpha-(4-methylcoumaryl-7-amide) + H2O
Ac-Asp-Asn-Leu-Asp + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Pro-Thr-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Pro-Thr-Asn + 7-amino-4-methylcoumarin
acetyl-Thr-Ala-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Thr-Ala-Asn + 7-amino-4-methylcoumarin
acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide + H2O
acetyl-Tyr-Val-Ala-Asp + 7-amino-4-methylcoumarin
AGTHNGQIGA + H2O
AGTHN + GQIGA
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived, low activity
-
?
AHIDNEEDIA + H2O
AHIDN + EEDIA
-
low activity, the peptide sequence is also cleaved in tetanus toxoid C fragment of which it is derived
-
?
ALKGNNLIWA + H2O
ALKGN + NLIWA
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
annexin II + H2O
?
cleavage of the N-terminus, enzyme plays a role in inactivation and degradation of annexin II in endosomes and lysosomes
-
?
AQLKNITDYA + H2O
AQLKN + ITDYA
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
AREDNNITLA + H2O
AREDN + NITLA
-
low activity, the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
ARLYNGLKFA + H2O
ARLYN + GLKFA
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
ASGFNSSVIA + H2O
ASGFN + SSVIA
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
ATITNDRLSA + H2O
ATITN + DLRSA
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
AYGTNEYSIA + H2O
AYGTN + EYSIA
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn + 7-amino-4-methylcoumarin
Benzyloxycarbonyl-Ala 4-nitrophenyl ester + H2O
Benzyloxycarbonyl-Ala + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcouamrin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Ala-Ala-Asp-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asp + 7-amino-4-methylcoumarin
the canonical Asn P1 specificity is only observed at pH 6.0, whereas a decrease in pH to 5.0 or even 4.0 results in a substantially increased number of cleavages of which almost half are after Asp
-
-
?
benzyloxycarbonyl-Ala-Glu-Asn-Xaa-Ala-Glu-Lys-NH2 + H2O
benzyloxycarbonyl-Ala-Glu-Asn + Xaa-Ala-Glu-Lys-NH2
-
substrate specificity at S1 position, overview
-
?
Benzyloxycarbonyl-Ala-Pro-Tyr-Asn 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Asn nitrophenyl ester + H2O
Benzyloxycarbonyl-Asn + 4-nitrophenol
-
-
-
?
Benzyloxycarbonyl-Gly 4-nitrophenyl ester + H2O
Benzyloxycarbonyl-Gly + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-Gly-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Gly-Ala-Asn + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Ile-Ser-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ile-Ser-Asn + 7-amino-4-methylcoumarin
low activity with
-
?
benzyloxycarbonyl-Leu-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Ala-Asn + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe 4-nitrophenyl ester + H2O
benzyloxycarbonyl-Phe + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-Phe-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Ala-Asn + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Pro-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Pro-Ala-Asn + 7-amino-4-methylcoumarin
Benzyloxycarbonyl-Tyr 4-nitrophenyl ester + H2O
Benzyloxycarbonyl-Tyr + 4-nitrophenol
-
-
-
?
benzyloxycarbonyl-Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Tyr-Ala-Asn + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
bovine albumin + H2O
peptides containing C-terminal Asn
-
-
-
?
bovine haemoglobin + H2O
peptides containing C-terminal Asn
exhibited strict specificity for the asparaginyl bonds on the carboxy-terminal side of a peptide
-
-
?
bovine serum albumin + H2O
3 fragments
-
SDS-denatured substrate, cleavage site are at positions 324 and 404
-
?
carbobenzyloxy-Ala-Ala-Asn-ethylenediamine-etoposide + H2O
etoposide-ethylenediamine + carbobenzyloxy-Ala-Ala-Asn
-
legumain releases the chemotherapeutic agent etoposide, as the active drug
-
-
?
CBZ-Ala-Ala-Asn-amido-4-methylcoumarin + H2O
CBZ-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
concanavalin A A-chain + H2O
3 fragments
-
cleavage site are at positions 159 and 163
-
?
concanavalin A precursor + H2O
activated concanavalin A
-
internal excision of the propeptide and transpeptidation that leads to the inverted fusion of the 2 fragments of the precursor
-
?
GSVKAYTNFDAERD + H2O
GSVKAYTN + FDAERD
synthetic peptide, residues24-37, derived from the N-terminal sequence of bovine annexin II, cleavage at position N31-F32
-
?
legumain + H2O
processed legumain + N-terminal and C-terminal prodomains
-
autocatalysis
-
?
lysozyme C + H2O
3 fragments
-
cleavage site are at positions 62 and 64
-
?
myelin basic protein MBP + H2O
5 fragments
-
cleavage sites at positions 84-85 and 92-93, multiple-sclerosis-associated autoantigen, digestion, destruction of the immunodominant epitope 83-99
product determination
?
octapeptides basing on the processing sites of 11S proglobulin + H2O
?
-
-
-
?
papain-like cysteine proteinase precursors + H2O
activated papin-like cysteine proteinases
progelatinase A + H2O
gelatinase A + ?
-
in cell culture of human fibrosarcoma HT1080 cells, 72 kDa proform, activation by cleavage of an asparaginyl peptide bond at Asn109-Tyr110 or Asn111-Phe112 to form the N-terminus of the mature active gelatinase
62 kDa mature form
?
Proglycinin + H2O
?
-
cleavage takes place between the conserved Asn and Gly residues
-
-
?
Prolegumin + H2O
?
-
cleavage takes place between the conserved Asn and Gly residues
-
-
?
rat alpha1-macroglobulin + H2O
3 fragments
-
cleavage site are at positions 721 and 899
-
?
recombinant C-fragment of tetanus toxoid + H2O
?
-
cleavage of 3 peptide bonds
-
?
Ser-Glu-Ser-Glu-Asn-Gly-Leu-Glu-Glu-Thr + H2O
Ser-Glu-Ser-Glu-Asn + Gly-Leu-Glu-Glu-Thr
-
-
-
?
succinyl-Tyr-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
succinyl-Tyr-Val-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
Tert-Butoxycarbonyl-Gln 4-nitrophenyl ester + H2O
Tert-Butoxycarbonyl-Gln + 4-nitrophenol
-
-
-
?
tetanus toxoid C fragment + H2O
3 fragments
-
cleavage sites are at Asn26, Asn97, and Asn372, but not Asn337
-
?
tetanus toxoid C fragment + H2O
?
-
cleavage site are at positions 26, 337, and 372
-
?
tetanus toxoid C fragment + H2O
tetanus toxoid fragments
-
cleavage sites are at Asn26, Asn337, and Asn372
-
?
transferrin + H2O
5 fragments
-
cleavage site are at positions 95, 529, 574, and 603
-
?
Vicilin + H2O
?
-
degradation of the principal reserve protein present in Vigna radiata seeds
-
-
?
Z-Ala-Pro-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Pro-Asn + 7-amino-4-methylcoumarin
-
-
-
?
Z-Ala-Ser-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ser-Asn + 7-amino-4-methylcoumarin
-
-
-
?
Z-ESEN-7-amido-4-methylcoumarin + H2O
Z-ESEN + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Val-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Val-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
11S proglobulin + H2O
?
-
degradation of unassembled proteins or misfolded precursors
-
?
11S proglobulin + H2O
?
-
degradation of unassembled proteins or misfolded precursors
-
?
11S proglobulin + H2O
?
degradation of unassembled proteins or misfolded precursors
-
?
11S proglobulin + H2O
?
-
degradation of unassembled proteins or misfolded precursors
-
?
11S proglobulin + H2O
?
-
degradation of unassembled proteins or misfolded precursors
-
?
acetoacetyl-CoA synthetase + H2O
?
Asn547 is the specific cleavage site of acetoacetyl-CoA synthetase in mouse livers. The cleaved form of acetoacetyl-CoA synthetase (1-547) loses the ability to convert acetoacetate to acetoacetyl-CoA. Cleavage of acetoacetyl-CoA synthetase by legumain is critical for the regulation of enzymatic activity and results in gain-of-function changes. Acetoacetyl-CoA synthetase(1-547) increases the protein expression of caveolin-1, the principal component of the caveolae
-
-
?
acetoacetyl-CoA synthetase + H2O
?
Asn547 is the specific cleavage site of acetoacetyl-CoA synthetase in mouse livers. The cleaved form of acetoacetyl-CoA synthetase (1-547) loses the ability to convert acetoacetate to acetoacetyl-CoA
-
-
?
acetyl-Pro-Thr-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Pro-Thr-Asn + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Pro-Thr-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Pro-Thr-Asn + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Thr-Ala-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Thr-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Thr-Ala-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Thr-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide + H2O
acetyl-Tyr-Val-Ala-Asp + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide + H2O
acetyl-Tyr-Val-Ala-Asp + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-Asn-4-nitroanilide + H2O
benzoyl-Asn + 4-nitroaniline
Bz-Asn-pNA, recombinant protein, at 37°C
-
-
?
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
best synthetic substrate
-
?
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
recombinant protein
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
recombinant protein
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
inhibitory activity of phytocystatin variants of Hordeum vulgare tested against commercial human legumain
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
inhibitory activity of cystatin variants of Hordeum vulgare against endogenous legumain activity in protein extracts of Hordeum vulgare analyzed
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
inhibitory activity of cystatin variants of Hordeum vulgare against endogenous legumain activity in protein extracts of roots of Hordeum vulgare analyzed
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
activity of recombinant protein determined
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
effect of legumain on fibronectin degradation analyzed, role of legumain in control of extracellular matrix turnover determined
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
role of legumain in backbone cyclization of proteins determined, catalysis of protein backbone cyclization by coupling asparaginyl bond hydrolysis at the C terminus of the cyclotide domain with peptide bond ligation
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
role of legumain in backbone cyclization of proteins analyzed, catalysis of protein backbone cyclization by coupling asparaginyl bond hydrolysis at the C terminus of the cyclotide domain with peptide bond ligation
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
best synthetic substrate
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
role of legumain in backbone cyclization of proteins analyzed, catalysis of protein backbone cyclization by coupling asparaginyl bond hydrolysis at the C terminus of the cyclotide domain with peptide bond ligation
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
the canonical Asn P1 specificity is only observed at pH 6.0, whereas a decrease in pH to 5.0 or even 4.0 results in a substantially increased number of cleavages of which almost half are after Asp
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Gly-Ala-Asn + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Gly-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Gly-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Gly-Ala-Asn + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Leu-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Ala-Asn + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Leu-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Ala-Asn + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Phe-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Ala-Asn + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Pro-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Pro-Ala-Asn + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Pro-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Pro-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Pro-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Pro-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
-
fluorogenic substrate
-
?
Bovine serum albumin + H2O
?
degradation in a dose-dependent manner at pH 7 and 30°C during 6 h of incubation, no cleavage detected at or above 37°C, strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines shown
-
-
?
Bovine serum albumin + H2O
?
degradation in a dose-dependent manner at pH 7 and 30°C during 6 h of incubation, no cleavage detected at or above 37°C, strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines shown
-
-
?
cathepsin B proform + H2O
activated cathepsin B
trans-processing and activation of the zymogen form of Schistosoma mansoni cathepsin B1 indicated
-
-
?
cathepsin B proform + H2O
activated cathepsin B
-
cleavage at the sequence Asp-Trp-Asn-Val-Ile-Pro, cleavage site between Asn and Val, between the prodomain and the mature regions of the protein, activation of the substrate, recombinant substrate from Schistosoma mansoni
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 + H2O
Dinitrophenyl-Pro-Glu-Ala-Asn + NH4OH
-
-
-
-
?
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 + H2O
Dinitrophenyl-Pro-Glu-Ala-Asn + NH4OH
-
-
-
?
gelatinase + H2O
gelatinase fragment
-
62 kDa active form, cleavage site is Asn430
36 kDa active form
?
gelatinase + H2O
gelatinase fragment
-
62 kDa active form, cleavage site is Asn430
36 kDa active form
?
Hemoglobin + H2O
?
strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines indicated
-
-
?
Hemoglobin + H2O
?
strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines indicated
-
-
?
Hemoglobin + H2O
?
degradation of human hemoglobin to a major product of 4000 Dalton at pH 4.5, less efficiency at pH 6.0, yielding two products at 6000 and 4000 Dalton, no reaction at pH 7.0 observed, strict specificity for Asn at P1 shown
-
-
?
Hemoglobin + H2O
?
the enzyme is involved in host hemoglobin degradation
-
-
?
Hemoglobin + H2O
?
the enzyme is involved in host hemoglobin degradation
-
-
?
Hemoglobin + H2O
?
the recombinant beta-galactosidase fusion enzyme shows hemoglobinase activity
-
-
?
papain-like cysteine proteinase precursors + H2O
activated papin-like cysteine proteinases
-
cleavage of C-terminal propeptide
-
?
papain-like cysteine proteinase precursors + H2O
activated papin-like cysteine proteinases
-
involved in the senescing of tissues and cell death
-
?
phaseolin + H2O
?
initiation of phaseolin proteolysis, enyme plays a key role in mobilization of phaseolin during and after kidney bean germination
-
?
precursor of basic vacuolar chitinase + H2O
active basic vacuolar chitinase
-
cleavage of C-terminal propeptide
-
?
precursor of basic vacuolar chitinase + H2O
active basic vacuolar chitinase
-
involved in the senescing of tissues and cell death
-
?
progelatinase A + H2O
gelatinase + ?
-
72 kDa proform, activation by cleavage of an asparaginyl peptide bonde to form the N-terminus of the mature active gelatinase
62 kDa mature form
?
progelatinase A + H2O
gelatinase + ?
-
72 kDa human proform, activation by cleavage of an asparaginyl peptide bonde to form the N-terminus of the mature active gelatinase
62 kDa mature form
?
protein + H2O
peptides
-
involved in mobilization of storage proteins and stress response processes
-
?
protein + H2O
peptides
-
enzyme is involved in antigen presentation within class II MHC positive cells and in pro-protein processing
-
?
protein + H2O
peptides
-
substrate specificity is dominated by the interaction of the S1 subsite
-
?
protein + H2O
peptides
-
an Asn residue at P1 position is strictly required
-
?
protein + H2O
peptides
-
strong specificity for asparaginyl residues located at the protein surface
-
?
protein + H2O
peptides
-
enzyme is critically involved in the lysosomal processing of bacterial antigens for MHC class II presentation
-
?
protein + H2O
peptides
-
enzyme is involved mainly in storage protein breakdown
-
?
tert-butoxycarbonyl-Asn nitrophenyl ester + H2O
tert-butoxycarbonyl-Asn + 4-nitrophenol
-
-
-
-
?
tert-butoxycarbonyl-Asn nitrophenyl ester + H2O
tert-butoxycarbonyl-Asn + 4-nitrophenol
-
-
-
?
vitamin D-binding protein + H2O
?
cleavage sites are, besides others, N150-Y151, and N83-S84
-
?
vitamin D-binding protein + H2O
?
enzyme is involved in the processing of mcromolecules absorbed by proximal tubule cells
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
-
during germination and seedling growth legumains might also act as processing enzymes, protein processing and degradation by legumains, overview
-
?
additional information
?
-
the enzyme has protease activity and efficient peptide bond ligase activity
-
-
?
additional information
?
-
-
the enzyme has protease activity and efficient peptide bond ligase activity
-
-
?
additional information
?
-
substrate specificity, no activity with acetyl-Asp-Glu-Val-Asp-4-methylcoumarin-7-amide, and acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide
-
?
additional information
?
-
-
substrate specificity, no activity with acetyl-Asp-Glu-Val-Asp-4-methylcoumarin-7-amide, and acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide
-
?
additional information
?
-
enzyme is a protease which specifically cleaves on the carboxyl side of asparagine residues
-
-
?
additional information
?
-
-
enzyme is a protease which specifically cleaves on the carboxyl side of asparagine residues
-
-
?
additional information
?
-
the function of legumain in the endometrium during early placentation may be through its role as an activator of protease zymogens such as progelatinase A
-
-
?
additional information
?
-
-
the function of legumain in the endometrium during early placentation may be through its role as an activator of protease zymogens such as progelatinase A
-
-
?
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
-
-
?
additional information
?
-
-
specificity overview with various peptide substrates, strict specificity towards asparagine bonds
-
-
?
additional information
?
-
-
thought to be involved in the hydrolysis of stored seed proteins
-
-
?
additional information
?
-
-
during germination and seedling growth legumains might also act as processing enzymes, protein processing and degradation by legumains, overview
-
?
additional information
?
-
-
the enzyme hydrolyzes peptide bonds with Asn in P1 and all 20 amino acids in P1' including S-alkylated Cys, with a few exceptions
-
-
?
additional information
?
-
enzyme is involved in host blood-meal digestion
-
-
?
additional information
?
-
-
enzyme is involved in host blood-meal digestion
-
-
?
additional information
?
-
-
recombinant HlLgm and HlLgm2 efficiently digest blood proteins, haemoglobin and bovine serum albumin
-
-
?
additional information
?
-
-
role of legumain in blood feeding and blood-meal digestion in ticks
-
-
?
additional information
?
-
-
no activity with acetyl-Phe-Tyr-Asn-4-methylcoumarin-7-amide
-
?
additional information
?
-
-
no activity with benzyloxycarbonyl-Gly-Ala-Gln-4-methylcoumarin-7-amide
-
?
additional information
?
-
enzyme inhibits osteoclast-like multinucleated cell formation in humans by more than 60% and bone resorption in the fetal rat long bone
-
?
additional information
?
-
-
enzyme inhibits osteoclast-like multinucleated cell formation in humans by more than 60% and bone resorption in the fetal rat long bone
-
?
additional information
?
-
-
silencing of endogenous specific inhibitor cystatin M by siRNA leads to increased enzyme activity in MDA-686Ln cells and increasec cell migration/proliferation, and also to reduced cysteine protease inhibitor activity, overview
-
-
?
additional information
?
-
-
the enzyme controls antigen processing performing the key step, mechanism, the enzyme expression is reduced in endotoxin-tolerant monocytes and by lipopolysaccharide priming
-
-
?
additional information
?
-
-
the inhibition of osteoclast formation and bone resorption is a nonenzymatic function of prolegumain
-
-
?
additional information
?
-
involved in lysosomal processing of bacterial antigens for MHC class II presentation
-
-
?
additional information
?
-
-
involved in lysosomal processing of bacterial antigens for MHC class II presentation
-
-
?
additional information
?
-
subsite specificity of legumain analyzed to design fluorescent activity-based probes for monitoring endogenous legumain activity
-
-
?
additional information
?
-
-
subsite specificity of legumain analyzed to design fluorescent activity-based probes for monitoring endogenous legumain activity
-
-
?
additional information
?
-
-
enzyme promote cell migration and is associated with enhanced tissue invasion and metastases
-
-
?
additional information
?
-
-
legumain is a member of the C13 family of peptidases that specifically cleaves asparaginyl bonds
-
-
?
additional information
?
-
a gel based label-free proteomic approach (DIPPS-direct in-gel profiling of protease specificity) is developed that enables quick and reliable determination of protease cleavage specificities under large variety of experimental conditions. The methodology is based on in-gel digestion of the gel-separated proteome with the studied protease, enrichment of cleaved peptides by gel extraction, and subsequent mass spectrometry analysis combined with a length-limited unspecific database search. Specificity profiling of legumain at pH 4.0 reveales a pH-dependent change in the specificity of this protease. The canonical Asn P1 specificity is only observed at pH 6.0, whereas a decrease in pH to 5.0 or even 4.0 results in a substantially increased number of cleavages of which almost half are after Asp
-
-
?
additional information
?
-
ideal cleavage sequence: Pro-Thr-Asn (P3-P2-P1)
-
-
?
additional information
?
-
-
ideal cleavage sequence: Pro-Thr-Asn (P3-P2-P1)
-
-
?
additional information
?
-
the cysteine protease enzyme legumain hydrolyzes peptide bonds with high specificity after asparagine and under more acidic conditions after aspartic acid. Legumain additionally exhibits ligase activity that prevails at pH above 5.5. Ligation is not the exact reverse of the proteolysis but can proceed via two distinct routes. Whereas the transpeptidation route involves aminolysis of the thioester, at pH 6 a cysteine-independent, histidine-assisted ligation route is detected
-
-
?
additional information
?
-
-
the cysteine protease enzyme legumain hydrolyzes peptide bonds with high specificity after asparagine and under more acidic conditions after aspartic acid. Legumain additionally exhibits ligase activity that prevails at pH above 5.5. Ligation is not the exact reverse of the proteolysis but can proceed via two distinct routes. Whereas the transpeptidation route involves aminolysis of the thioester, at pH 6 a cysteine-independent, histidine-assisted ligation route is detected
-
-
?
additional information
?
-
-
contrasting its endopeptidase activity, legumain can develop a carboxypeptidase activity which remains stable at neutral pH
-
-
?
additional information
?
-
-
the enzyme is not required for class II MHC antigen presentation but is essential for processing of cathepsin L in mice
-
-
?
additional information
?
-
role in extracellular matrix remodeling via degradation of fibronectin indicated
-
-
?
additional information
?
-
-
role in extracellular matrix remodeling via degradation of fibronectin indicated
-
-
?
additional information
?
-
-
asparaginyl endopeptidase plays a pivotal role in the endosome and lysosomal degradation system and is implicated in antigen processing and presentation
-
-
?
additional information
?
-
-
asparaginyl endopeptidaseprotein substrates on the C-terminal side of asparagine
-
-
?
additional information
?
-
-
role in backbone cyclization of proteins determined, catalyis of peptide bond cleavage and of ligation of plant-specific cyclotides in a single processing event
-
-
?
additional information
?
-
during germination and seedling growth legumains might also act as processing enzymes, protein processing and degradation by legumains, overview
-
?
additional information
?
-
-
role in backbone cyclization of proteins determined, catalyis of peptide bond cleavage and of ligation of plant-specific cyclotides in a single processing event
-
-
?
additional information
?
-
asparaginyl endopeptidases are cysteine proteases that hydrolyze peptides and proteins on the carboxyl side of asparagine residues
-
-
?
additional information
?
-
-
asparaginyl endopeptidases are cysteine proteases that hydrolyze peptides and proteins on the carboxyl side of asparagine residues
-
-
?
additional information
?
-
-
enzyme has high YVADase (caspase-1-like) activity (set to 100%). It also exhibits a significant level of IETDase (caspase-8) activity (39%) and DEVDase activity (18%). Unprocessed VPE1 has residual VEIDase (caspase-6) and LEVDase (caspase-4) activities, and negligible LEHDase (caspase-9) and GRRase (metacaspase) activities
-
-
?
additional information
?
-
-
PrVPE1 binds to the DEVD tetrapeptide, a signature substrate for caspase-3
-
-
?
additional information
?
-
-
substrate specificity for P3 position residues
-
?
additional information
?
-
-
the enzyme hydrolyzes peptide bonds with Asn in P1
-
-
?
additional information
?
-
-
processing enzyme of vacuoles, is responsible for the conversion of several vacuolar precursors into their mature forms
-
-
?
additional information
?
-
-
during germination and seedling growth legumains might also act as processing enzymes, protein processing and degradation by legumains, overview
-
?
additional information
?
-
-
the enzyme is involved in degradation of seed storage proteins
-
-
?
additional information
?
-
bioinformatic approach, studies on vacuolar targeting by determination of minimal vacuole targeting motifs, GFP reporter analysis and subcellular staining indicated
-
-
?
additional information
?
-
bioinformatic approach, studies on vacuolar targeting, determination of minimal vacuole targeting motifs, GFP reporter analysis and subcellular staining indicated
-
-
?
additional information
?
-
-
no activity with acetyl-Phe-Tyr-Asn-4-methylcoumarin-7-amide
-
?
additional information
?
-
the enzyme strictly requires Asn at P1, and prefers Ala, Thr, Val, Asn in descending order at P2, and Thr, Ala, Val, and Ile at P3, overview
-
-
?
additional information
?
-
the enzyme strictly requires Asn at P1, and prefers Ala, Thr, Val, Asn in descending order at P2, and Thr, Ala, Val, and Ile at P3, overview
-
-
?
additional information
?
-
no pivotal role for cathepsin B1 activation in vivo
-
-
?
additional information
?
-
-
no pivotal role for cathepsin B1 activation in vivo
-
-
?
additional information
?
-
analysis of in vivo processing activity of schistosome legumain to convert cathepsin B1 into its active form, no essential role for cathepsin B1 activation in vivo determined
-
-
?
additional information
?
-
-
analysis of in vivo processing activity of schistosome legumain to convert cathepsin B1 into its active form, no essential role for cathepsin B1 activation in vivo determined
-
-
?
additional information
?
-
ideal cleavage sequence: Thr-Ala-Asn (P3-P2-P1)
-
-
?
additional information
?
-
-
no activity with angiotensin I, [Asn1,Val5]angiotensin II, peptides ASTTNYT and GSNKGAIIGLM, substance P, and dynorphin A fragment 1-13, no activity with Asn-4-methylcoumarin-7-amide or Asp-4-methylcoumarin-7-amide
-
?
additional information
?
-
-
substrate specificity for P3 position residues
-
?
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
-
?
additional information
?
-
-
the enzyme acts strictly as asparaginyl endopeptidase, substrate specificity, overview
-
-
?
additional information
?
-
-
plant legumain shows a preference for bulky residues at P3 position
-
-
?
additional information
?
-
-
during germination and seedling growth legumains might also act as processing enzymes, protein processing and degradation by legumains, overview
-
?
additional information
?
-
-
role in backbone cyclization of proteins determined, catalyis of peptide bond cleavage and of ligation of plant-specific cyclotides in a single processing event
-
-
?
