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Information on EC 3.4.22.34 - Legumain
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3.4.22.34 LegumainSpecify your search results
Word Map
- 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
legumain, phaseolin, asparaginyl endopeptidase, lysosomal cysteine proteinase, vacuolar processing enzyme, hemoglobinase, asparagine endopeptidase, vicilin peptidohydrolase, hllgm, hllgm2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AEP
Antigen Sj32
Antigen SM32
Asn-specific vacuolar cysteine proteinase
asparagine endopeptidase
Asparaginyl endopeptidase
Bean endopeptidase
-
-
-
-
hemoglobinase
HlLgm2
legumain
LGMN
lysosomal cysteine proteinase
Phaseolin
-
-
-
-
Proteinase B
schistosome legumain
vacuolar processing enzyme
Vicilin peptidohydrolase
-
-
-
-
VPE
additional information
Antigen Sj32
-
-
-
-
Antigen SM32
-
-
-
-
Asparaginyl endopeptidase
-
-
-
-
Proteinase B
-
-
-
-
additional information
the enzyme belongs to the C13 peptidase family
additional information
the enzyme belongs to the C13 peptidase family
additional information
the enzyme belongs to the C13 peptidase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
-
-
-
-
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
best known from legume seeds, the trematode Schistosoma mansoni and mammalian lysosomes. Not inhibited by compound E-64. Type example of peptidase family C13
-
-
-
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
active site His151
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
active site His151 and Cys197
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
the enzyme contains essential catalytic His and Cys residues
-
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
the enzyme contains essential catalytic His and Cys residues
-
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
the enzyme contains essential catalytic His and Cys residues
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
149371-18-6
-
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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
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
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
-
-
?
annexin II + H2O
?
cleavage of the N-terminus, enzyme plays a role in inactivation and degradation of annexin II in endosomes and lysosomes
-
?
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
-
-
?
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
-
involved in the senescing of tissues and cell death
-
?
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
?
Vicilin + H2O
?
-
degradation of the principal reserve protein present in Vigna radiata seeds
-
-
?
vitamin D-binding protein + H2O
?
enzyme is involved in the processing of mcromolecules absorbed by proximal tubule cells
-
?
Hemoglobin + H2O
?
the enzyme is involved in host hemoglobin degradation
-
-
?
Hemoglobin + H2O
?
the enzyme is involved in host hemoglobin degradation
-
-
?
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
-
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
-
?
additional information
?
-
-
during germination and seedling growth legumains might also act as processing enzymes, protein processing and degradation by legumains, overview
-
?
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
?
-
-
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
?
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
no pivotal role for cathepsin B1 activation in vivo
-
-
?
additional information
?
-
-
no pivotal role for cathepsin B1 activation in vivo
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]cyclopropyl)carbamic acid
-
-
(1-[[(2S)-2-[[2-(2-amino-2-oxoethyl)-2-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]hydrazinyl]carbonyl]pyrrolidin-1-yl]carbonyl]cyclopropyl)carbamic acid
-
-
(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidine-1-carboxylic acid
-
-
(2S)-2-[[2-(2-amino-2-oxoethyl)-2-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]hydrazinyl]carbonyl]pyrrolidine-1-carboxylic acid
-
-
(2S)-N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2-[[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl](methanesulfonyl)amino]butanamide
-
(3-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]phenyl)carbamic acid
-
-
(3S)-3-[(1-acetyl-L-prolyl)amino]-5-[(2,6-dimethylbenzoyl)oxy]-4-oxopentanoic acid
-
starting structure for development of activity-based probes for in vivo imaging
(4-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]benzyl)carbamic acid
-
-
2,2-dimethyl-propionic acid 3-benzyloxycarbonylamino-4-carbamoyl-2-oxo-butyl ester
-
weak inhibition
2,6-dimethyl-benzoic acid 3-benzyloxycarbonylamino-4-carbamoyl-2-oxo-butyl ester
-
enters cells and causes complete, irreversible inhibition of the enzyme, inhibition of autocatalytic processing in vivo
2-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]piperidine-1-carboxylic acid
-
-
3-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]-3,4-dihydroisoquinoline-2(1H)-carboxylic acid
-
-
4-(2-aminoethyl) benzenesulfonyl fluoride
AEBSF, 45.8% inhibition at 5 mM
4-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]-1,3-thiazolidine-3-carboxylic acid
-
-
Ac-Tyr-Val-Ala-Asp-chloromethylketone
the rate of inhibition by Asp-CMK is approximately 3times more rapid at pH 4.0 than at pH 5.5
Ala-Ala-Asn-chloromethylketone
the rate of inhibition by Asn-CMK is approximately 1.3times more rapid at pH 5.5 than at pH 4.0
alpha-2-Macroglobulin
proteinase inhibitor, may be a candidate for the binding of legumain as it is an agent for the removal of endopeptidases from extracellular fluids
-
antipain
papain-like cysteine proteinase inhibitor, 28.77% inhibition at 0.1 mM concentration relative to control
asparaginyl endopeptidase inhibitor
-
i.e. AEPi or cysteine protease inhibitor
-
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-bromomethylketone
-
strong specific and irreversible inhibition
E-64
papain-like cysteine proteinase inhibitor, 7.51% inhibition at 0.3 mM concentration relative to control
egg white cystatin
concentration of 2 microM, 45.13% inhibition of recombinant protein activity
-
ethyl (2E)-4-[1-(2-amino-2-oxoethyl)-2-[[(2S)-1-(2-oxopropanoyl)pyrrolidin-2-yl]carbonyl]hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[(2E)-2-(acetylamino)but-2-enoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)-3-(4-hydroxy-3-nitrophenyl)propanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)butanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)pent-4-ynoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[2-(acetylamino)-2-methylpropanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[2-(acetylamino)-3-methylbut-2-enoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[3-(acetylamino)benzoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[4-(acetylamino)benzoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-[[(2S)-1-[[(2R)-1-acetylpiperidin-2-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-[[(2S)-1-[[(3S)-2-acetyl-1,2,3,4-tetrahydroisoquinolin-3-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-[[(2S)-1-[[(4S)-3-acetyl-1,3-thiazolidin-4-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-[[(2S)-1-[[1-(acetylamino)cyclopropyl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2S,3S)-3-[[1-(2-amino-2-oxoethyl)-2-[([2S)-1-(2-oxopropanoyl)pyrrolidin-2-yl]carbonyl]hydrazinyl]carbonyl]oxirane-2-carboxylate
-
-
ethyl (2S,3S)-3-[[2-([(2S)-1-[(2R)-2-(acetylamino)butanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
-
-
ethyl (2S,3S)-3-[[2-([(2S)-1-[(2R)-2-(acetylamino)pent-4-ynoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
-
-
ethyl (2S,3S)-3-[[2-[[(2S)-1-acetylpyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
-
starting structure for development of activity-based probes for in vivo imaging
ethyl (2S,3S)-3-[[2-[[(2S)-1-[[1-(acetylamino)cyclopropyl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
-
-
human cystatin C mutant L9G
-
inhibitory potential similar to wild-type cystatin C
-
human cystatin C mutant N39K
-
reduced inhibitory effect compared to the wild-type cystatin C
-
human cystatin C mutant R8G
-
inhibitory potential similar to wild-type cystatin C
-
human cystatin C mutant V10G
-
inhibitory potential similar to wild-type cystatin C
-
human cystatin C mutant W106G
-
inhibitory potential similar to wild-type cystatin C
-
N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone
0.1 mM, 0.23% remaining activity
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(2',4'-dichloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(2'-chloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(2,4-dichlorobenzene-1-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(3',4'-dichloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(3',4'-difluoro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(3'-fluoro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-chloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-cyano[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-ethyl[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-methoxy[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-methyl[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-tert-butyl[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4-bromobenzene-1-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4-chlorobenzene-1-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4-fluorobenzene-1-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-([1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[2'-(trifluoromethyl)[1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4'-(propan-2-yl)[1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4'-(trifluoromethyl)[1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4'-[(propan-2-yl)oxy][1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4-(2H-1,3-benzodioxol-5-yl)benzene-1-sulfonyl]-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4-(trifluoromethyl)benzene-1-sulfonyl]-L-prolinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[2'-(trifluoromethyl)[1,1'-biphenyl]-4-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4'-(trifluoromethyl)[1,1'-biphenyl]-4-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(1-methyl-1H-indazol-5-yl)benzene-1-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(1-methyl-1H-indazol-7-yl)benzene-1-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(2-methyl-2H-indazol-5-yl)benzene-1-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(2-methyl-2H-indazol-7-yl)benzene-1-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(4-methylpyridin-3-yl)benzene-1-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(5-methylpyridin-3-yl)benzene-1-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-[4-(trifluoromethyl)pyridin-3-yl]benzene-1-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-[5-(trifluoromethyl)pyridin-3-yl]benzene-1-sulfonyl]propanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(2',3'-difluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(2',4'-dichloro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(2',4'-difluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(3',5'-difluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(3'-fluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(4'-butyl[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(4'-chloro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(4'-fluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(4'-tert-butyl[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-([1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(1,3-benzothiazol-5-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(4-chloropyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(4-fluoropyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(4-tert-butylpyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(5-chloropyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(5-fluoropyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(ethanesulfonyl)-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[(3'-methoxy[1,1'-biphenyl]-4-yl)methyl]-D-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[(3'-methoxy[1,1'-biphenyl]-4-yl)methyl]-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[(3'-propoxy[1,1'-biphenyl]-4-yl)methyl]-D-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[(3'-propoxy[1,1'-biphenyl]-4-yl)methyl]-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[[3'-(trifluoromethyl)[1,1'-biphenyl]-4-yl]methyl]-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(2-methylpropane-1-sulfonyl)-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(ethanesulfonyl)-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-norvalinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(propane-1-sulfonyl)-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3',4'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3',4'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3',5'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-chloro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-ethoxy[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(2-methylpropane-1-sulfonyl)-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-norvalinamide
-
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(4'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
-
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E)-4-oxo-4-phenylbut-2-enoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E,4E)-hexa-2,4-dienoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
N-[(benzyloxy)carbonyl]-L-alanyl-N-[(1S,3E)-1-(2-amino-2-oxoethyl)-5-[methyl(naphthalen-1-yl)amino]-2,5-dioxopent-3-en-1-yl]-L-alaninamide
i.e. aza-peptide Michael acceptor Aza-Asn-11a, inhibition of trans-processing and activation of the zymogen form of Schistosoma mansoni cathepsin B1 by prior incubation with the legumain-specific inhibitor Aza-Asn-11a, reaction in CPS buffer, pH 5.5 for 30 min
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1,3-dihydroisoindol-2-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2,3-dihydroindol-1-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2-furyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-1H-quinolin-2-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-2H-quinolin-1-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-phenyl-5,6-dihydro-2H-pyridin-1-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-bis-(2-furylmethyl)carbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-3-(N-methyl-N-(1-(N-methyl-N-phenethylcarbamoyl)phenylethyl)carbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
pepstatin
concentration of 500 microM, 7.8% inhibition of recombinant protein activity
PMSF
serine peptidase inhibitor, 13.84% inhibition at 5 mM concentration relative to control
trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane
E-64, concentration of 500 microM, 8.88% inhibition of recombinant protein activity
Z-Phe-Ala-CHN2
i.e. benzyloxycarbonyl-phenylalanyl-alanyl-diazomethane, 40.8% inhibition at 0.01 mM
[(2S)-1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-3-[4-hydroxy-3-[hydroxy(oxo)ammonio]phenyl]-1-oxopropan-2-yl]carbamate
-
-
[(2Z)-1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-1-oxobut-2-en-2-yl]carbamic acid
-
-
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-1-oxobutan-2-yl]carbamic acid
-
-
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-1-oxopent-4-yn-2-yl]carbamic acid
-
-
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-2-methyl-1-oxopropan-2-yl]carbamic acid
-
-
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-3-methyl-1-oxobut-2-en-2-yl]carbamic acid
-
-
[1-[(2S)-2-[[2-(2-amino-2-oxoethyl)-2-[[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]hydrazinyl]carbonyl]pyrrolidin-1-yl]-1-oxobutan-2-yl]carbamic acid
-
-
1,10-phenanthroline
concentration of 1 mM, 10 min before addition of substrate, 40% inhibition; concentration of 1mM, 10 min before addition of substrate, 40% inhibition observed
acetyl-Glu-Ser-Glu-Asn-aldehyde
-
hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner
acetyl-Glu-Ser-Glu-Asn-aldehyde
-
hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner
acetyl-Glu-Ser-Glu-Asn-aldehyde
-
hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner
Acetyl-Tyr-Val-Ala-Asp-aldehyde
-
hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner, reduced amounts of cyclic cyclotide produced in transiently transformed tobacco leaves determined
Acetyl-Tyr-Val-Ala-Asp-aldehyde
-
hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner
Acetyl-Tyr-Val-Ala-Asp-aldehyde
-
hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-chloromethylketone
Z-Ala-Ala-AzaAsn-CMK, 1 microM, 10 min before addition of substrate, 100% inhibition; Z-Ala-Ala-AzaAsn-CMK, 1 microM, 10 min before addition of substrate, 100% inhibition observed
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-chloromethylketone
-
strong specific and irreversible inhibition
carbobenzyloxy-Ala-Ala-(aza-Asn)-epoxycarboxylate ethyl ester
-
cystatin
from egg white, 62.3% inhibition at 0.003 mM concentration relative to control
-
cystatin E/M
-
cystatin E/M controls both intra- and extracellular legumain activity
-
cystatin M
-
specific endogenous inhibitor of lysosomal cysteine proteases, diverse tissue distribution, target specificity, and biological function, overview, high expression level in MDA-686Ln cells, silencing of cystatin M by siRNA leads to increased enzyme activity in MDA-686Ln cells
-
iodoacetamide
concentration of 5 mM,10 min before addition of substrate, 100% inhibition; concentration of 5 mM, 10 min before addition of substrate, 100% inhibition determined
iodoacetamide
concentration of 3 mM, 100% inhibition of recombinant protein activity, BSA cleavage inhibited by 5 mM iodoacetamide
iodoacetamide
100% inhibition at 3 mM concentration relative to control
iodoacetamide
complete inhibition at 5 mM inhibitor concentration
L-3-carboxy-2,3-trans-epoxypropionyl-leucyl-amido(4-guanidino)butane
-
i.e. E-64, not
leupeptin
concentration of 300 microM, 16.07% inhibition of recombinant protein activity
leupeptin
papain-like cysteine proteinase inhibitor, 3.9% inhibition at 0.3 mM concentration relative to control
N-ethylmaleimide
concentration of 3 mM, 95.74% inhibition of recombinant protein activity
N-ethylmaleimide
100% inhibition at 3 mM concentration relative to control
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E)-4-oxo-4-phenylbut-2-enoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
-
-
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E)-4-oxo-4-phenylbut-2-enoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
-
-
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E)-4-oxo-4-phenylbut-2-enoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
-
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E,4E)-hexa-2,4-dienoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
-
-
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E,4E)-hexa-2,4-dienoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
-
-
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E,4E)-hexa-2,4-dienoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1,3-dihydroisoindol-2-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1,3-dihydroisoindol-2-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1,3-dihydroisoindol-2-ylcarbonyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2,3-dihydroindol-1-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2,3-dihydroindol-1-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2,3-dihydroindol-1-ylcarbonyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2-furyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2-furyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2-furyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-1H-quinolin-2-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-1H-quinolin-2-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-1H-quinolin-2-ylcarbonyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-2H-quinolin-1-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-2H-quinolin-1-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-2H-quinolin-1-ylcarbonyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-phenyl-5,6-dihydro-2H-pyridin-1-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-phenyl-5,6-dihydro-2H-pyridin-1-ylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-phenyl-5,6-dihydro-2H-pyridin-1-ylcarbonyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-bis-(2-furylmethyl)carbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-bis-(2-furylmethyl)carbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-bis-(2-furylmethyl)carbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-3-(N-methyl-N-(1-(N-methyl-N-phenethylcarbamoyl)phenylethyl)carbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-3-(N-methyl-N-(1-(N-methyl-N-phenethylcarbamoyl)phenylethyl)carbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-3-(N-methyl-N-(1-(N-methyl-N-phenethylcarbamoyl)phenylethyl)carbamoylpropenoyl)hydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
-
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
-
-
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
-
-
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
-
pepstatin A
aspartic peptidase inhibitor has minimal effects on the enzyme activity, 12.22% inhibition at 0.3 mM concentration relative to control
pepstatin A
-
no effect on ability to cleave the Asn-containing substrate
pepstatin A
-
no effect on ability to cleave the Asn-containing substrate
phenylmethanesulfonyl fluoride
PMSF, concentration of 2 mM, 10 min before addition of substrate, 66% inhibition; PMSF, concentration of 2 mM, 10 min before addition of substrate, 66% inhibition shown
phenylmethanesulfonyl fluoride
PMSF, concentration of 5 mM, 19% inhibition of recombinant protein activity
phenylmethylsulfonyl fluoride
-
no effect on ability to cleave the Asn-containing substrate
phenylmethylsulfonyl fluoride
-
no effect on ability to cleave the Asn-containing substrate
phenylmethylsulfonyl fluoride
-
no effect on ability to cleave the Asn-containing substrate
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane
-
i.e. E-64, no effect on ability to cleave the Asn-containing substrate
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane
-
i.e. E-64, no effect on ability to cleave the Asn-containing substrate
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane
-
i.e. E-64, no effect on abilityto cleave the Asn-containing substrate
additional information
the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A
-
additional information
no inhibition by the general cysteine protease inhibitor E-64
-
additional information
-
no inhibition by the general cysteine protease inhibitor E-64
-
additional information
no significant inhibition by trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane (E-64) in a concentration of 10 microM, leupeptin in a concentration of 10 microM or pepstatin in a concentration of 5 microM; no significant inhibition observed by using trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane (E-64) in a concentration of 10 microM, leupeptin in a concentration of 10 microM or pepstatin in a concentration of 5 microM
-
additional information
no significant inhibition by trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane (E-64) in a concentration of 10 microM, leupeptin in a concentration of 10 microM or pepstatin in a concentration of 5 microM; no significant inhibition observed by using trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane (E-64) in a concentration of 10 microM, leupeptin in a concentration of 10 microM or pepstatin in a concentration of 5 microM
-
additional information
-
no significant inhibition by trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane (E-64) in a concentration of 10 microM, leupeptin in a concentration of 10 microM or pepstatin in a concentration of 5 microM; no significant inhibition observed by using trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane (E-64) in a concentration of 10 microM, leupeptin in a concentration of 10 microM or pepstatin in a concentration of 5 microM
-
additional information
-
the enzyme expression is reduced by lipopolysaccharide priming and in endotoxin-tolerant monocytes
-
additional information
inhibitory activity of the phytocystatins HvCPI-4 of Hordeum vulgare and FaCPI-1 of Fragaria sp. measured by the inhibition of legumain proteinase activity, ability of HvCPI-4 and FaCPI-1 to inhibit human legumain in vitro demonstrated
-
additional information
-
inhibitory activity of the phytocystatins HvCPI-4 of Hordeum vulgare and FaCPI-1 of Fragaria sp. measured by the inhibition of legumain proteinase activity, ability of HvCPI-4 and FaCPI-1 to inhibit human legumain in vitro demonstrated
-
additional information
inhibitor specificity profiles of cathepsin B and legumain regarded and used for analysis of the suitability of fluorescent activity-based probes
-
additional information
-
inhibitor specificity profiles of cathepsin B and legumain regarded and used for analysis of the suitability of fluorescent activity-based probes
-
additional information
the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A
-
additional information
-
the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A
-
additional information
-
inhibitory activity measured by the inhibition of legumain proteinase activity, phytocystatins that are able to inhibit human legumain also inhibit the barley legumain proteinase activities in developing roots, endogenous barley legumain activities inhibited by iodoacetamide, no inhibition by the non-legumain inhibitors leupeptin and E64 observed; inhibitory effects against endogenous legumain activity in barley protein extracts tested, inhibitory activity measured by the inhibition of legumain-like proteinase activity, phytocystatins able to inhibit human legumain also inhibit the barley legumain proteinase activities in developing endosperms, endogenous barley legumain activities inhibited by iodoacetamide, no inhibition by the non-legumain inhibitors leupeptin and E64 observed
-
additional information
-
the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A
-
additional information
no inhibition with EDTA, PMSF, pepstatin A, leupeptin, and E-64
-
additional information
-
no inhibition with EDTA, PMSF, pepstatin A, leupeptin, and E-64
-
additional information
no inhibition by Z-Phe-Ala-CHN2 and 1,10-phenanthroline
-
additional information
no inhibition by Z-Phe-Ala-CHN2 and 1,10-phenanthroline
-
additional information
the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A
-
additional information
-
glycosylation of asparaginyl residues totally prevents cleavage by the enzyme, no binding to human alpha2-macroglobulin
-
additional information
-
construction and irreversible specific inhibition of the enzyme by several derivatives of Michael acceptor inhibitors based on the backbone benzyloxycarbonal-L-Ala-L-Ala-L-Asn, overview
-
additional information
-
no inhibition by E-64, i.e. trans-epoxysuccinyl-L-leucylamido-(4-guanidino)-butane, no inhibition by PMSF, pepstatin and 1,10-phenanthroline
-
additional information
-
inhibition mechanism by human cystatins, enzyme inhibitor complex formation analysis, no inhibition by human type 1 cystatins A and B, type 2 cystatin D, and type 3 low MW kininogen
-
additional information
-
the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A
-
additional information
-
not: EDTA; N-tosyl-L-lysine chloromethyl ketone; phenylmethylsulfonyl fluoride
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
mRNAs is up-regulated in the endometrium during the luteal phase of the oestrous cycle and during early pregnancy
-
additional information
-
mRNAs is up-regulated in the endometrium during the luteal phase of the oestrous cycle and during early pregnancy
-
additional information
endogenous HlLgm2 expression in the midgut that is upregulated by the blood-feeding process is shown in all the developmental stages
-
additional information
-
endogenous HlLgm2 expression in the midgut that is upregulated by the blood-feeding process is shown in all the developmental stages
-
additional information
-
expression levels of endogenous legumain elevate in HEK-293 cells following stress
-
additional information
the enzyme expression in enhanced in the dark and after ethephon treatment of leaves
-
additional information
-
the enzyme expression in enhanced in the dark and after ethephon treatment of leaves
-
additional information
-
asparaginyl endopeptidase activation is autocatalytic and requires sequential removal of C- and N-terminal propeptides at different pH thresholds
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05195
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin
pH 5.5, 39°C
0.09
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
-
pH 5.5, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.33
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin
pH 5.5, 39°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000022
human cystatin C mutant R8G, human cystatin C mutant V10G, human cystatin C mutant W106G
-
pH 5.6, 37°C
-
0.000059
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[2'-(trifluoromethyl)[1,1'-biphenyl]-4-sulfonyl]propanamide
pH 7.4, 37°C
0.00029
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4'-(trifluoromethyl)[1,1'-biphenyl]-4-sulfonyl]propanamide
pH 7.4, 37°C
0.0000036
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(1-methyl-1H-indazol-5-yl)benzene-1-sulfonyl]propanamide
pH 7.4, 37°C
0.00000012
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(1-methyl-1H-indazol-7-yl)benzene-1-sulfonyl]propanamide
pH 7.4, 37°C
0.00000026
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(2-methyl-2H-indazol-5-yl)benzene-1-sulfonyl]propanamide
pH 7.4, 37°C
0.0000098
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(2-methyl-2H-indazol-7-yl)benzene-1-sulfonyl]propanamide
pH 7.4, 37°C
0.000026
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(4-methylpyridin-3-yl)benzene-1-sulfonyl]propanamide
pH 7.4, 37°C
0.000015
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-(5-methylpyridin-3-yl)benzene-1-sulfonyl]propanamide
pH 7.4, 37°C
0.000018
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-[4-(trifluoromethyl)pyridin-3-yl]benzene-1-sulfonyl]propanamide
pH 7.4, 37°C
0.000012
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2,2-dimethyl-3-[4-[5-(trifluoromethyl)pyridin-3-yl]benzene-1-sulfonyl]propanamide
pH 7.4, 37°C
0.000033
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(2',3'-difluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.00028
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(2',4'-dichloro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.000082
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(2',4'-difluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.00011
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(3',5'-difluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.0000013
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(3'-fluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.00016
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(4'-butyl[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.0000071
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(4'-chloro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.0000055
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(4'-fluoro[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.00087
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-(4'-tert-butyl[1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.000034
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-([1,1'-biphenyl]-4-sulfonyl)-2,2-dimethylpropanamide
pH 7.4, 37°C
0.00000047
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(1,3-benzothiazol-5-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
pH 7.4, 37°C
0.000012
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(4-chloropyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
pH 7.4, 37°C
0.000096
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(4-fluoropyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
pH 7.4, 37°C
0.0000014
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(4-tert-butylpyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
pH 7.4, 37°C
0.0000015
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(5-chloropyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
pH 7.4, 37°C
0.000078
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-3-[4-(5-fluoropyridin-3-yl)benzene-1-sulfonyl]-2,2-dimethylpropanamide
pH 7.4, 37°C
0.00076
FaCPI-1
-
inhibitor concentrations between 25 and 500 nM used, incubation with 10 microgram of a soluble endosperm protein extract, at 25°C and pH 6 for 10 min
-
0.00076
FaCPI-1
-
inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25°C and pH 6 for 10 min
-
0.00019
HvCPI-4
-
inhibitor concentrations between 25 and 500 nM used, incubation with 10 microgram of a soluble endosperm protein extract, at 25°C and pH 6 for 10 min
-
0.00019
HvCPI-4
-
inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25°C and pH 6 for 10 min
-
0.00019
HvCPI-4-deltaT143-Cterm
-
inhibitor concentrations between 25 and 500 nM used, incubation with 10 microgram of a soluble endosperm protein extract, at 25°C and pH 6 for 10 min
-
0.00019
HvCPI-4-deltaT143-Cterm
-
inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25°C and pH 6 for 10 min
-
0.00029
HvCPI-4-deltaT151-Cterm
-
inhibitor concentrations between 25 and 500 nM used, incubation with 10 microgram of a soluble endosperm protein extract, at 25°C and pH 6 for 10 min
-
0.00029
HvCPI-4-deltaT151-Cterm
-
inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25°C and pH 6 for 10 min
-
0.00013
HvCPI-4-Q86P
-
mutant Q86P of HvCPI-4, inhibitor concentrations between 25 and 500 nM used, incubation with 10 microgram of a soluble endosperm protein extract, at 25°C and pH 6 for 10 min
-
0.00013
HvCPI-4-Q86P
-
mutant Q86P of HvCPI-4, inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25°C and pH 6 for 10 min
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000093
(1-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]cyclopropyl)carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.0000044 - 0.0000086
(1-[[(2S)-2-[[2-(2-amino-2-oxoethyl)-2-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]hydrazinyl]carbonyl]pyrrolidin-1-yl]carbonyl]cyclopropyl)carbamic acid
0.0000083
(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidine-1-carboxylic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.0000093
(2S)-2-[[2-(2-amino-2-oxoethyl)-2-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]hydrazinyl]carbonyl]pyrrolidine-1-carboxylic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.005854
(2S)-N-[(1S)-3-amino-1-cyano-3-oxopropyl]-2-[[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl](methanesulfonyl)amino]butanamide
Homo sapiens
pH 7.4, 37°C
0.001
(3-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]phenyl)carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.000704
(3S)-3-[(1-acetyl-L-prolyl)amino]-5-[(2,6-dimethylbenzoyl)oxy]-4-oxopentanoic acid
Mus musculus
-
pH 7.4
0.000267
(4-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]benzyl)carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.000638
2-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]piperidine-1-carboxylic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.001
3-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]-3,4-dihydroisoquinoline-2(1H)-carboxylic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.000167
4-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]-1,3-thiazolidine-3-carboxylic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.0083
ethyl (2E)-4-[1-(2-amino-2-oxoethyl)-2-[[(2S)-1-(2-oxopropanoyl)pyrrolidin-2-yl]carbonyl]hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000141
ethyl (2E)-4-[2-([(2S)-1-[(2E)-2-(acetylamino)but-2-enoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.001
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)-3-(4-hydroxy-3-nitrophenyl)propanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0000065
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)butanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000017
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)pent-4-ynoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000198
ethyl (2E)-4-[2-([(2S)-1-[2-(acetylamino)-2-methylpropanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000148
ethyl (2E)-4-[2-([(2S)-1-[2-(acetylamino)-3-methylbut-2-enoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.001
ethyl (2E)-4-[2-([(2S)-1-[3-(acetylamino)benzoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000267
ethyl (2E)-4-[2-([(2S)-1-[4-(acetylamino)benzoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000638
ethyl (2E)-4-[2-[[(2S)-1-[[(2R)-1-acetylpiperidin-2-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.001
ethyl (2E)-4-[2-[[(2S)-1-[[(3S)-2-acetyl-1,2,3,4-tetrahydroisoquinolin-3-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000167
ethyl (2E)-4-[2-[[(2S)-1-[[(4S)-3-acetyl-1,3-thiazolidin-4-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0000093
ethyl (2E)-4-[2-[[(2S)-1-[[1-(acetylamino)cyclopropyl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0093
ethyl (2S,3S)-3-[[1-(2-amino-2-oxoethyl)-2-[([2S)-1-(2-oxopropanoyl)pyrrolidin-2-yl]carbonyl]hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0081
ethyl (2S,3S)-3-[[2-([(2S)-1-[(2R)-2-(acetylamino)butanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0086
ethyl (2S,3S)-3-[[2-([(2S)-1-[(2R)-2-(acetylamino)pent-4-ynoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0000115
ethyl (2S,3S)-3-[[2-[[(2S)-1-acetylpyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
pH 7.4
0.0044
ethyl (2S,3S)-3-[[2-[[(2S)-1-[[1-(acetylamino)cyclopropyl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000006
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(2',4'-dichloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000035
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(2'-chloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000593
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(2,4-dichlorobenzene-1-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000169
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(3',4'-dichloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000023
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(3',4'-difluoro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000033 - 0.000047
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(3'-fluoro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
0.000045 - 0.000067
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-chloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
0.000033
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-cyano[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000071
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-ethyl[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000006
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-methoxy[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000032
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-methyl[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000071
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-tert-butyl[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000282
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4-bromobenzene-1-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000073
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4-chlorobenzene-1-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000269
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4-fluorobenzene-1-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000012
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-([1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000093
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[2'-(trifluoromethyl)[1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000005
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4'-(propan-2-yl)[1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000121
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4'-(trifluoromethyl)[1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000073 - 0.000969
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4'-[(propan-2-yl)oxy][1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
0.000049
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4-(2H-1,3-benzodioxol-5-yl)benzene-1-sulfonyl]-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000332
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4-(trifluoromethyl)benzene-1-sulfonyl]-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.003889
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(ethanesulfonyl)-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.005854
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[(3'-methoxy[1,1'-biphenyl]-4-yl)methyl]-D-alaninamide
Homo sapiens
pH 7.4, 37°C
0.000378
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[(3'-methoxy[1,1'-biphenyl]-4-yl)methyl]-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.00505
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[(3'-propoxy[1,1'-biphenyl]-4-yl)methyl]-D-alaninamide
Homo sapiens
pH 7.4, 37°C
0.000882
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[(3'-propoxy[1,1'-biphenyl]-4-yl)methyl]-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.000601
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-(methanesulfonyl)-N2-[[3'-(trifluoromethyl)[1,1'-biphenyl]-4-yl]methyl]-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.001818
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(2-methylpropane-1-sulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.001086
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(ethanesulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.001459
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
Homo sapiens
pH 7.4, 37°C
0.007749
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-norvalinamide
Homo sapiens
pH 7.4, 37°C
0.006745
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2',3'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(propane-1-sulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.000356
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(2'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.006296
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3',4'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
Homo sapiens
pH 7.4, 37°C
0.000252
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3',4'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.001359 - 0.009249
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3',5'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
0.000425
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-chloro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)alaninamide
Homo sapiens
pH 7.4, 37°C
0.000586
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-ethoxy[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.002272
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(2-methylpropane-1-sulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.002259
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
Homo sapiens
pH 7.4, 37°C
0.000128
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.004384
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-norvalinamide
Homo sapiens
pH 7.4, 37°C
0.000323 - 0.001035
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(4'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
0.008
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E,4E)-hexa-2,4-dienoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000045 - 0.0003
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1,3-dihydroisoindol-2-ylcarbonyl)propenoyl)hydrazine
0.0005 - 0.001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
0.000018 - 0.00007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2,3-dihydroindol-1-ylcarbonyl)propenoyl)hydrazine
0.0075
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2-furyl)propenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000025 - 0.0002
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-1H-quinolin-2-ylcarbonyl)propenoyl)hydrazine
0.0000035 - 0.00007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-2H-quinolin-1-ylcarbonyl)propenoyl)hydrazine
0.008 - 0.01
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000075 - 0.0008
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
0.00001 - 0.00075
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-phenyl-5,6-dihydro-2H-pyridin-1-ylcarbonyl)propenoyl)hydrazine
0.0000055 - 0.000035
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
0.00005 - 0.0006
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
0.0000018 - 0.00006
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
0.00001 - 0.001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
0.00000055 - 0.000055
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
0.0009 - 0.015
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-bis-(2-furylmethyl)carbamoylpropenoyl)hydrazine
0.0000023 - 0.00045
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
0.0001 - 0.001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
0.002 - 0.0027
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
0.0000045 - 0.000031
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
0.00001 - 0.0006
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
0.00007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00001 - 0.0007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
0.00008 - 0.00075
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-3-(N-methyl-N-(1-(N-methyl-N-phenethylcarbamoyl)phenylethyl)carbamoylpropenoyl)hydrazine
0.00006 - 0.0007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
0.000006 - 0.000062
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
0.000006 - 0.00007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
0.000005 - 0.000038
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
0.0000028 - 0.00001
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
0.001
[(2S)-1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-3-[4-hydroxy-3-[hydroxy(oxo)ammonio]phenyl]-1-oxopropan-2-yl]carbamate
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.000141
[(2Z)-1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-1-oxobut-2-en-2-yl]carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.0000065
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-1-oxobutan-2-yl]carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.000017
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-1-oxopent-4-yn-2-yl]carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.000198
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-2-methyl-1-oxopropan-2-yl]carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.000148
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-3-methyl-1-oxobut-2-en-2-yl]carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.0000081
[1-[(2S)-2-[[2-(2-amino-2-oxoethyl)-2-[[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]hydrazinyl]carbonyl]pyrrolidin-1-yl]-1-oxobutan-2-yl]carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.0000044
(1-[[(2S)-2-[[2-(2-amino-2-oxoethyl)-2-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]hydrazinyl]carbonyl]pyrrolidin-1-yl]carbonyl]cyclopropyl)carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.0000086
(1-[[(2S)-2-[[2-(2-amino-2-oxoethyl)-2-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]hydrazinyl]carbonyl]pyrrolidin-1-yl]carbonyl]cyclopropyl)carbamic acid
Homo sapiens
-
pH 5.8, temperature not specified in the publication
0.000068
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Schistosoma mansoni
-
pH 6.8, 25°C
0.000058
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Schistosoma mansoni
-
pH 6.8, 25°C
0.00007
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Schistosoma mansoni
-
pH 6.8, 25°C
0.00075
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Schistosoma mansoni
-
pH 6.8, 25°C
0.000103
Mu-Ala-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Schistosoma mansoni
-
pH 6.8, 25°C
0.000033
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(3'-fluoro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000047
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(3'-fluoro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000045
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-chloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000067
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-(4'-chloro[1,1'-biphenyl]-4-sulfonyl)-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000073
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4'-[(propan-2-yl)oxy][1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000969
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-1-[4'-[(propan-2-yl)oxy][1,1'-biphenyl]-4-sulfonyl]-L-prolinamide
Homo sapiens
pH and temperature not specified in the publication
0.001359
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3',5'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
Homo sapiens
pH 7.4, 37°C
0.009249
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(3',5'-difluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-D-alaninamide
Homo sapiens
pH 7.4, 37°C
0.000323
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(4'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.001035
N-[(1S)-3-amino-1-cyano-3-oxopropyl]-N2-[(4'-fluoro[1,1'-biphenyl]-4-yl)methyl]-N2-(methanesulfonyl)-L-alaninamide
Homo sapiens
pH 7.4, 37°C
0.0000045
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1,3-dihydroisoindol-2-ylcarbonyl)propenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0002
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1,3-dihydroisoindol-2-ylcarbonyl)propenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0003
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1,3-dihydroisoindol-2-ylcarbonyl)propenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0005
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000018
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2,3-dihydroindol-1-ylcarbonyl)propenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00005
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2,3-dihydroindol-1-ylcarbonyl)propenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2,3-dihydroindol-1-ylcarbonyl)propenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000025
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-1H-quinolin-2-ylcarbonyl)propenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-1H-quinolin-2-ylcarbonyl)propenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0002
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-1H-quinolin-2-ylcarbonyl)propenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000035
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-2H-quinolin-1-ylcarbonyl)propenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000004
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-2H-quinolin-1-ylcarbonyl)propenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-2H-quinolin-1-ylcarbonyl)propenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000075
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00025
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0008
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-phenyl-5,6-dihydro-2H-pyridin-1-ylcarbonyl)propenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000085
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-phenyl-5,6-dihydro-2H-pyridin-1-ylcarbonyl)propenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00075
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-phenyl-5,6-dihydro-2H-pyridin-1-ylcarbonyl)propenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000055
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000035
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00005
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0006
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000018
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000005
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00006
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0002
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00000055
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000055
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0009
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-bis-(2-furylmethyl)carbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.005
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-bis-(2-furylmethyl)carbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.015
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-bis-(2-furylmethyl)carbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000023
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000012
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000045
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00009
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00045
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00055
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.002
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0027
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000045
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000045
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000031
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00035
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0006
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00002
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00008
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-3-(N-methyl-N-(1-(N-methyl-N-phenethylcarbamoyl)phenylethyl)carbamoylpropenoyl)hydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0003
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-3-(N-methyl-N-(1-(N-methyl-N-phenethylcarbamoyl)phenylethyl)carbamoylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00075
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-3-(N-methyl-N-(1-(N-methyl-N-phenethylcarbamoyl)phenylethyl)carbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00006
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000006
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000062
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000006
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000008
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00007
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000005
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
Trichomonas vaginalis
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.000038
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.0000028
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
Ixodes ricinus
-
0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
0.00001
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
Schistosoma mansoni
-
in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
additional information
Ixodes ricinus
IC50 concentration of the aza-peptide Michael acceptor Aza-Asn-11a in a range of about 500 nM determined
-
additional information
additional information
Ixodes ricinus
-
IC50 concentration of the aza-peptide Michael acceptor Aza-Asn-11a in a range of about 500 nM determined
-
additional information
additional information
Hordeum vulgare
-
inhibitory doses for 50% proteinase activity inhibition higher for root legumain activity than for endosperm one
-
additional information
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E)-4-oxo-4-phenylbut-2-enoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
Trichomonas vaginalis
IC50 is above 0.01 mM, in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E)-4-oxo-4-phenylbut-2-enoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
Ixodes ricinus
-
IC50 is above 0.02 mM, 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E)-4-oxo-4-phenylbut-2-enoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
Schistosoma mansoni
-
no inhibition after 20 min of preincubation with inhibitor in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E,4E)-hexa-2,4-dienoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
Schistosoma mansoni
-
no inhibition after 20 min of preincubation with inhibitor in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2-furyl)propenoyl)hydrazine
Schistosoma mansoni
-
IC50 is above 0.002 mM, in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
Schistosoma mansoni
-
IC50 is above 0.002 mM, in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
Ixodes ricinus
-
IC50 is above 0.15 mM, 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
Trichomonas vaginalis
IC50 is below 0.000001 mM, in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
Ixodes ricinus
-
IC50 is below 0.000001 mM, 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
Schistosoma mansoni
-
no inhibition after 20 min of preincubation with inhibitor in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
Ixodes ricinus
-
IC50 is below 0.000001 mM, 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
IC50 is below 0.000001 mM, in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Trichomonas vaginalis
IC50 is below 0.000001 mM, in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Trichomonas vaginalis
IC50 is below 0.000001 mM, in 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 6.8, 0.01 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
Ixodes ricinus
-
IC50 is below 0.000001 mM, 0.1 M citrate phosphate, 4 mM dithiothreitol, pH 5.5, 0.1 mM Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin as substrate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000133
hydrolysis of substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methyl-coumaryl-7-amide
0.00041
hydrolysis of substrate acetyl-aspartyl-asparaginyl-leucyl-aspartic acid alpha-(4-methylcoumaryl-7-amide)
0.642
recombinant protein, 37°C, pH 7, benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide, activity profile shown, inhibition assay described, up-regulation by the host blood-feeding process shown by in vitro proteolysis assay
8.1
-
purified enzyme, substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide, pH 5.8, 30°C
additional information
additional information
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay described, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing indicated
additional information
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay described, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing indicated
additional information
-
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay described, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing indicated
additional information
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing
additional information
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing
additional information
-
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing
additional information
ability of carboxy-terminal extensions and mutants of phytocystatin to inhibit in vitro human legumain shown, inhibitory activity measured by the inhibition of legumain proteinase activity, assay described
additional information
-
ability of carboxy-terminal extensions and mutants of phytocystatin to inhibit in vitro human legumain shown, inhibitory activity measured by the inhibition of legumain proteinase activity, assay described
additional information
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
-
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed, human monocyte legumain activity assay described, migration/proliferation and invasion assay described
additional information
-
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed, human monocyte legumain activity assay described, migration/proliferation and invasion assay described
additional information
positional scanning combinatorial library of peptide acyloxymethyl ketones (AOMKs) to probe subsite specificity of legumain, design of fluorescent activity-based probes indicating high selectivity and cell-permeability for monitoring legumain activity in complex proteome structures, selectivity of optimized legumain probes in intact cells shown, structure of developed probes indicated
additional information
-
positional scanning combinatorial library of peptide acyloxymethyl ketones (AOMKs) to probe subsite specificity of legumain, design of fluorescent activity-based probes indicating high selectivity and cell-permeability for monitoring legumain activity in complex proteome structures, selectivity of optimized legumain probes in intact cells shown, structure of developed probes indicated
additional information
role of legumain in the pathophysiology of atherosclerosis analyzed, human monocyte legumain activity assay described, migration/proliferation and invasion assay described
additional information
-
role of legumain in the pathophysiology of atherosclerosis analyzed, human monocyte legumain activity assay described, migration/proliferation and invasion assay described
additional information
-
HEK-293 serum-starved cells show a slight 1.2fold increase in enzymatic activity toward carbobenzyloxy-Ala-Ala-Asn-amido-4-methyl coumarin compared to that of nonstarved 293 HEK cells, while PC-3 serum-starved or nonstarved cells shows no significant difference in enzymatic activity
additional information
-
HEK-293-overexpressing legumain cells cleave 100% of the prodrug carbobenzyloxy-Ala-Ala-Asn-ethylenediamine-etoposide, whereas HEK-293 cells, which express low levels of legumain, cleave only 33% of it
additional information
-
ability of carboxy-terminal extensions and mutants of phytocystatin to inhibit endogenous legumain activity present in barley protein extracts analyzed, inhibitory activity measured by the inhibition of legumain proteinase activity, assay described
additional information
activity profile shown, specificity profile using a positional scanning synthetic combinatorial library indicated
additional information
-
activity profile shown, specificity profile using a positional scanning synthetic combinatorial library indicated
additional information
assay of legumain activity described, fibronectin degradation by legumain shown, enhanced fibronectin processing by overexpression of legumain indicated, experimental design of unilateral ureteral obstruction reveals increased protein accumulation of fibronectin in the renal interstitial area in kidneys from legumain-deficient mice
additional information
-
assay of legumain activity described, fibronectin degradation by legumain shown, enhanced fibronectin processing by overexpression of legumain indicated, experimental design of unilateral ureteral obstruction reveals increased protein accumulation of fibronectin in the renal interstitial area in kidneys from legumain-deficient mice
additional information
expression determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
-
expression determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
-
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
-
asparaginyl endopeptidase deficiency provokes extramedullary hematopoiesis in the spleen and abnormally enlarged histiocytes with ingested red blood cells in bone marrow
additional information
-
asparaginyl endopeptidase depletion evidently enhances the phagocytic activity, suggesting that phagocytic activity of macrophages in asparaginyl endopeptidase-/- mice is elevated
additional information
-
disruption of asparaginyl endopeptidase leads to late endosomes and lysosomes augmentation and dislocation from the apical region of the kidney-proximal tubule cells and the abnormal lysosomes contained in electron-dense or membranous materials
additional information
-
in contrast to the enhanced macrophage activity, the natural killer cell activity in the asparaginyl endopeptidase-null animal is significantly reduced
additional information
-
mutant mice lacking asparaginyl endopeptidase develop fever, cytopenia, hepatosplenomegaly and hemophagocytosis, which are primary pathological manifestations of hemophagocytic syndrome/hemophagocytic lymphohistiocytosis
additional information
-
myeloid cells are also increased in the asparaginyl endopeptidase-null mice, e.g. 10.2% in asparaginyl endopeptidase-null mice versus 1.2% in wild-type
additional information
-
red blood cells from asparaginyl endopeptidase-null mice are defective in plasma membrane components
additional information
-
the liver is significantly enlarged in asparaginyl endopeptidase deficient mice as compared with the normal counterparts
additional information
-
the percentage of Ter-119+/CD45+ erythroid lineage cells in the spleen is increased in the asparaginyl endopeptidase-deficient mice, e.g. 18.2% in a representative asparaginyl endopeptidase-null mouse compared with just 0.4% in a wild type control
additional information
-
the processing of the lysosomal proteases cathepsins in kidney is completely defective in asparaginyl endopeptidase-deficient mice with accumulation of macromolecules in the lysosomes, which is typically seen in lysosomal disorders
additional information
-
the spleens from asparaginyl endopeptidase-null mice are 5-10times larger than those of wild type controls
additional information
-
involvement of legumain in backbone cyclization of plant-produced cyclotides determined, transient expression of precursor of the cyclotide kalata B1 in tobacco leads to production of the circular cyclotide, in vivo asparaginyl bond hydrolysis shown to be necessary for cyclization, reduced amounts of cyclic cyclotide shown by suppression of legumain either by decreasing gene expression or by a specific inhibitor, detection and quantification of cyclotide proteins by MALDI-TOF
additional information
-
involvement of legumain in backbone cyclization of plant-produced cyclotides analyzed, assay for asparaginyl bond hydrolysis in leaf extracts described
additional information
the specific activity of recombinant asparaginyl endopeptidase is lower than that detected for excretory-secretory products of adult worm
additional information
-
the specific activity of recombinant asparaginyl endopeptidase is lower than that detected for excretory-secretory products of adult worm
additional information
cleavage sites for N- and C-terminus indicated, predicted motif for vacuolar proteins analyzed, targeting ability sucessfully tested in Saccharum officinarum and in other plant species by transient expression analysis after biolistic bombardment using the construct pCvsEndoexp1
additional information
expression of the SmAE gene in adult Schistosoma mansoni suppressed by RNA interference, full processing and activity of cathepsin B1 in the absence of detectable SmAE protein observed, experimental data indicate that schistosome legumain is not essential to activate cathepsin B1 in vivo
additional information
-
expression of the SmAE gene in adult Schistosoma mansoni suppressed by RNA interference, full processing and activity of cathepsin B1 in the absence of detectable SmAE protein observed, experimental data indicate that schistosome legumain is not essential to activate cathepsin B1 in vivo
additional information
-
involvement of legumain in backbone cyclization of plant-produced cyclotides analyzed, assay for asparaginyl bond hydrolysis in leaf extracts described
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 5.5
5.4
5.5
5.6
5.8
6.5
-
recombinant legumain cleaves carbobenzyloxy-Ala-Ala-Asn-amido-4-methyl coumarin more potently at pH 6.5 than at pH 5.0
7.5
additional information
4
Legumain activity shows a pH optimum of 4.0 towards substrates with Asp at the P1 position
5.4
activity assay at, maximum of activity observed at pH 5-6
5.4
activity assay at, maximum of activity observed at pH 56
5.4
-
with substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
5.5
Legumain activity shows a pH optimum of 5.5 towards substrates with Asn at the P1 position: maximum activity towards substrate benzoyl-L-Arg-4-nitroanilide is observed at pH 5.5
7
-
recombinant enzymes digested hemoglobin and bovine serum albumin optimally at pH 7
7
the rHlLgm2 is more active in neutral to slightly alkaline condition
7.5
biphasic pH optima with peaks at pH 4 (about 70% activity) and pH 7.5 (100% activity)
7.5
biphasic pH optima with peaks at pH 4 (about 70% activity) and pH 7.5 (100% activity)
additional information
legumain activity is pH-dependent and substrate-dependent
additional information
-
aza-peptide Michael acceptors react with dithiothreitol in the assay buffer at variable rates depending on pH and the nature of the substituents on the double bond, lowering the pH of the assay decreases the rate of reactivity dramatically
additional information
-
aza-peptide Michael acceptors react with dithiothreitol in the assay buffer at variable rates depending on pH and the nature of the substituents on the double bond, lowering the pH of the assay decreases the rate of reactivity dramatically
additional information
aza-peptide Michael acceptors react with dithiothreitol in the assay buffer at variable rates depending on pH and the nature of the substituents on the double bond, lowering the pH of the assay decreases the rate of reactivity dramatically
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
3.5 - 8
4 - 6
5.5 - 7
at neutral pH, full-length legumain remains stable with no indication of proteolytic processing. Shifting the pH to 5.5 the C-terminal propeptide Asp324-Tyr433 is cleaved within 20 h at 37°C
additional information
2 - 7
assay under different pH conditions tested in 0.2 M sodium citrate/citric acid, 1 mM DTT at 37°C, no enzyme activity observed at pH 4 and below, activity dropped to 55% at pH 7
2 - 7
assay under different pH conditions tested in 0.2 M sodium citrate/citric acid, 1 mM DTT at 37°C, no enzyme activity observed at pH 4 and below, activity drops to 55% at pH 7
additional information
-
rHlLgm and rHlLgm2 are active at neutral to alkaline pH
additional information
-
asparaginyl endopeptidase activation requires sequential removal of C- and N-terminal propeptides at different pH thresholds
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
high activity (90%) is observed at 30°C, while a gradual loss of activity is observed after the prolonged exposure to higher temperatures
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
encoded by the HlLgm gene; parthenogenetic Okayama strain
SwissProt
brenda
gene leg-1; barber pole worm, parasitic nematode
SwissProt
brenda
no endogenous cyclotides, transiently transformed with the cyclotide kalata B1
-
-
brenda
endogenous cyclotides as potential substrates for backbone cyclization by legumain analyzed
-
-
brenda
encoded by VPE-1 gene; sugarcane, transgenic plants regenerated from callus culture
SwissProt
brenda
endogenous cyclotides as potential substrates for backbone cyclization by legumain analyzed
-
-
brenda
4 genes, 3 of them encoded in a cluster, 2 isoforms of vegetative vacuolar processing enzymes alpha-VPE and beta-VPE
-
-
brenda
legumain-1, differentiated from legumain-2 by N-terminal sequence; collected from bile ducts and gall bladders of naturally infected cattle
SwissProt
brenda
legumain-2, differentiated from legumain-1 by N-terminal sequence; collected from bile ducts and gall bladders of naturally infected cattle
SwissProt
brenda
encoded by the HlLgm gene; parthenogenetic Okayama strain
SwissProt
brenda
14-week-old male C57BL/6J wild-type and legumain-deficient mice analyzed
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
specific for
brenda
lesions at the aortic sinus and in injured carotid arteries of Apolipoprotein E deficient mice, mRNA expression increases with development of atherosclerosis in the aorta
brenda
legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer
brenda
for generation of transformed plants, GFP reporter analysis indicated
brenda
inflamed areas in advanced human coronary atherosclerotic plaques
brenda
-
attached to storage-protein substrates in ER bodies
brenda
legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer
brenda
human umbilical vascular endothelial cells (HUVECs) tested in migration/proliferation and invasion assays
brenda
-
gene TcLeg3 shows an accumulation of transcripts for all analyzed tissues. It is least expressed in the root, which is used as calibrator (1.00X), and is most expressed in the seed (21.7X) and tegument (21.5X). Expression in tegument (21.5X), seed (21.7X), leaf (9.9X), and stalk (17.8X). The TcLeg9 gene shows expression in all organs and tissues analyzed. The leaf is the organ with the highest expression (25.5X) as compared to the calibrator (root). Statistically significant differences are observed in the tegument (4.7X), leaf (25.6X), and stalk (19.0X) as compared to the expression in the root (1.00X)
brenda
caecal epithelium, 2-6 week old juveniles and adults, mRNA expression also in metacercariae
brenda
-
LGMN expression is increased in hepatocellular carcinoma cells relative to normal hepatocytes in the same specimens
brenda
legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer
brenda
legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer
brenda
-
gene TcLeg3 shows an accumulation of transcripts for all analyzed tissues. It is least expressed in the root, which is used as calibrator (1.00X), and is most expressed in the seed (21.7X) and tegument (21.5X). Expression in tegument (21.5X), seed (21.7X), leaf (9.9X), and stalk (17.8X). The TcLeg9 gene shows expression in all organs and tissues analyzed. The leaf is the organ with the highest expression (25.5X) as compared to the calibrator (root). Statistically significant differences are observed in the tegument (4.7X), leaf (25.6X), and stalk (19.0X) as compared to the expression in the root (1.00X)
brenda
control plants and transformed plants, GFP reporter analysis indicated
brenda
additional information
legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer
brenda
inhibitory effects by phytocystatins against commercial human legumain analyzed
brenda
-
developing endosperms of 18 days after flowering, inhibitory effects by cystatins against endogenous legumain activity in barley protein extracts analyzed
brenda
anthere only
brenda
anthere, ovules, filaments
brenda
expression in, localized in digestive vesicles of gut cells and within the peritrophic matrix, function associated with the degradation of host hemoglobin suggested
brenda
exclusively expressed in the gut tissue. IsAE1 is the principle legumain transcript in partially engorged females, and demonstrates its strong regulation by on-host feeding in larvae, nymphs and females. IsAE1 is the most highly expressed gut-specific legumain in blood fed ticks where it predominated over all its paralogues
brenda
IsAE2 is the predominant gut legumain in unfed nymphs, unfed females and males
brenda
protein from kidney tissues used for western blot analysis, unilateral ureteral obstruction in legumain-deficient mice
brenda
-
leaf extracts, assay for asparaginyl bond hydrolysis in, analysis of backbone cyclization of endogenous cyclotides in
brenda
-
in the leaf tissue the Leg1 is the highest expressed isoform, followed by Leg3
brenda
-
gene TcLeg3 shows an accumulation of transcripts for all analyzed tissues. It is least expressed in the root, which is used as calibrator (1.00X), and is most expressed in the seed (21.7X) and tegument (21.5X). Expression in tegument (21.5X), seed (21.7X), leaf (9.9X), and stalk (17.8X). The TcLeg9 gene shows expression in all organs and tissues analyzed. The leaf is the organ with the highest expression (25.5X) as compared to the calibrator (root). Statistically significant differences are observed in the tegument (4.7X), leaf (25.6X), and stalk (19.0X) as compared to the expression in the root (1.00X)
brenda
M-CSF differentiated primary macrophages, in vitro expression, also detected in the culture media
brenda
of atherosclerotic aorta of aging Apolipoprotein E deficient mice, mRNA expression increases with development of atherosclerosis
brenda
lmidgut epithelium shown by immunohistochemistry
brenda
-
lmidgut epithelium shown by immunohistochemistry
-
brenda
fluorimetric assay measuring legumain protease activity applied
brenda
RAW264.7 monocyte lysate utilized for monitoring endogenous legumain by designed activity-based probes, lysates from 816 B cells used for detection assay of endogenous legumain
brenda
-
collected from plants germinated at 22°C in the dark for 7 days
brenda
-
in root tissues the isoform Leg1 has the greatest mRNA levels, whereas Leg2 has the lowest ones
brenda
-
gene TcLeg3 shows an accumulation of transcripts for all analyzed tissues. It is least expressed in the root, which is used as calibrator (1.00X), and is most expressed in the seed (21.7X) and tegument (21.5X). Expression in tegument (21.5X), seed (21.7X), leaf (9.9X), and stalk (17.8X). The TcLeg9 gene shows expression in all organs and tissues analyzed. The leaf is the organ with the highest expression (25.5X) as compared to the calibrator (root). Statistically significant differences are observed in the tegument (4.7X), leaf (25.6X), and stalk (19.0X) as compared to the expression in the root (1.00X)
brenda
-
gene TcLeg3 shows an accumulation of transcripts for all analyzed tissues. It is least expressed in the root, which is used as calibrator (1.00X), and is most expressed in the seed (21.7X) and tegument (21.5X). Expression in tegument (21.5X), seed (21.7X), leaf (9.9X), and stalk (17.8X). The TcLeg9 gene shows expression in all organs and tissues analyzed. The leaf is the organ with the highest expression (25.5X) as compared to the calibrator (root). Statistically significant differences are observed in the tegument (4.7X), leaf (25.6X), and stalk (19.0X) as compared to the expression in the root (1.00X). TcLeg6 is only expressed in the stages of seed development. No transcripts of TcLeg6 gene are detected in the analysis of the mature seed (quiescent) and germinating cotyledon
brenda
additional information
-
VPE isoforms are also found during stress response of plant organ, e.g. wounded leaves, the precursor enzyme is synthesized at membrane-bound polysomes in the cytoplasm
brenda
additional information
-
the alpha and gamma vacuolar processing enzyme occurs only in vegetative organs
brenda
additional information
-
legumain is not detected in salivary glands, ovaries, cuticles, tracheae, Malpighian tubules and synganglia
brenda
additional information
tissue distribution, low expression level in all tissues tested, no expression in MG63 osteosarcoma cells
brenda
additional information
-
tissue distribution, low expression level in all tissues tested, no expression in MG63 osteosarcoma cells
brenda
additional information
-
expression of enzyme in healthy and in cancer cells, the expression is increased in cancer cells, overview
brenda
additional information
in all vegetative organs, the precursor enzyme is synthesized at membrane-bound polysomes in the cytoplasm
brenda
additional information
tissue-specific and developmental expression patterns, overview
brenda
additional information
tissue-specific and developmental expression patterns, overview
brenda
additional information
tissue-specific and developmental expression patterns, overview
brenda
additional information
tissue-specific and developmental expression patterns, overview
brenda
additional information
tissue-specific and developmental expression patterns, overview
brenda
additional information
tissue-specific and developmental expression patterns, overview
brenda
additional information
tissue-specific and developmental expression patterns, overview
brenda
additional information
-
tissue-specific and developmental expression patterns, overview
brenda
additional information
-
the precursor enzyme is synthesized at membrane-bound polysomes in the cytoplasm
brenda
additional information
-
the precursor enzyme is synthesized at membrane-bound polysomes in the cytoplasm
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
special proteinase-storage vesicle that contain the enzyme precursor, which is probably packed together with its storage-protein substrates
brenda
crude worm protein extracts but not in excretion-secretion products of adult parasites, polyclonal antisera and activity assay
brenda
additional information
the enzyme is secreted into the digestive tract of host animals
-
brenda
the enzyme is secreted into the digestive tract of host animals
-
brenda
-
the alpha and gamma vacuolar processing enzyme occurs only in vegetative organs, while the beta VPE occurs in seeds
brenda
-
PrVPE1 localizes to a reticulate compartment resembling the vacuole
brenda
vacuoles within the sugarcane storage parenchyma tissue, bioinformatical studies on vacuolar targeting, GFP-constructs sucessfully targeted to lytic vacuolar compartments of Saccharum officinarum
brenda
additional information
proenzyme is probably attached to its storage-protein substrates
-
brenda
additional information
-
proenzyme is probably attached to its storage-protein substrates
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
for sufficient functionality, recombinant legumain-1 needs trans-activation through Dictyocaulus viviparus cathepsin L-2. Since recombinant legumain-1 needs trans-activation through a cathepsin, it is probably involved in an enzyme cascade and therefore remains interesting as a candidate in a multi-component vaccine
physiological function
malfunction
-
knockdown of LGMN by siRNA decreases proliferation of SKHep1 cells by 50% as measured both by BrdU uptake and mitotic index, although an inhibitor of LGMN activity does not affect BrdU incorporation. A significant reduction in the fraction of cells in G2/M phase is seen. This is associated with increases in the expression of cyclins A and E
malfunction
-
in pathological settings, such as cancer or Alzheimer's disease, the proper association of legumain activities with the corresponding cellular compartments is breached
physiological function
-
nuclear Ca2+ signals regulate cell proliferation in part through the modulation ofLGMN expression
physiological function
cleavage of acetoacetyl-CoA synthetase by legumain is critical for the regulation of enzymatic activity and results in gain-of-function changes
physiological function
important roles in immunity, cancer, and neurodegenerative diseases
physiological function
important roles in many physiological processes, including programmed cell death
physiological function
legumain promotes cell migration and its overexpression is associated with enhanced tissue invasion and metastasis. It promotes tumorigenesis and correlates with poor prognosis in different cancer types
physiological function
-
plant legumains are key enzymes in the processing and activation of seed storage proteins during seed maturation. Plants legumains are important components of the immune system. Plant legumains are discussed as main mediators of programmed cell death
physiological function
potential role of legumain in differential substrate recognition during endolysosomal maturation
physiological function
-
TcLeg3 may be related to the mobilization of reserve proteins
physiological function
-
TcLeg9 is related to development and defense against pathogens
Show AA Sequence and Transmembrane Helices (1004 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
31000
32000
34000
35000
36000
37000
38000
38100
x * 38100, mature enzyme, SDS-PAGE, x * 53400, pre-proenzyme, SDS-PAGE
45000
46000
47000
49000
50000
53400
x * 38100, mature enzyme, SDS-PAGE, x * 53400, pre-proenzyme, SDS-PAGE
56000
75000
x * 49000, about, amino acid sequence calculation, x * 75000, recombinant GST-fusion enzyme, SDS-PAGE
31000
-
x * 34000, glycosylated enzyme, SDS-PAGE, x * 31000, deglycosylated enzyme, SDS-PAGE
31000
x * 31000, SDS-PAGE, x * 50000, amino acid sequence calculation of the proenzyme
32000
x * 32000, SDS-PAGE, x * 50000, amino acid sequence calculation
32000
x * 32000, SDS-PAGE, x * 50000, amino acid sequence calculation of the proenzyme
32000
x * 32000, SDS-PAGE, no signals after RNA interference of the SMAE gene encoding schistosome legumain
34000
-
x * 34000, glycosylated enzyme, SDS-PAGE, x * 31000, deglycosylated enzyme, SDS-PAGE
38000
removal of a peptide of 9000 Dalton from the preprotein
38000
endogenous HlLgm2, predicted and confirmed by SDS-PAGE and immunoblot analysis
46000
-
non-mature, active form, determined by SDS-PAGE and Westen blot analysis
46000
x * 46000, recombinant enzyme from Escherichia coli, SDS-PAGE, x * 50000, native wild-type and recombinant enzyme from 293 cells, SDS-PAGE
49000
x * 49000, about, amino acid sequence calculation, x * 75000, recombinant GST-fusion enzyme, SDS-PAGE
50000
x * 46000, recombinant enzyme from Escherichia coli, SDS-PAGE, x * 50000, native wild-type and recombinant enzyme from 293 cells, SDS-PAGE
50000
x * 31000, SDS-PAGE, x * 50000, amino acid sequence calculation of the proenzyme
50000
x * 32000, SDS-PAGE, x * 50000, amino acid sequence calculation
50000
x * 32000, SDS-PAGE, x * 50000, amino acid sequence calculation of the proenzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 49000, about, amino acid sequence calculation, x * 75000, recombinant GST-fusion enzyme, SDS-PAGE
?
x * 46000, recombinant enzyme from Escherichia coli, SDS-PAGE, x * 50000, native wild-type and recombinant enzyme from 293 cells, SDS-PAGE
?
x * 38100, mature enzyme, SDS-PAGE, x * 53400, pre-proenzyme, SDS-PAGE
?
x * 31000, SDS-PAGE, x * 50000, amino acid sequence calculation of the proenzyme
?
x * 32000, SDS-PAGE, x * 50000, amino acid sequence calculation
?
x * 32000, SDS-PAGE, x * 50000, amino acid sequence calculation of the proenzyme
?
x * 32000, SDS-PAGE, no signals after RNA interference of the SMAE gene encoding schistosome legumain
?
-
x * 34000, glycosylated enzyme, SDS-PAGE, x * 31000, deglycosylated enzyme, SDS-PAGE
additional information
-
comparison of the tertiary structure of the enzyme with other cysteine endopeptidases
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no glycoprotein
but enzyme contains 1 putative N-glycosylation site at N326
proteolytic modification
glycoprotein
presence of at least two glycosylation sites on the mature protease. Glycosylation of prolegumain is necessary for correct processing to active forms and internalization
glycoprotein
C-terminal hexa-His-tag is cleaved off together with the pro-peptide
glycoprotein
4 potential N-glycosylation sites at Asn91, ASn167, Asn263, and Asn272
glycoprotein
the enzyme harbours 4 N-glycosylation sites resulting in a molecular weight of about 56000 Da of the fully glycosylated proenzyme
glycoprotein
potential N-linked glycosylation sites (NXS/T) are detected at Asn-68 and Asn-173
glycoprotein
-
4 potential N-glycosylation sites at Asn91, ASn167, Asn263, and Asn272
proteolytic modification
-
autocatalytic processing of inactive proenzyme to the active mature enzyme by removal of C- and N-terminally propeptides, activation takes place in the vacuole or cell wall after fusion with the ER bodies
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
mechanisms of autoactivation, including a plant-specific two-chain activation state, which remains conformationally stable at neutral pH, which is a prerequisite for full ligase activity and survival in different cell compartments
proteolytic modification
activation of the recombinant legumain is autocatalytic and triggered by acidic pH
proteolytic modification
-
Both recombinant legumain expressed in yeast and endogenous legumain are able to be converted into active protein of approximately 37 kDa via a C-terminal autocleavage at acid pH values
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
N-terminal and C-terminal cleavage sites predicted, N-terminal sequence
proteolytic modification
N-terminal and C-terminal cleavage sites predicted, N-terminal sequence indicated
proteolytic modification
cleavage site at asparagines 364-365 at the C-terminus identified in endogenous and in recombinant protein
proteolytic modification
the values expected on the basis of the predicted MW indicating that post-translational processing of HlLgm2 occurred during biosynthesis to form a mature protein through removal of 9 kDa peptides from the precursor protein, putative C-terminal autocleavage at site Asn364-365
proteolytic modification
-
cleavage site at asparagines 364-365 at the C-terminus identified in endogenous and in recombinant protein
-
proteolytic modification
-
autocatalytic activation by cleavage of aspartic acid residues, overview
proteolytic modification
-
the 56 kDa proform is cleavaed to the active 46 kDa and 36 kDa forms
proteolytic modification
legumain is synthesized as a zymogen und undergoes pH-dependent autoproteolytic activation. All but one of the autocatalytic cleavage events occur in trans, with only the release of the C-terminal propeptide being relevant to enzymatic activity. Legumain matures to the fully active form (super-activation) only when incubated at pH 4.0
proteolytic modification
human prolegumain starts with a signal peptide (Met1-Ala17) that is released during trafficking, followed by a short 8 amino acid N-terminal propeptide (Val18-Asp25), the cysteine protease domain (Gly26-Asn323) and a C-terminal prodomain (Asp324-Tyr433)
proteolytic modification
the optimum pH for the autocatalytic activation of recombinant legumain is very acidic at a pH value of 3
proteolytic modification
C-terminus, in endogenous and in recombinant protein
proteolytic modification
autocatalytic processing of inactive proenzyme to the active mature enzyme by removal of C- and N-terminally propeptides, activation takes place in the vacuole or cell wall
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
-
autocatalytic processing of inactive proenzyme to the active mature enzyme by removal of C- and N-terminally propeptides, activation takes place in the vacuole or cell wall, precursor is cleaved at sites containing Asn residues at the P1 position
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
C-terminus, in endogenous and in recombinant protein
proteolytic modification
-
three-dimensional modeling shows that the propeptide, which is located in the terminal C region of legumains blocks the catalytic cleft
proteolytic modification
-
autocatalytic processing of inactive proenzyme to the active mature enzyme by removal of C- and N-terminally propeptides, activation takes place in the vacuole or cell wall after fusion with the ER bodies
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
super-activated legumain is crystallized in complex with the legumain-specific inhibitor Ala-Ala-Asn-chloromethylketone to resolution of 2.47 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C189S
dead mutant: in contrast to the wild-type protein, no evidence for the additional C-terminal cleavage after Asp303/309 is found
D303E/D309E
double mutant in which the pH 4-dependent cleavage site is disrupted
DELTA18-25
N-terminal truncation variant lacking the N-terminal propeptide [DELTA-(Val18-Asp25)] is created. The activity of this variant resembles that of the wild-type protein and it is inactive in the unprocessed form (Gly26-Tyr433) at pH 7.0 or pH 5.5. Like the wild-type protein, the truncation variant undergoes correct maturation at pH 5.5 to the Gly26-Asn323 form, confirming correct folding of the protein
H150A
-
site-directed mutagenesis, adaptation of the mouse sequence to the human one by introduction of a silent mutation A152S, 4fold less effective expressionin HEK 293 cells compared to wild-type, completely inactive
N197C
-
site-directed mutagenesis, the mutation renders the enzyme of Sm32 active
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 5.5
the thermal stability of active legumain is highest in the pH interval 4.0-5.5, with a melting temperature Tm of 60°C. At pH values higher than 6.0 the melting temperature Tm decreased to below 30°C
717046
6
the isolated enzyme becomes irreversibly denatured at pH values above 6.0
731134
7
-
no enzymatic activity at pH 7.0, legumain undergoes denaturation at these basic conditions
696499
additional information
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C to -20°C, pH 5.8, 0.05 M sodium citrate, 0.2 M NaCl, 1 mM EDTA, 10 mm cysteine, 0.1% CHAPS, stable for several months with little loss of activity
-
4°C, 50 mM sodium citrate-buffered saline, pH 5.0, 2 mM 2-mercaptoethanol, a few weeks, stable
4°C, purified native enzyme from kidney, pH 5.8, little loss of activity over several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography (glutathione-Sepharose)
native enzyme from dry seeds, to homogeneity
native enzyme from germinated seeds, to homogeneity
recombinant enzyme is purified by affinity chromatography using His-Trap nickel columns
recombinant His-tagged enzyme from Escherichia coli, gel filtration and SDS-PAGE
recombinant His-tagged enzyme from Escherichia coli, SDS-PAGE
recombinant protein is purified using Ni-Sepharos under native conditions
SDS-PAGE
soluble recombinant C197 from Pichia pastoris, native enzyme to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AEP -/-, +/- and +/+ mice on a mixed 129/Ola and C57BL/6 background are generated
-
C-terminal hexa-His-tagged is expressed in the yeast Pichia pastoris
DNA and amino acid sequence determination and analysis
DNA sequence and structure determination and analysis, expression in mammalian cells
-
DNA sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli BL21, stable expression in 293 cells and secretion to the medium
embryonic kidney cells are stably transfected with human legumain to achieve overexpression in vitro, HEK-Leg cells expressed both active and inactive legumain and secreted it to the medium
-
expressed in Escherichia coli
expressed in Escherichia coli, RNA interference applied to silence expression of the SmAE gene encoding schistosome legumain
expressed in Pichia pastoris
expression as beta-galactosidase fusion protein in Escherichia coli, the recombinant enzyme shows hemoglobinase activity, the N197 enzyme form might not be the active one, but the C197 form
expression of C197 in Pichia pastoris, expression as beta-galactosidase fusion protein in Escherichia coli, the recombinant enzyme shows hemoglobinase activity, the N197 enzyme form might not be the active one, but the C197 form
expression of inactive precursor enzyme in yeast and insect cells, expression of a processing-site mutant in yeast and subsequent in vitro processing study
-
expression of vegetative enzyme in seeds and of seed enzyme in stamen, phylogenetic tree
gene leg-1, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree, expression in Escherichia coli as GST-fusion protein
gene PRSC1, DNA and amino acid sequence determination and analysis, localization on chromosome 14q32.1, expression in insect cells
-
gene SPAE or Y192, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression of His-tagged enzyme
glutathione S-transferase-fusion protein expressed in Escherichia coli BL21(DE3)
in Escherichia coli, Champion-pET directional expression kit, pET100/D-TOPO expression vector, functionally expression of recombinant protein in Pichia pastoris, expression vector pPICZaB
in Escherichia coli, construct pCvsEndoexp1 transformed into callus derived from Q117 meristematic tissue, transgenic plants regenerated
inserted in pET20b(+), transformed into the Escherichia coli BL21(DE3)pLysS strain
Pichia pastoris expression system can produce highly active recombinant legumain protein allowing it to be used for high-throughput screening applications
plasmid pTrcHisB/HlLgm transformed into the Escherichia coli Top10F0 strain
recombinant Ov-AEP-1 is expressed as hexa-His tag in Escherichia coli in inclusion bodies
transient expression under control of the CMV promotor of wild-type and mutant enzymes in human embryonic kidney HEK 293 cells, all recombinant enzymes are processed normally
-
glutathione S-transferase-fusion protein expressed in Escherichia coli BL21(DE3)
glutathione S-transferase-fusion protein expressed in Escherichia coli BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
bafilomycin A1 enhances the secretion of the the enzyme, which is also is up-regulated in tumour and tumour-associated cells
-
expression levels of legumain mRNA and protein and legumain activity are increased in DJ-1-knockout cells. Legumain expression and activation is regulated by DJ-1 through p53
in the cotyledons of germinating seeds, the accumulation of transcripts of gene TcLeg3 decreases 90fold from the initial time (quiescent seed) to the 30th day
-
in the cotyledons of germinating seeds, the TcLeg9 expression rises from time zero to the 20th day, with an approximate 64fold increase as compared to the control
-
IsAE1 expression was strongly upregulated by feeding when the mRNA levels in unfed and fully fed samples are compared. However, IsAE1 mRNA is also detectable at relatively high levels in unfed larvae, almost comparable with fully fed females
isoform Leg-2 mRNA expression responds in leaves to biotic and abiotic stimuli, such as salicylic acid, jasmonic acid, nitric oxide, abscisic acid, and aphid infestation, and is induced by gibberellic acid in seeds. Isoform Leg-4 responds in leaves to wounding, nitric oxide, and abscisic acid treatments
-
isoform Leg1 mRNA is strongly induced in senescent leaves. Wounding is capable of inducing all the four expressed genes Leg1, 2, 3 and 4. Inthe leaf tissues there is a high increase in the expression of Leg2 and Leg4 after 24 h of the abscisic acid treatment, while for Leg1 an increase in the mRNA levels is observed in 4 h and decreases in 24 h after treatment. Isoform Leg4 mRNA levels increase with nicotinamide
-
isoform Leg4 mRNA levels do not increase when the plants are submitted to NaCl
-
legumain expression is increased during monocyte-to-macrophage differentiation
-
legumain mRNA is down-regulated in monocytes isolated from patients treated with atorvastatin
-
LGMN expression is increased in hepatocellular carcinoma cells relative to normal hepatocytes in the same specimens
-
the enzyme expression is down-regulated in plantlets treated with salicylic acid
the enzyme expression is up-regulated in plantlets treated with abscisic acid
when Ca2+ is buffered in the nucleus of SKHep1 cells, LGMN mRNA is decreased by 97%, in part by a transcriptional mechanism, and decreased expression at the protein level is observed by immunoblot and immunofluorescence
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
to obtain bioactive recombinant protein, the protein isolated in its denatured form is refolded by stepwise dialysis (1 M urea increments every 24 h) against phosphate buffered saline, pH 7.4
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
studies on vacuolar targeting, targeting motif of legumain as a potential tool for plant engineering analyzed
diagnostics
potential for serodiagnosis of human opisthorchiasisas immunodiagnostic antigen
drug development
-
enzyme serves as a promising candidate for prodrug tumor therapy
medicine
medicine
since recombinant legumain-1 needs trans-activation through a cathepsin, it is probably involved in an enzyme cascade and therefore remains interesting as a candidate in a multi-component vaccine
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baumgartner, B.; Chrispeels, M.J.
Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings
Eur. J. Biochem.
77
223-233
1977
Vigna radiata
brenda
Csoma, C.; Polgar, L.
Proteinase from germinating bean cotyledons. Evidence for involvement of a thiol group in catalysis
Biochem. J.
222
769-776
1984
Phaseolus vulgaris
brenda
Ishii, S.I.
Legumain: asparaginyl endopeptidase
Methods Enzymol.
244
604-615
1994
Canavalia ensiformis
brenda
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
J. Biol. Chem.
268
3525-3529
1993
Canavalia ensiformis
brenda
Takeda, O.; Miura, Y.; Mitta, M.; Matsushita, H.; Kato, I.; Abe, Y.; Yokosawa, H.; Ishii, S.
Isolation and analysis of cDNA encoding a precursor of Canavalia ensiformis asparaginyl endopeptidase (legumain)
J. Biochem.
116
541-546
1994
Canavalia ensiformis
brenda
Kembhavi, A.A.; Buttle, D.J.; Knight, C.G.; Barrett, A.J.
The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assays
Arch. Biochem. Biophys.
303
208-213
1993
Vigna aconitifolia
brenda
Scott, M.P.; Jung, R.; Muntz, K.; Nielsen, N.C.
A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean
Proc. Natl. Acad. Sci. USA
89
658-662
1992
Glycine max
brenda
Hara-Nishimura, I.; Inoue, K.; Nishimura, M.
A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms
FEBS Lett.
294
89-93
1991
Ricinus communis
brenda
Dando, P.M.; Fortunato, M.; Smith, L.; Knight, C.G.; McKendrick, J.E.; Barrett, A.J.
Pig kidney legumain: an asparaginyl endopeptidase with restricted
Biochem. J.
339
743-749
1999
Sus scrofa
-
brenda
Yamane, T.; Takeuchi, K.; Yamamoto, Y.; Li, Y.H.; Fujiwara, M.; Nishi, K.; Takahashi, S.; Ohkubo, I.
Legumain from bovine kidney: its purification, molecular clonin, immunohistochemical localization and degradation of annexin II and vitamin D-binding protein
Biochim. Biophys. Acta
1596
108-120
2002
Bos taurus (Q95M12), Bos taurus
brenda
Chen, J.M.; Fortunato, M.; Stevens, R.A.E.; Barrett, A.J.
Activation of progelatinase A by mammalian lugumain, a recently discovered cysteine proteinase
Biol. Chem.
382
777-783
2001
Homo sapiens, Sus scrofa
brenda
Rotari, V.I.; Dando, P.M.; Barrett, A.J.
Legumain forms from plants and animals differ in their specificity
Biol. Chem.
382
953-959
2001
Phaseolus vulgaris, Sus scrofa
brenda
Niestroj, A.J.; Feuner, K.; Heiser, U.; Dando, P.M.; Barrett, A.J.; Gerhartz, B.; Demuth, H.U.
Inhibition of mammalian legumain by Michael acceptors and AzaAsn-halomethylketones
Biol. Chem.
383
1205-1214
2002
Sus scrofa
brenda
Schwarz, G.; Brandenburg, J.; Reich, M.; Burster T.; Driessen, C.; Kalbacher, H.
Characterization of legumain
Biol. Chem.
383
1813-1816
2002
Sus scrofa
brenda
Loak, K.; Li, D.N.; Manoury, B.; Billson, J.; Morton, F.; Hewitt, E.; Watts, C.
Novel cell-permeable acyloxymethylketone inhibitors of asparaginyl endopeptidase
Biol. Chem.
384
1239-1246
2003
Homo sapiens
brenda
Senyuk, V.; Rotari, V.; Becker, C.; Zakharov, A.; Hortmann, C.; Mntz, K.; Vaintraub, I.
Does an asparaginyl-specific cysteine endopeptidase trigger phaseolin degradation in cotyledons of kidney bean seedlings ?
Eur. J. Biochem.
258
546-558
1998
Phaseolus vulgaris (O24325), Phaseolus vulgaris
brenda
Halfon, S.; Patel, S.; Vega, F.; Zurawski, S.; Zurawski, G.
Autocatalytic activation of human legumain at aspartic acid residues
FEBS Lett.
438
114-118
1998
Homo sapiens, Mus musculus (O89017), Mus musculus
brenda
Chen, J.M.; Rawlings, N.D.; Stevens, R.A.E.; Barrett, A.J.
Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of endopeptidases
FEBS Lett.
441
361-365
1998
Mus musculus
brenda
Chen, J.M.; Dando, P.M.; Rawlings, N.D.; Brown, M.A.; Young, N.E.; Stevens, R.A.; Hewitt, E.; Watts, C.; Barrett, A.J.
Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase
J. Biol. Chem.
272
8090-8098
1997
Sus scrofa, Homo sapiens (Q99538), Homo sapiens
brenda
Alvarez-Fernandez, M.; Barrett, A.J.; Gerhartz, B.; Dando, P.M.; Ni, J.; Abrahamson, M.
Inhibition of mammalian legumain by some cystatins is due too a novel second reactive site
J. Biol. Chem.
274
19195-19203
1999
Sus scrofa
brenda
Choi, S.J.; Reddy, S.V.; Devlin, R.D.; Menaa, C.; Chung, H.; Boyce, B.B.; Roodman, G.D.
Identification of human asparaginyl endopeptidase (legumain) as an inhibitor of osteoclast formation and bone resorption
J. Biol. Chem.
274
27747-27753
1999
Homo sapiens (Q99538), Homo sapiens
brenda
Mathieu, M.A.; Bogyo, M.; Caffrey, C.R.; Choe, Y.; Lee, J.; Chapman, H.; Sajid, M.; Craik, C.S.; McKerrow, J.H.
Substrate specificity of schistosome versus human legumain determined by P1-P3 peptide libraries
Mol. Biochem. Parasitol.
121
99-105
2002
Homo sapiens, Schistosoma mansoni
brenda
Mntz, K.; Shutov, A.D.
Legumains and their functions in plants
Trends Plant Sci.
2
1360-1385
2002
Arabidopsis thaliana, Canavalia ensiformis, Ricinus communis, Vicia sativa, Nicotiana tabacum (Q9XG75)
-
brenda
Murthy, R.V.; Arbman, G.; Gao, J.; Roodman, G.D.; Sun, X.F.
Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer
Clin. Cancer Res.
11
2293-2299
2005
Homo sapiens
brenda
Wolk, K.; Gruetz, G.; Witte, K.; Volk, H.D.; Sabat, R.
The expression of legumain, an asparaginyl endopeptidase that controls antigen processing, is reduced in endotoxin-tolerant monocytes
Genes Immun.
6
452-456
2005
Homo sapiens
brenda
Chen, J.; Dando, P.M.; Barrett, A.J.
Mammalian legumain
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1302-1305
2004
Homo sapiens, Mus musculus, Sus scrofa
-
brenda
Brindley, P.J.; Dalton, J.P.
Schistosome legumain
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1305-1310
2004
Schistosoma mansoni (P09841), Schistosoma mansoni (Q9NFY9), Schistosoma japonicum (P42665), Homo sapiens (Q99538)
-
brenda
Hara-Nishimura, I.
Plant legumain, asparaginyl endopeptidase
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1310-1313
2004
Arabidopsis thaliana, Canavalia ensiformis, Ricinus communis, Glycine max, Vigna mungo, Phaseolus vulgaris, Vigna aconitifolia
-
brenda
Zakharov, A.; Muentz, K.
Seed legumains are expressed in stamens and vegetative legumains in seeds of Nicotiana tabacum L
J. Exp. Bot.
55
1593-1595
2004
Nicotiana tabacum (Q707T9), Nicotiana tabacum (Q852T0), Nicotiana tabacum (Q852T1), Nicotiana tabacum (Q852T2), Nicotiana tabacum (Q852T3), Nicotiana tabacum (Q9XG75), Nicotiana tabacum (Q9XG76), Nicotiana tabacum
brenda
Chen, H.J.; Hou, W.C.; Liu, J.S.; Yang, C.Y.; Huang, D.J.; Lin, Y.H.
Molecular cloning and characterization of a cDNA encoding asparaginyl endopeptidase from sweet potato (Ipomoea batatas (L.) Lam) senescent leaves
J. Exp. Bot.
55
825-835
2004
Ipomoea batatas (Q9M4R6), Ipomoea batatas
brenda
Maehr, R.; Hang, H.C.; Mintern, J.D.; Kim, Y.M.; Cuvillier, A.; Nishimura, M.; Yamada, K.; Shirahama-Noda, K.; Hara-Nishimura, I.; Ploegh, H.L.
Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice
J. Immunol.
174
7066-7074
2005
Mus musculus
brenda
Vigneswaran, N.; Wu, J.; Nagaraj, N.; James, R.; Zeeuwen, P.; Zacharias, W.
Silencing of cystatin M in metastatic oral cancer cell line MDA-686Ln by siRNA increases cysteine proteinases and legumain activities, cell proliferation and in vitro invasion
Life Sci.
78
898-907
2006
Homo sapiens
brenda
Oliver, E.M.; Skuce, P.J.; McNair, C.M.; Knox, D.P.
Identification and characterization of an asparaginyl proteinase (legumain) from the parasitic nematode, Haemonchus contortus
Parasitology
133
237-244
2006
Haemonchus contortus (Q2UVF3), Haemonchus contortus
brenda
Martinez, M.; Diaz-Mendoza, M.; Carrillo, L.; Diaz, I.
Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases
FEBS Lett.
581
2914-2918
2007
Hordeum vulgare, Homo sapiens (Q99538), Homo sapiens
brenda
Clerin, V.; Shih, H.H.; Deng, N.; Hebert, G.; Resmini, C.; Shields, K.M.; Feldman, J.L.; Winkler, A.; Albert, L.; Maganti, V.; Wong, A.; Paulsen, J.E.; Keith, J.C.; Vlasuk, G.P.; Pittman, D.D.
Expression of the cysteine protease legumain in vascular lesions and functional implications in atherogenesis
Atherosclerosis
201
53-66
2008
Mus musculus (O89017), Mus musculus, Homo sapiens (Q99538), Homo sapiens
brenda
Sexton, K.B.; Witte, M.D.; Blum, G.; Bogyo, M.
Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain
Bioorg. Med. Chem. Lett.
17
649-653
2007
Homo sapiens (Q99538), Homo sapiens
brenda
Morita, Y.; Araki, H.; Sugimoto, T.; Takeuchi, K.; Yamane, T.; Maeda, T.; Yamamoto, Y.; Nishi, K.; Asano, M.; Shirahama-Noda, K.; Nishimura, M.; Uzu, T.; Hara-Nishimura, I.; Koya, D.; Kashiwagi, A.; Ohkubo, I.
Legumain/asparaginyl endopeptidase controls extracellular matrix remodeling through the degradation of fibronectin in mouse renal proximal tubular cells. [Erratum to document cited in CA146:460121]
FEBS Lett.
581
3579
2007
Mus musculus (O89017), Mus musculus
brenda
Jackson, M.A.; Rae, A.L.; Casu, R.E.; Grof, C.P.; Bonnett, G.D.; Maclean, D.J.
A bioinformatic approach to the identification of a conserved domain in a sugarcane legumain that directs GFP to the lytic vacuole
Funct. Plant Biol.
34
633-644
2007
Saccharum officinarum (Q0ZHB0)
brenda
Abdul Alim, M.; Tsuji, N.; Miyoshi, T.; Khyrul Islam, M.; Huang, X.; Motobu, M.; Fujisaki, K.
Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis
Insect Biochem. Mol. Biol.
37
911-922
2007
Haemaphysalis longicornis (A4PF00), Haemaphysalis longicornis, Haemaphysalis longicornis Okayama (A4PF00)
brenda
Sojka, D.; Hajdusek, O.; Dvorak, J.; Sajid, M.; Franta, Z.; Schneider, E.L.; Craik, C.S.; Vancova, M.; Buresova, V.; Bogyo, M.; Sexton, K.B.; McKerrow, J.H.; Caffrey, C.R.; Kopacek, P.
IrAE: an asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus
Int. J. Parasitol.
37
713-724
2007
Ixodes ricinus (Q6PRC7), Ixodes ricinus
brenda
Saska, I.; Gillon, A.D.; Hatsugai, N.; Dietzgen, R.G.; Hara-Nishimura, I.; Anderson, M.A.; Craik, D.J.
An asparaginyl endopeptidase mediates in vivo protein backbone cyclization
J. Biol. Chem.
282
29721-29728
2007
Nicotiana benthamiana, Viola tricolor, Oldenlandia affinis
brenda
Adisakwattana, P.; Viyanant, V.; Chaicumpa, W.; Vichasri-Grams, S.; Hofmann, A.; Korge, G.; Sobhon, P.; Grams, R.
Comparative molecular analysis of two asparaginyl endopeptidases and encoding genes from Fasciola gigantica
Mol. Biochem. Parasitol.
156
102-116
2007
Fasciola gigantica (A6Y9U8), Fasciola gigantica (A6Y9U9), Fasciola gigantica
brenda
Krautz-Peterson, G.; Skelly, P.J.
Schistosome asparaginyl endopeptidase (legumain) is not essential for cathepsin B1 activation in vivo
Mol. Biochem. Parasitol.
159
54-58
2008
Schistosoma mansoni (P09841), Schistosoma mansoni
brenda
Stern, L.; Perry, R.; Ofek, P.; Many, A.; Shabat, D.; Satchi-Fainaro, R.
A novel antitumor prodrug platform designed to be cleaved by the endoprotease legumain
Bioconjug. Chem.
20
500-510
2009
Homo sapiens
brenda
Laha, T.; Sripa, J.; Sripa, B.; Pearson, M.; Tribolet, L.; Kaewkes, S.; Sithithaworn, P.; Brindley, P.J.; Loukas, A.
Asparaginyl endopeptidase from the carcinogenic liver fluke, Opisthorchis viverrini, and its potential for serodiagnosis
Int. J. Infect. Dis.
12
49-59
2008
Opisthorchis viverrini (Q208S4), Opisthorchis viverrini
brenda
Alim, M.A.; Tsuji, N.; Miyoshi, T.; Islam, M.K.; Huang, X.; Hatta, T.; Fujisaki, K.
HlLgm2, a member of asparaginyl endopeptidases/legumains in the midgut of the ixodid tick Haemaphysalis longicornis, is involved in blood-meal digestion
J. Insect Physiol.
54
573-585
2008
Haemaphysalis longicornis (A9CQC1), Haemaphysalis longicornis
brenda
Goetz, M.G.; James, K.E.; Hansell, E.; Dvorak, J.; Seshaadri, A.; Sojka, D.; Kopacek, P.; McKerrow, J.H.; Caffrey, C.R.; Powers, J.C.
Aza-peptidyl Michael acceptors. A new class of potent and selective inhibitors of asparaginyl endopeptidases (legumains) from evolutionarily diverse pathogens
J. Med. Chem.
51
2816-2832
2008
Schistosoma mansoni, Ixodes ricinus, Trichomonas vaginalis (Q6EHZ7)
brenda
Alim, M.A.; Tsuji, N.; Miyoshi, T.; Islam, M.K.; Hatta, T.; Yamaji, K.; Fujisaki, K.
Developmental stage- and organ-specific expression profiles of asparaginyl endopeptidases/legumains in the ixodid tick Haemaphysalis longicornis
J. Vet. Med. Sci.
70
1363-1366
2008
Haemaphysalis longicornis
brenda
Ledgard, A.M.; Lee, R.S.; Peterson, A.J.
Bovine endometrial legumain and TIMP-2 regulation in response to presence of a conceptus
Mol. Reprod. Dev.
76
65-74
2009
Bos taurus (Q95M12), Bos taurus
brenda
Chan, C.B.; Abe, M.; Hashimoto, N.; Hao, C.; Williams, I.R.; Liu, X.; Nakao, S.; Yamamoto, A.; Li, S.Y.; Hara-Nishimura, I.; Asano, M.; Ye, K.
Mice lacking asparaginyl endopeptidase develop disorders resembling hemophagocytic syndrome
Proc. Natl. Acad. Sci. USA
106
468-473
2009
Mus musculus
brenda
Briggs, J.; Haugen, M.; Johansen, H.; Riker, A.; Abrahamson, M.; Fodstad, .; Mlandsmo, G.; Solberg, R.
Cystatin E/M suppresses legumain activity and invasion of human melanoma
BMC Cancer
10
17
2010
Homo sapiens
brenda
Lee, J.; Bogyo, M.
Development of near-infrared fluorophore (NIRF)-labeled activity-based probes for in vivo imaging of legumain
Chem. Biol.
5
233-243
2010
Mus musculus
brenda
Wu, B.; Yin, J.; Texier, C.; Roussel, M.; Tan, K.S.
Blastocystis legumain is localized on the cell surface, and specific inhibition of its activity implicates a pro-survival role for the enzyme
J. Biol. Chem.
285
1790-1798
2010
Blastocystis sp. BW-2009a (C1K3M8), Blastocystis hominis (D1M8Z4)
brenda
Ovat, A.; Muindi, F.; Fagan, C.; Brouner, M.; Hansell, E.; Dvorak, J.; Sojka, D.; Kopacek, P.; McKerrow, J.H.; Caffrey, C.R.; Powers, J.C.
Aza-peptidyl Michael acceptor and epoxide inhibitors--potent and selective inhibitors of Schistosoma mansoni and Ixodes ricinus legumains (asparaginyl endopeptidases)
J. Med. Chem.
52
7192-7210
2009
Schistosoma mansoni, Ixodes ricinus
brenda
Dall, E.; Brandstetter, H.
Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profile
Acta Crystallogr. Sect. F
68
24-31
2012
Homo sapiens (Q99538)
brenda
Lee, J.; Bogyo, M.
Synthesis and evaluation of aza-peptidyl inhibitors of the lysosomal asparaginyl endopeptidase, legumain
Bioorg. Med. Chem. Lett.
22
1340-1343
2011
Homo sapiens, Mus musculus
brenda
Teng, L.; Wada, H.; Zhang, S.
Identification and functional characterization of legumain in amphioxus Branchiostoma belcheri
Biosci. Rep.
30
177-186
2010
Branchiostoma belcheri
brenda
Andrade, V.; Guerra, M.; Jardim, C.; Melo, F.; Silva, W.; Ortega, J.M.; Robert, M.; Nathanson, M.H.; Leite, F.
Nucleoplasmic calcium regulates cell proliferation through legumain
J. Hepatol.
55
626-635
2011
Homo sapiens
brenda
Bosch, M.; Poulter, N.S.; Perry, R.M.; Wilkins, K.A.; Franklin-Tong, V.E.
Characterization of a legumain/vacuolar processing enzyme and YVADase activity in Papaver pollen
Plant Mol. Biol.
74
381-393
2010
Papaver rhoeas
brenda
Dall, E.; Fegg, J.C.; Briza, P.; Brandstetter, H.
Structure and mechanism of an aspartimide-dependent peptide ligase in human legumain
Angew. Chem. Int. Ed. Engl.
54
2917-2921
2015
Homo sapiens (Q99538), Homo sapiens
brenda
Smith, R.; Johansen, H.T.; Nilsen, H.; Haugen, M.H.; Pettersen, S.J.; Maelandsmo, G.M.; Abrahamson, M.; Solberg, R.
Intra- and extracellular regulation of activity and processing of legumain by cystatin E/M
Biochimie
94
2590-2599
2012
Homo sapiens
brenda
Solberg, R.; Smith, R.; Almloef, M.; Tewolde, E.; Nilsen, H.; Johansen, H.T.
Legumain expression, activity and secretion are increased during monocyte-to-macrophage differentiation and inhibited by atorvastatin
Biol. Chem.
396
71-80
2015
Homo sapiens
brenda
Julian, I.; Gandullo, J.; Santos-Silva, L.K.; Diaz, I.; Martinez, M.
Phylogenetically distant barley legumains have a role in both seed and vegetative tissues
J. Exp. Bot.
64
2929-2941
2013
Hordeum vulgare
brenda
Pierre, O.; Hopkins, J.; Combier, M.; Baldacci, F.; Engler, G.; Brouquisse, R.; Herouart, D.; Boncompagni, E.
Involvement of papain and legumain proteinase in the senescence process of Medicago truncatula nodules
New Phytol.
202
849-863
2014
Medicago truncatula
brenda
Santos-Silva, L.K.; Soares-Costa, A.; Gerald, L.T.; Meneghin, S.P.; Henrique-Silva, F.
Recombinant expression and biochemical characterization of sugarcane legumain
Plant Physiol. Biochem.
57
181-192
2012
Saccharum sp. (H2EUL5)
brenda
Christoff, A.P.; Turchetto-Zolet, A.C.; Margis, R.
Uncovering legumain genes in rice
Plant Sci.
215-216
100-109
2014
Oryza sativa
brenda
Hasegawa, S.; Inoue, D.; Yamasaki, M.; Li, C.; Imai, M.; Takahashi, N.; Fukui, T.
Site-specific cleavage of acetoacetyl-CoA synthetase by legumain
FEBS Lett.
590
1592-1601
2016
Mus musculus (O89017), Mus musculus
brenda
Elsaesser, B.; Zauner, F.B.; Messner, J.; Soh, W.T.; Dall, E.; Brandstetter, H.
Distinct roles of catalytic cysteine and histidine in the protease and ligase mechanisms of human legumain as revealed by DFT-based QM/MM simulations
ACS Catal.
7
5585-5593
2017
Homo sapiens (Q99538), Homo sapiens
brenda
Yamane, T.; Yamamoto, Y.; Nakano, Y.; Nakagaki, T.; Ohkubo, I.; Ariga, H.
Expression and protease activity of mouse legumain are regulated by the oncogene/transcription co-activator, DJ-1 through p53 and cleavage of annexin A2 is increased in DJ-1-knockout cells
Biochem. Biophys. Res. Commun.
467
472-477
2015
Mus musculus (O89017), Mus musculus
brenda
Dall, E.; Brandstetter, H.
Structure and function of legumain in health and disease
Biochimie
122
126-150
2016
Mammalia, unidentified plant, Schistosoma mansoni (P09841), Bos taurus (Q95M12), Homo sapiens (Q99538), Homo sapiens
brenda
Lunde, N.N.; Haugen, M.H.; Bodin Larsen, K.B.; Damgaard, I.; Pettersen, S.J.; Kasem, R.; Rut, W.; Drag, M.; Poreba, M.; Johansen, H.T.; Solberg, R.
Glycosylation is important for legumain localization and processing to active forms but not for cystatin E/M inhibitory functions
Biochimie
139
27-37
2017
Bos taurus (Q95M12), Bos taurus
brenda
Ness, K.A.; Eddie, S.L.; Higgins, C.A.; Templeman, A.; DCosta, Z.; Gaddale, K.K.; Bouzzaoui, S.; Jordan, L.; Janssen, D.; Harrison, T.; Burkamp, F.; Young, A.; Burden, R.; Scott, C.J.; Mullan, P.B.; Williams, R.
Development of a potent and selective cell penetrant Legumain inhibitor
Bioorg. Med. Chem. Lett.
25
5642-5645
2015
Homo sapiens (Q99538)
brenda
Ness, K.A.; Eddie, S.L.; Burton, S.; Harrison, T.; Mullan, P.; Williams, R.
Flat SAR of P3-methylsulphonamide based small molecule legumain inhibitors
Bioorg. Med. Chem. Lett.
26
413-416
2016
Homo sapiens (Q99538)
brenda
Eddie, S.L.; Gregson, A.; Graham, E.; Burton, S.; Harrison, T.; Burden, R.; Scott, C.J.; Mullan, P.B.; Williams, R.
Identification and SAR exploration of a novel series of legumain inhibitors
Bioorg. Med. Chem. Lett.
29
1546-1548
2019
Homo sapiens (Q99538)
brenda
Vidmar, R.; Vizovisek, M.; Turk, D.; Turk, B.; Fonovic, M.
Protease cleavage site fingerprinting by label-free in-gel degradomics reveals pH-dependent specificity switch of legumain
EMBO J.
36
2455-2465
2017
Homo sapiens (Q99538)
brenda
Hartmann, D.; Sima, R.; Konvickova, J.; Perner, J.; Kopacek, P.; Sojka, D.
Multiple legumain isoenzymes in ticks
Int. J. Parasitol.
48
167-178
2018
Ixodes scapularis, Ixodes scapularis (A0A1S6XZC8)
brenda
Nourrisson, C.; Wawrzyniak, I.; Cian, A.; Livrelli, V.; Viscogliosi, E.; Delbac, F.; Poirier, P.
On Blastocystis secreted cysteine proteases a legumain-activated cathepsin B increases paracellular permeability of intestinal Caco-2 cell monolayers
Parasitology
143
1713-1722
2016
Blastocystis hominis (D8M176)
brenda
Holzhausen, J.; Haake, C.; Schicht, S.; Hinse, P.; Jordan, D.; Kremmer, E.; Strube, C.
Biological function of Dictyocaulus viviparus asparaginyl peptidase legumain-1 and its suitability as a vaccine target
Parasitology
145
378-392
2018
Dictyocaulus viviparus (I6R478), Dictyocaulus viviparus
brenda
Zauner, F.B.; Dall, E.; Regl, C.; Grassi, L.; Huber, C.G.; Cabrele, C.; Brandstetter, H.
Crystal structure of plant legumain reveals a unique two-chain state with pH-dependent activity regulation
Plant Cell
30
686-699
2018
Arabidopsis thaliana (Q39119), Arabidopsis thaliana
brenda
Santana, J.O.; Freire, L.; de Sousa, A.O.; Fontes Soares, V.L.; Gramacho, K.P.; Pirovani, C.P.
Characterization of the legumains encoded by the genome of Theobroma cacao L
Plant Physiol. Biochem.
98
162-170
2016
Theobroma cacao
brenda
Zhao, T.; Li, Z.; Guo, Z.; Wang, A.; Liu, Z.; Zhao, Q.; Li, Y.; McKenzie, E.A.; Diao, A.
Functional recombinant human Legumain protein expression in Pichia pastoris to enable screening for Legumain small molecule inhibitors
Protein Expr. Purif.
150
12-16
2018
Homo sapiens (Q99538), Homo sapiens
brenda
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