Information on EC 3.4.22.34 - Legumain

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The expected taxonomic range for this enzyme is: Eukaryota

SplaateEC_Number,Commentary
EC NUMBER
COMMENTARY
3.4.22.34
-
SplaateRecommended_Name,GO_Number
RECOMMENDED NAME
GeneOntology No.
Legumain
-
SplaateReaction,Reaction_id,Commentary,IF(Commentary != '',Organism,'') ,IF(Commentary != '',Literature,'')
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
show the reaction diagram
; 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
show the reaction diagram
the enzyme contains essential catalytic His and Cys residues
-
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
show the reaction diagram
active site His151; active site His151 and Cys197
SplaateReaction_Type,Organism,Commentary,Literature
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
SplaatePathway,BRENDA_Link,KEGG_Link,MetaCyc_Link,Source_Database
SplaateSystematic_Name,Commentary_IUBMB
SplaateSynonyms,Organism,Commentary,Literature
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AEP
-
-
Antigen Sj32
-
-
-
-
Antigen SM32
-
-
-
-
As-specific vacuolar cysteine proteinase
-
-
Asn-specific vacuolar cysteine proteinase
-
-
Asn-specific vacuolar cysteine proteinase
-
Asn-specific vacuolar cysteine proteinase
-
-
asparagine endopeptidase
-
-
asparagine endopeptidase
-
asparagine endopeptidase
-
-
asparagine endopeptidase
-
-
asparagine endopeptidase
-
asparaginly endopeptidase
-
-
asparaginyl endopepidase
-
-
Asparaginyl endopeptidase
-
-
-
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
Haemaphysalis longicornis Okayama
-
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
-
Asparaginyl endopeptidase
-
Asparaginyl endopeptidase
-
-
asparaginyl endopeptidase legumain
-
-
asparaginyl endopeptidase,
-
-
asparaginyl proteinase
-
asparaginyl-specific cysteine endopeptidase
-
asparagyl-endopeptidase
-
-
aspartate-specific endopeptidase
-
-
Bean endopeptidase
-
-
-
-
cysteine protease 1
-
IrAE protein
-
Leg-2
-
isoform
Leg-4
-
isoform
Leg1
-
isoform
Leg2
-
isoform
Leg3
-
isoform
Leg4
-
isoform
Leg5
-
isoform
legumain
-
legumain
-
-
LGMN
-
-
lysosomal asparaginycysteine endopeptidase
-
-
lysosomal asparaginyl endopeptidase
-
-
osteoclast inhibitory peptide 2
-
-
Phaseolin
-
-
-
-
Proteinase B
-
-
-
-
PrVPE1
-
-
schistosome legumain
-
schistosome legumain
-
schistosome legumain
-
vacuolar processing enzyme
-
-
vacuolar processing enzyme
-
-
vacuolar processing enzyme
-
-
vacuolar processing enzyme
-
vacuolar processing enzyme
-
-
vacuolar processing enzyme 1a
-
vacuolar processing enzyme 1b
-
vacuolar processing enzyme 2
-
vacuolar processing enzyme 3
-
Vicilin peptidohydrolase
-
-
-
-
lysosomal cysteine proteinase
-
-
additional information
-
the enzyme belongs to the C13 peptidase family
additional information
belongs to the peptidase family C13
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
additional information
the enzyme belongs to the C13 peptidase family
additional information
-
belongs to the peptidase family C13
additional information
-
the enzyme belongs to the C13 peptidase family
SplaateCAS_Registry_Number,Commentary
CAS REGISTRY NUMBER
COMMENTARY
149371-18-6
-
SplaateOrganism, Commentary,Literature, Sequence_Code,Sequence_db,Textmining
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
4 genes, 3 of them encoded in a cluster, 2 isoforms of vegetative vacuolar processing enzymes alpha-VPE and beta-VPE
-
-
Manually annotated by BRENDA team
legumain-1, differentiated from legumain-2 by N-terminal sequence; collected from bile ducts and gall bladders of naturally infected cattle
SwissProt
Manually annotated by BRENDA team
legumain-2, differentiated from legumain-1 by N-terminal sequence; collected from bile ducts and gall bladders of naturally infected cattle
SwissProt
Manually annotated by BRENDA team
encoded by the HlLgm gene; parthenogenetic Okayama strain
SwissProt
Manually annotated by BRENDA team
Haemaphysalis longicornis Okayama
encoded by the HlLgm gene; parthenogenetic Okayama strain
SwissProt
Manually annotated by BRENDA team
gene leg-1; barber pole worm, parasitic nematode
SwissProt
Manually annotated by BRENDA team
; Homo sapiens
Swissprot
Manually annotated by BRENDA team
Homo sapiens
Swissprot
Manually annotated by BRENDA team
cultivar Bomi
-
-
Manually annotated by BRENDA team
legumain activity in barley protein extracts analyzed
-
-
Manually annotated by BRENDA team
gene SPAE or Y192
SwissProt
Manually annotated by BRENDA team
adult females
SwissProt
Manually annotated by BRENDA team
14-week-old male C57BL/6J wild-type and legumain-deficient mice analyzed
SwissProt
Manually annotated by BRENDA team
C57BL/6J mice and class II MHC-deficient mice
-
-
Manually annotated by BRENDA team
no endogenous cyclotides, transiently transformed with the cyclotide kalata B1
-
-
Manually annotated by BRENDA team
gene pb1
GenBank
Manually annotated by BRENDA team
gene pb2
SwissProt
Manually annotated by BRENDA team
gene pb3
SwissProt
Manually annotated by BRENDA team
gene VPE1a
SwissProt
Manually annotated by BRENDA team
gene VPE1b
SwissProt
Manually annotated by BRENDA team
gene VPE2
SwissProt
Manually annotated by BRENDA team
gene VPE3
SwissProt
Manually annotated by BRENDA team
endogenous cyclotides as potential substrates for backbone cyclization by legumain analyzed
-
-
Manually annotated by BRENDA team
legumain-like proteinase LLP
SwissProt
Manually annotated by BRENDA team
purfied enzyme
-
-
Manually annotated by BRENDA team
encoded by VPE-1 gene; sugarcane, transgenic plants regenerated from callus culture
SwissProt
Manually annotated by BRENDA team
sugarcane cultivar SP80-3280
UniProt
Manually annotated by BRENDA team
the enzyme contains a Cys at position 197
SwissProt
Manually annotated by BRENDA team
2 recombinant isoforms Sm32 and N197CSm32
-
-
Manually annotated by BRENDA team
fragment; from infected mice and humans
SwissProt
Manually annotated by BRENDA team
from infected mice and humans
SwissProt
Manually annotated by BRENDA team
product of the SmAE gene
SwissProt
Manually annotated by BRENDA team
moth bean
-
-
Manually annotated by BRENDA team
endogenous cyclotides as potential substrates for backbone cyclization by legumain analyzed
-
-
Manually annotated by BRENDA team
SplaateGeneral_Information, Organism, Commentary, Literature
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
-
nuclear Ca2+ signals regulate cell proliferation in part through the modulation ofLGMN expression
SplaateSubstrates,Products,id,Organism_Substrates,Commentary_Substrates, Literature_Substrates, Commentary_Products, Literature_Products,Reversibility
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
11S proglobulin + H2O
?
show the reaction diagram
-
degradation of unassembled proteins or misfolded precursors
-
-
?
11S proglobulin + H2O
?
show the reaction diagram
degradation of unassembled proteins or misfolded precursors
-
-
?
11S proglobulin + H2O
?
show the reaction diagram
-
processing to the active trimer
-
-
?
11S proglobulin + H2O
?
show the reaction diagram
processing to the active trimer
-
-
?
Ac-Asp-Asn-Leu-Asp alpha-(4-methylcoumaryl-7-amide) + H2O
Ac-Asp-Asn-Leu-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Ac-Tyr-Val-Ala-Asp-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Thr-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Pro-Thr-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
acetyl-Thr-Ala-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Thr-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide + H2O
acetyl-Tyr-Val-Ala-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
AGTHNGQIGA + H2O
AGTHN + GQIGA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived, low activity
-
?
AHIDNEEDIA + H2O
AHIDN + EEDIA
show the reaction diagram
-
low activity, the peptide sequence is also cleaved in tetanus toxoid C fragment of which it is derived
-
?
AHIDNESDIA + H2O
AHIDN + ESDIA
show the reaction diagram
-
low activity
-
?
ALKGNNLIWA + H2O
ALKGN + NLIWA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
allatotropin + H2O
?
show the reaction diagram
-
-
-
-
?
annexin II + H2O
?
show the reaction diagram
cleavage of the N-terminus, enzyme plays a role in inactivation and degradation of annexin II in endosomes and lysosomes
-
-
?
AQLKNITDYA + H2O
AQLKN + ITDYA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
AREDNNITLA + H2O
AREDN + NITLA
show the reaction diagram
-
low activity, the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
ARLYNGLKFA + H2O
ARLYN + GLKFA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
ASGFNSSVIA + H2O
ASGFN + SSVIA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
ATITNDRLSA + H2O
ATITN + DLRSA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
AYGTNEYSIA + H2O
AYGTN + EYSIA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
fragments of azocasein
show the reaction diagram
-
-
-
-
benzoyl-Asn-4-nitroanilide + H2O
benzoyl-Asn + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-Asn-4-nitroanilide + H2O
benzoyl-Asn + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-Asn-4-nitroanilide + H2O
benzoyl-Asn + 4-nitroaniline
show the reaction diagram
Bz-Asn-pNA, recombinant protein, at 37C
-
?
benzoyl-L-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
best synthetic substrate
-
?
Benzyloxycarbonyl-Ala 4-nitrophenyl ester + H2O
Benzyloxycarbonyl-Ala + 4-nitrophenol
show the reaction diagram
-
-
-
-
Benzyloxycarbonyl-Ala-Ala-Asn 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcouamrin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
best synthetic substrate
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
recombinant protein
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
activity of recombinant protein determined
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
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
show the reaction diagram
-
inhibitory activity of cystatin variants of Hordeum vulgare against endogenous legumain activity in protein extracts of Hordeum vulgare analyzed, 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
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Haemaphysalis longicornis Okayama
recombinant protein
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-metylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
benzyloxycarbonyl-Ala-Glu-Asn-Xaa-Ala-Glu-Lys-NH2 + H2O
benzyloxycarbonyl-Ala-Glu-Asn + Xaa-Ala-Glu-Lys-NH2
show the reaction diagram
-
substrate specificity at S1 position, overview
-
?
Benzyloxycarbonyl-Ala-Pro-Asn 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Ala-Pro-Tyr-Asn 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Asn nitrophenyl ester + H2O
Benzyloxycarbonyl-Asn + 4-nitrophenol
show the reaction diagram
-
-
-
-
Benzyloxycarbonyl-Gly 4-nitrophenyl ester + H2O
Benzyloxycarbonyl-Gly + 4-nitrophenol
show the reaction diagram
-
-
-
-
benzyloxycarbonyl-Gly-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Gly-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Gly-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
low activity
-
?
benzyloxycarbonyl-Ile-Ser-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ile-Ser-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
low activity with
-
?
benzyloxycarbonyl-Leu-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Leu-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
low activity
-
?
Benzyloxycarbonyl-Phe 4-nitrophenyl ester + H2O
Benzyloxycarbonyl-Phe + 4-nitrophenol
show the reaction diagram
-
-
-
-
benzyloxycarbonyl-Phe-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
low activity
-
?
Benzyloxycarbonyl-Pro-Ala-Asn 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-Pro-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Pro-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Pro-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Pro-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Pro-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Pro-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
low activity
-
?
Benzyloxycarbonyl-Tyr 4-nitrophenyl ester + H2O
Benzyloxycarbonyl-Tyr + 4-nitrophenol
show the reaction diagram
-
-
-
-
benzyloxycarbonyl-Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Tyr-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Tyr-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Tyr-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
low activity
-
?
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
fluorogenic substrate
-
?
Boc-Asn-4-nitrophenyl ester + H2O
Boc-Asn + 4-nitrophenol
show the reaction diagram
-
-
-
?
Boc-Asn-4-nitrophenyl ester + H2O
Boc-Asn + 4-nitrophenol
show the reaction diagram
-
-
-
?
bombesin + H2O
?
show the reaction diagram
-
-
-
-
?
bovine albumin + H2O
peptides containing C-terminal Asn
show the reaction diagram
-
-
?
bovine haemoglobin + H2O
peptides containing C-terminal Asn
show the reaction diagram
exhibited strict specificity for the asparaginyl bonds on the carboxy-terminal side of a peptide
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
Haemaphysalis longicornis, Haemaphysalis longicornis Okayama
degradation in a dose-dependent manner at pH 7 and 30C during 6 h of incubation, no cleavage detected at or above 37C, strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines shown
-
-
?
bovine serum albumin + H2O
3 fragments
show the reaction diagram
-
SDS-denatured substrate, cleavage site are at positions 324 and 404
-
?
carbobenzyloxy-Ala-Ala-Asn-ethylenediamine-etoposide + H2O
etoposide-ethylenediamine + carbobenzyloxy-Ala-Ala-Asn
show the reaction diagram
-
legumain releases the chemotherapeutic agent etoposide, as the active drug
-
?
casein + H2O
?
show the reaction diagram
-
-
-
?
casein 1 + H2O
2 fragments
show the reaction diagram
-
cleavage site is at position 95
-
?
cathepsin B proform + H2O
activated cathepsin B
show the reaction diagram
-
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
-
?
cathepsin B proform + H2O
activated cathepsin B
show the reaction diagram
trans-processing and activation of the zymogen form of Schistosoma mansoni cathepsin B1 indicated
-
?
cathepsin L + H2O
?
show the reaction diagram
-
processing/activation
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
CBZ-Ala-Ala-Asn-amino-4-methyl coumarin + H2O
CBZ-Ala-Ala-Asn + 7-amino-4-methyl coumarin
show the reaction diagram
-
-
-
?
Cbz-Ala-Ala-azaAsn-7-amido-4-methyl-coumarin + H2O
?
show the reaction diagram
-
-
-
-
?
chicken vasoactive intestinal peptide fragment 16-28 + H2O
?
show the reaction diagram
-
-
-
-
?
concanavalin A A-chain + H2O
3 fragments
show the reaction diagram
-
cleavage site are at positions 159 and 163
-
?
concanavalin A precursor + H2O
activated concanavalin A
show the reaction diagram
-
internal excision of the propeptide and transpeptidation that leads to the inverted fusion of the 2 fragments of the precursor
-
?
cystatin E + H2O
?
show the reaction diagram
-
-
-
-
?
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 + H2O
Dinitrophenyl-Pro-Glu-Ala-Asn + NH4OH
show the reaction diagram
-
-
-
-
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 + H2O
Dinitrophenyl-Pro-Glu-Ala-Asn + NH4OH
show the reaction diagram
-
-
-
-
Dnp-Pro-Glu-Ala-Asn-NH2 + H2O
Dnp-Pro-Glu-Ala-Asn + NH3
show the reaction diagram
-
-
-
?
ETRNGVEE + H2O
ETRN + GVEE
show the reaction diagram
-
-
-
?
Gelatin + H2O
Hydrolyzed gelatin
show the reaction diagram
-
-
-
-
gelatinase + H2O
gelatinase fragment
show the reaction diagram
-
62 kDa active form, cleavage site is Asn430
36 kDa active form
?
GSVKAYTNFDAERD + H2O
GSVKAYTN + FDAERD
show the reaction diagram
synthetic peptide, residues24-37, derived from the N-terminal sequence of bovine annexin II, cleavage at position N31-F32
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
the enzyme is involved in host hemoglobin degradation
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
the enzyme is involved in host hemoglobin degradation
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
the recombinant beta-galactosidase fusion enzyme shows hemoglobinase activity
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
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
?
show the reaction diagram
Haemaphysalis longicornis, Haemaphysalis longicornis Okayama
strict specificity for hydrolysis of the peptide on the carboxyl side of the asparagines indicated
-
-
?
human vasoactive intestinal peptide fragment 1-12 + H2O
?
show the reaction diagram
-
-
-
-
?
legumain + H2O
processed legumain + N-terminal and C-terminal prodomains
show the reaction diagram
-
autocatalysis
-
?
myelin basic protein + H2O
?
show the reaction diagram
-
-
-
-
?
myelin basic protein MBP + H2O
5 fragments
show the reaction diagram
-
cleavage sites at positions 84-85 and 92-93, multiple-sclerosis-associated autoantigen, digestion, destruction of the immunodominant epitope 83-99
product determination
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
specific cleavage
-
-
?
neurotensin fragment 1-11 + H2O
?
show the reaction diagram
-
-
-
-
?
octapeptides basing on the processing sites of 11S proglobulin + H2O
?
show the reaction diagram
-
-
-
-
?
papain-like cysteine proteinase precursors + H2O
activated papin-like cysteine proteinases
show the reaction diagram
-
cleavage of C-terminal propeptide, involved in the senescing of tissues and cell death
-
?
phaseolin + H2O
?
show the reaction diagram
initiation of phaseolin proteolysis, enyme plays a key role in mobilization of phaseolin during and after kidney bean germination
-
-
?
pig vasoactive intestinal peptide fragment 1-28 + H2O
?
show the reaction diagram
-
-
-
-
?
precursor of basic vacuolar chitinase + H2O
active basic vacuolar chitinase
show the reaction diagram
-
cleavage of C-terminal propeptide, involved in the senescing of tissues and cell death
-
?
progelatinase A + H2O
gelatinase
show the reaction diagram
-
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
?
progelatinase A + H2O
gelatinase
show the reaction diagram
-
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 A
show the reaction diagram
-
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
?
progelatinase A + H2O
gelatinase A + gelatinase K propeptide
show the reaction diagram
-
activation
-
?
Proglycinin + H2O
?
show the reaction diagram
-
cleavage takes place between the conserved Asn and Gly residues
-
-
-
Prolegumin + H2O
?
show the reaction diagram
-
cleavage takes place between the conserved Asn and Gly residues
-
-
-
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
?
protein + H2O
peptides
show the reaction diagram
-
an Asn residue at P1 position is strictly required
-
?
protein + H2O
peptides
show the reaction diagram
-
strong specificity for asparaginyl residues located at the protein surface
-
?
protein + H2O
peptides
show the reaction diagram
-
substrate specificity is dominated by the interaction of the S1 subsite
-
?
protein + H2O
peptides
show the reaction diagram
-
enzyme is critically involved in the lysosomal processing of bacterial antigens for MHC class II presentation
-
?
protein + H2O
peptides
show the reaction diagram
-
enzyme is involved in antigen presentation within class II MHC positive cells and in pro-protein processing
-
?
protein + H2O
peptides
show the reaction diagram
-
enzyme is involved mainly in storage protein breakdown
-
?
protein + H2O
peptides
show the reaction diagram
-
involved in mobilization of storage proteins and stress response processes
-
?
rat alpha1-macroglobulin + H2O
3 fragments
show the reaction diagram
-
cleavage site are at positions 721 and 899
-
?
recombinant C-fragment of tetanus toxoid + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
serum albumin + H2O
?
show the reaction diagram
-
-
-
?
SESENGLEET + H2O
SESEN + GLEET
show the reaction diagram
-
-
-
?
somatostatin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Tyr-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
succinyl-Tyr-Val-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
tert-butoxycarbonyl-Asn nitrophenyl ester + H2O
tert-butoxycarbonyl-Asn + 4-nitrophenol
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Asn nitrophenyl ester + H2O
tert-butoxycarbonyl-Asn + 4-nitrophenol
show the reaction diagram
-
-
-
-
Tert-Butoxycarbonyl-Gln 4-nitrophenyl ester + H2O
Tert-Butoxycarbonyl-Gln + 4-nitrophenol
show the reaction diagram
-
-
-
-
tetanus toxin + H2O
?
show the reaction diagram
-
-
-
-
?
tetanus toxoid C fragment + H2O
?
show the reaction diagram
-
cleavage site are at positions 26, 337, and 372
-
-
?
tetanus toxoid C fragment + H2O
3 fragments
show the reaction diagram
-
cleavage sites are at Asn26, Asn97, and Asn372, but not Asn337
-
?
tetanus toxoid C fragment + H2O
tetanus toxoid fragments
show the reaction diagram
-
cleavage sites are at Asn26, Asn337, and Asn372
-
?
transferrin + H2O
?
show the reaction diagram
-
-
-
?
transferrin + H2O
5 fragments
show the reaction diagram
-
cleavage site are at positions 95, 529, 574, and 603
-
?
Vasoactive intestinal peptide + H2O
?
show the reaction diagram
-
specific cleavage
-
-
?
Vicilin + H2O
Hydrolyzed vicilin
show the reaction diagram
-
-
-
-
Vicilin + H2O
?
show the reaction diagram
-
degradation of the principal reserve protein present in Vigna radiata seeds
-
-
-
vitamin D-binding protein + H2O
?
show the reaction diagram
cleavage sites are, besides others, N150-Y151, and N83-S84
-
-
?
vitamin D-binding protein + H2O
?
show the reaction diagram
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
show the reaction diagram
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Z-Ala-Pro-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Pro-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Z-Ala-Ser-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ser-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Z-ESEN-7-amido-4-methylcoumarin + H2O
Z-ESEN + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Val-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Val-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
ZN-alpha2-glycoprotein + H2O
?
show the reaction diagram
-
-
-
?
lysozyme C + H2O
3 fragments
show the reaction diagram
-
cleavage site are at positions 62 and 64
-
?
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
?
-
-
no activity with acetyl-Phe-Tyr-Asn-4-methylcoumarin-7-amide
-
-
?
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
?
-
-
no activity with benzyloxycarbonyl-Gly-Ala-Gln-4-methylcoumarin-7-amide
-
-
?
additional information
?
-
-
no activity with pro-/gelatinase B
-
-
?
additional information
?
-
-
substrate specificity for P3 position residues
-
-
?
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, 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
?
-
-
processing enzyme of vacuoles, is responsible for the conversion of several vacuolar precursors into their mature forms
-
-
-
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
?
-
during germination and seedling growth legumains might also act as processing enzymes, protein processing and degradation by legumains, overview
-
-
?
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 enzyme is involved in degradation of seed storage proteins
-
-
-
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
?
-
-
the inhibition of osteoclast formation and bone resorption is a nonenzymatic function of prolegumain
-
-
-
additional information
?
-
-
the enzyme acts strictly as asparaginyl endopeptidase, substrate specificity, overview
-
-
-
additional information
?
-
-
the enzyme hydrolyzes peptide bonds with Asn in P1
-
-
-
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
?
-
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
?
-
-
involved in lysosomal processing of bacterial antigens for MHC class II presentation
-
-
-
additional information
?
-
no pivotal role for cathepsin B1 activation in vivo
-
-
-
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
?
-
role in extracellular matrix remodeling via degradation of fibronectin indicated
-
-
-
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
?
-
bioinformatic approach, studies on vacuolar targeting by determination of minimal vacuole targeting motifs, GFP reporter analysis and subcellular staining indicated, bioinformatic approach, studies on vacuolar targeting, determination of minimal vacuole targeting motifs, GFP reporter analysis and subcellular staining indicated
-
-
-
additional information
?
-
-
subsite specificity of legumain analyzed to design fluorescent activity-based probes for monitoring endogenous legumain activity
-
-
-
additional information
?
-
-
asparaginyl endopeptidase plays a pivotal role in the endosome and lysosomal degradation system and is implicated in antigen processing and presentation, asparaginyl endopeptidaseprotein substrates on the C-terminal side of asparagine
-
-
-
additional information
?
-
asparaginyl endopeptidases are cysteine proteases that hydrolyze peptides and proteins 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
?
-
enzyme is involved in host blood-meal digestion
-
-
-
additional information
?
-
-
enzyme promote cell migration and is associated with enhanced tissue invasion and metastases, legumain is a member of the C13 family of peptidases that specifically cleaves asparaginyl bonds
-
-
-
additional information
?
-
-
recombinant HlLgm and HlLgm2 efficiently digest blood proteins, haemoglobin and bovine serum albumin, role of legumain in blood feeding and blood-meal digestion in ticks
-
-
-
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
?
-
-
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, PrVPE1 binds to the DEVD tetrapeptide, a signature substrate for caspase-3
-
-
-
SplaateNatural_Substrates,Natural_Products,id,Organism_Substrates,Commentary_Substrates,Literature_Substrates,Commentary_Products,Literature_Products,Reversibility
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
11S proglobulin + H2O
?
show the reaction diagram
-
processing to the active trimer
-
-
?
11S proglobulin + H2O
?
show the reaction diagram
Q9XG75
processing to the active trimer
-
-
?
annexin II + H2O
?
show the reaction diagram
Q95M12
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
show the reaction diagram
A9CQC1
-
-
?
bovine haemoglobin + H2O
peptides containing C-terminal Asn
show the reaction diagram
A9CQC1
exhibited strict specificity for the asparaginyl bonds on the carboxy-terminal side of a peptide
-
?
cathepsin L + H2O
?
show the reaction diagram
-
processing/activation
-
-
?
cystatin E + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
P09841, Q9NFY9
the enzyme is involved in host hemoglobin degradation
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
specific cleavage
-
-
?
papain-like cysteine proteinase precursors + H2O
activated papin-like cysteine proteinases
show the reaction diagram
-
involved in the senescing of tissues and cell death
-
?
phaseolin + H2O
?
show the reaction diagram
O24325
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
show the reaction diagram
-
involved in the senescing of tissues and cell death
-
?
progelatinase A + H2O
gelatinase A
show the reaction diagram
-
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
?
progelatinase A + H2O
gelatinase A + gelatinase K propeptide
show the reaction diagram
-
activation
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
Q99538
-
-
?
protein + H2O
peptides
show the reaction diagram
-
-
-
?
protein + H2O
peptides
show the reaction diagram
Q9XG75
-
-
?
protein + H2O
peptides
show the reaction diagram
O89017
-
-
?
protein + H2O
peptides
show the reaction diagram
-
enzyme is critically involved in the lysosomal processing of bacterial antigens for MHC class II presentation
-
?
protein + H2O
peptides
show the reaction diagram
-
enzyme is involved in antigen presentation within class II MHC positive cells and in pro-protein processing
-
?
protein + H2O
peptides
show the reaction diagram
-
enzyme is involved mainly in storage protein breakdown
-
?
protein + H2O
peptides
show the reaction diagram
-
involved in mobilization of storage proteins and stress response processes
-
?
serum albumin + H2O
?
show the reaction diagram
Q95M12
-
-
-
?
transferrin + H2O
?
show the reaction diagram
Q95M12
-
-
-
?
Vasoactive intestinal peptide + H2O
?
show the reaction diagram
-
specific cleavage
-
-
?
Vicilin + H2O
?
show the reaction diagram
-
degradation of the principal reserve protein present in Vigna radiata seeds
-
-
-
vitamin D-binding protein + H2O
?
show the reaction diagram
Q95M12
enzyme is involved in the processing of mcromolecules absorbed by proximal tubule cells
-
-
?
ZN-alpha2-glycoprotein + H2O
?
show the reaction diagram
Q95M12
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
P42665
the enzyme is involved in host hemoglobin degradation
-
-
?
additional information
?
-
-
processing enzyme of vacuoles, is responsible for the conversion of several vacuolar precursors into their mature forms
-
-
-
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
?
-
Q9XG75
during germination and seedling growth legumains might also act as processing enzymes, protein processing and degradation by legumains, overview
-
-
?
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 enzyme is involved in degradation of seed storage proteins
-
-
-
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
?
-
-
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
?
-
P09841
no pivotal role for cathepsin B1 activation in vivo
-
-
-
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
?
-
O89017
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, asparaginyl endopeptidaseprotein substrates on the C-terminal side of asparagine
-
-
-
additional information
?
-
Q208S4
asparaginyl endopeptidases are cysteine proteases that hydrolyze peptides and proteins 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
?
-
A9CQC1
enzyme is involved in host blood-meal digestion
-
-
-
additional information
?
-
-
enzyme promote cell migration and is associated with enhanced tissue invasion and metastases, legumain is a member of the C13 family of peptidases that specifically cleaves asparaginyl bonds
-
-
-
additional information
?
-
-
recombinant HlLgm and HlLgm2 efficiently digest blood proteins, haemoglobin and bovine serum albumin, role of legumain in blood feeding and blood-meal digestion in ticks
-
-
-
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
?
-
-
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, PrVPE1 binds to the DEVD tetrapeptide, a signature substrate for caspase-3
-
-
-
SplaateCofactor,Organism,Commentary,Literature,Filename
SplaateMetals_Ions,Organism,Commentary, Literature
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
no effect by DTT
SplaateInhibitors, Organism, Commentary, Literature,Filename
INHIBITORS
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
-
-
(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
-
-
1,10-phenanthroline
27.5% inhibition at 5 mM
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
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-chloromercuribenzoate
-
-
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
-
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
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
-
atorvastatin
-
-
benzoic acid 3-benzyloxycarbonylamino-4-carbamoyl-2-oxo-butyl ester
-
-
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-benzyloxymethylketone
-
moderate inhibition
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-bromoacetate
-
-
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-bromomethylketone
-
strong specific and irreversible inhibition
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-chloroacetate
-
-
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-chloromethylketone
-
strong specific and irreversible inhibition
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-Phe-Ala-CHN2
-
-
Boc-azaAsn-CH=CH-COOEt
-
-
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
-
-
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
-
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
-
-
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
-
-
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
-
-
Boc-Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
-
Ca2+
moderate inhibition
carbobenzyloxy-Ala-Ala-(aza-Asn)-epoxycarboxylate ethyl ester
-
carbobenzyloxy-Ala-Ala-(aza-Asn)-epoxycarboxylate ethyl ester
-
caspase 1 inhibitor V
-
-
-
Cbz-Ala-Ala-azaAsn-CH=CH-COOEt
-
-
Cbz-Ala-Ile-azaAsn-CH=CH-COOEt
-
-
Cbz-Ala-Phe-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
-
Cbz-Ala-Phe-azaAsn-CH=CH-CONHCH2-furyl
-
-
Cbz-Ala-Val-azaAsn-CH=CH-CO-tetrahydroquinoline
-
-
Cbz-Ala-Val-azaAsn-CH=CH-CONHCH2-1-naphthyl
-
-
Cbz-Ala-Val-azaAsn-CH=CH-COOEt
-
-
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
-
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
-
-
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
-
-
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
-
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroquinoline
-
-
Cd2+
-
-
Co2+
strong inhibition
Cu2+
-
-
Cu2+
-
strong inhibition
Cu2+
strong inhibition
Cystatin
-
-
-
Cystatin
-
-
-
Cystatin
-
from chicken egg white
-
Cystatin
from egg white, 62.3% inhibition at 0.003 mM concentration relative to control
-
Cystatin
-
from egg-white
-
cystatin 3
strong inhibition
-
cystatin C
-
-
-
cystatin C
-
endogenous inhibitor
-
cystatin C
-
-
-
cystatin C
-
human
-
cystatin CPI-4
-
-
-
cystatin E
-
high affinity inhibitor of legumain
-
cystatin E/M
-
-
-
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
-
cystatin M
-
high affinity inhibitor of legumain
-
diisopropyl fluorophosphate
-
not
diisopropyl fluorophosphate
-
-
E-64
papain-like cysteine proteinase inhibitor, 7.51% inhibition at 0.3 mM concentration relative to control
E64
slight inhibition at 1 mM
E64
17.1% inhibition at 0.001 mM
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
-
-
FaCPI-1
-
strawberry cystatin, phytocystatin of Fragaria sp.
-
Fe2+
strong inhibition
Hg2+
-
-
Hg2+
-
strong inhibition
High molecular weight kininogen
-
-
-
High-molecular mass kininogen
-
kinin-free, F1.2-free
-
Human cystatin C
-
-
-
Human cystatin C
-
competitive inhibition
-
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
-
human cystatin E/M
-
type 2 cystatin
-
human cystatin F
-
type 2 cystatin
-
HvCPI-4
-
cystatin HvCPI-4 of Hordeum vulgare
-
HvCPI-4-deltaT143-Cterm
-
C-terminal extended part of cystatin HvCPI-4
-
HvCPI-4-deltaT151-Cterm
-
C-terminal extended part of cystatin HvCPI-4
-
HvCPI-4-Q86P
-
cystatin HvCPI-4 of Hordeum vulgare, mutant Q86P
-
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetamide
11.6% remaining activity
iodoacetamide
-
-
iodoacetamide
concentration of 3 mM, 100% inhibition of recombinant protein activity, BSA cleavage inhibited by 5 mM iodoacetamide
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
complete inhibition at 5 mM inhibitor concentration
iodoacetamide
100% inhibition at 3 mM concentration relative to control
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetamide
irreversible millimolar inhibitor
iodoacetate
-
-
iodoacetate
-
-
iodoacetate
55.8 remaining activity
iodoacetate
-
-
L-3-carboxy-2,3-trans-epoxypropionyl-leucyl-amido(4-guanidino)butane
-
i.e. E-64, not
L-3-carboxy-2,3-trans-epoxypropionyl-leucyl-amido(4-guanidino)butane
-
-
Leupeptin
-
-
Leupeptin
slight inhibition at 1 mM
Leupeptin
47.3% inhibition at 1 mM
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
low molecular mass kininogen
-
-
-
Mg2+
moderate inhibition
Mu-Ala-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
-
Mu-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
-
Mu-Ala-Ala-azaAsn-CH=CH-CONHCH2CH2CH2Ph
-
-
Mu-Ala-Ala-azaAsn-CH=CH-COOEt
-
-
Mu-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
-
Mu-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
-
-
Mu-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
16.6% remaining activity
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
complete inhibition at 2 mM
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-ethylmaleimide
-
-
N-Phenylmaleimide
-
-
N-Phenylmaleimide
-
strong inhibition
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-[(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-(1,3-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-(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-(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-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-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-(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-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-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-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-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-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-(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-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-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
-
Ni2+
strong inhibition
ovocystatin
-
weak inhibition, from egg-white
-
ovocystatin
-
from egg-white
-
ovocystatin
-
from chicken egg white
-
p-chloromercuribenzene sulfonic acid
-
-
p-chloromercuribenzene-sulfonic acid
-
-
p-chloromercuribenzoate
-
-
PCMB
-
-
Pepstatin
concentration of 500 microM, 7.8% inhibition of recombinant protein activity
pepstatin A
8.4% inhibition at 0.1 mM
pepstatin A
-
no effect on ability to cleave the Asn-containing substrate
pepstatin A
aspartic peptidase inhibitor has minimal effects on the enzyme activity, 12.22% inhibition at 0.3 mM concentration relative to control
phenylmethanesulfonyl fluoride
PMSF, concentration of 5 mM, 19% inhibition of recombinant protein activity
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
phenylmethylsulfonyl fluoride
-
no effect on ability to cleave the Asn-containing substrate
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)-CH2-1-naphthyl
-
-
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
-
-
Pip-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
-
Pip-Ala-Ala-azaAsn-CH=CH-CONHCH2CH2Ph
-
-
Pip-Ala-Ala-azaAsn-CH=CH-COOEt
-
-
Pip-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
-
Pip-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
-
-
Pip-Ala-Ala-azaAsn-EP(S,S)-COOEt
-
-
Pip-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
-
Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
-
-
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
-
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
-
-
Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
-
-
Piz-Ala-Ala-azaAsn-CH=CH-COOEt
-
-
Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
-
PMSF
serine peptidase inhibitor, 13.84% inhibition at 5 mM concentration relative to control
rat alpha1-macroglobulin
-
-
-
tosyl-Phe-CH2Cl
-
-
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
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
Zn2+
moderate inhibition
[(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
-
-
Mn2+
moderate inhibition
additional information
-
not: EDTA; N-tosyl-L-lysine chloromethyl ketone; phenylmethylsulfonyl fluoride
-
additional information
-
not: EDTA; phenylmethylsulfonyl fluoride
-
additional information
-
-
-
additional information
-
alpha2-macroglobulin; leupeptin; not: EDTA; pepstatin
-
additional information
-
glycosylation of asparaginyl residues totally prevents cleavage by the enzyme, no binding to human alpha2-macroglobulin
-
additional information
-
no inhibition by E-64, leupeptin, and elastatinal
-
additional information
-
no inhibition by PMSF, EDTA and 1,10-phenanthroline
-
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 and EDTA
-
additional information
-
no inhibition by E-64 and leupeptin
-
additional information
no inhibition with EDTA, PMSF, pepstatin A, leupeptin, and E-64
-
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 expression is reduced by lipopolysaccharide priming and in endotoxin-tolerant monocytes
-
additional information
-
no inhibition by E64 and leupeptin
-
additional information
no inhibition by Z-Phe-Ala-CHN2 and 1,10-phenanthroline
-
additional information
-
no inhibition by E64
-
additional information
-
no inhibition by leupeptin
-
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 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
-
inhibitor specificity profiles of cathepsin B and legumain regarded and used for analysis of the suitability of fluorescent activity-based probes
-
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
E-64 has no effect on enzyme activity
-
SplaateActivating_Compound, Organism, Commentary, Literature,Filename
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
10 mM, 300% activation
DTT
-
stimulates
additional information
-
the enzyme requires activation by a thiol compound
-
additional information
the enzyme expression in enhanced in the dark and after ethephon treatment of leaves
-
additional information
-
expression levels of endogenous legumain elevate in HEK-293 cells following stress
-
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
-
mRNAs is up-regulated in the endometrium during the luteal phase of the oestrous cycle and during early pregnancy
-
additional information
-
asparaginyl endopeptidase activation is autocatalytic and requires sequential removal of C- and N-terminal propeptides at different pH thresholds
-
SplaateKM_Value,KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.122
acetyl-Pro-Thr-Asn-4-methylcoumarin-7-amide
-
pH 5.5, 25C
0.286
acetyl-Pro-Thr-Asn-4-methylcoumarin-7-amide
-
pH 5.5, 25C
0.07
acetyl-Thr-Ala-Asn-4-methylcoumarin-7-amide
-
pH 5.5, 25C
0.128
acetyl-Thr-Ala-Asn-4-methylcoumarin-7-amide
-
pH 5.5, 25C
0.05
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
-
pH 5.8, 30C
0.08
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
-
pH 5.5, 25C
0.09
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
-
pH 5.5, 25C
0.67
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
-
pH 5.0, 37C
0.05
benzyloxycarbonyl-Ile-Ser-Asn-4-methylcoumarin-7-amide
-
pH 5.0, 37C
0.023
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2
-
pH 5.0
0.033
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2
-
pH 5.9
additional information
additional information
-
-
-
SplaateTurnover_Number, Turnover_Number_Maximum, Substrate,Organism,Commentary, Literature, Filename
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.9
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
Bos taurus
-
pH 5.0, 37C
46
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
Sus scrofa
-
pH 5.8, 30C
0.1
benzyloxycarbonyl-Ile-Ser-Asn-4-methylcoumarin-7-amide
Bos taurus
-
pH 5.0, 37C
additional information
additional information
Homo sapiens
-
-
-
SplaateKCat_KM_Value,KCat_KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
SplaateKI_Value,KI_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
cystatin 3
pH and temperature not specified in the publication
-
0.00076
FaCPI-1
-
inhibitor concentrations between 25 and 500 nM used, incubation with 10 microgram of a soluble endosperm protein extract, at 25C and pH 6 for 10 min; inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25C and pH 6 for 10 min
-
0.0000002
Human cystatin C
-
pH 5.6, 37C
-
0.000005
Human cystatin C
-
below, pH 5.8, 30C
-
0.00000022
human cystatin C mutant L9G
-
pH 5.6, 37C
-
0.001
human cystatin C mutant N39K
-
above, pH 5.6, 37C
-
0.00000022
human cystatin C mutant R8G, human cystatin C mutant V10G, human cystatin C mutant W106G
-
pH 5.6, 37C
-
0.0000000016
human cystatin E/M
-
pH 5.6, 37C
-
0.00001
human cystatin F
-
pH 5.6, 37C
-
0.00019
HvCPI-4, HvCPI-4-deltaT143-Cterm
-
inhibitor concentrations between 25 and 500 nM used, incubation with 10 microgram of a soluble endosperm protein extract, at 25C and pH 6 for 10 min; inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25C 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 25C and pH 6 for 10 min; inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25C 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 25C and pH 6 for 10 min; mutant Q86P of HvCPI-4, inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25C and pH 6 for 10 min
-
additional information
additional information
-
-
-
SplaateIC50_Value,IC50_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
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
(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
0.0000083
(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
0.001
(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
0.00075
Boc-azaAsn-CH=CH-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.00003
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
Ixodes ricinus
-
pH 6.8, 25C
0.000045
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.000005
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Ixodes ricinus
-
pH 6.8, 25C
0.000068
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.00002
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Ixodes ricinus
-
pH 6.8, 25C
0.000058
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Schistosoma mansoni
-
pH 6.8, 25C
0.0000075
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
Ixodes ricinus
-
pH 6.8, 25C
0.000045
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
Schistosoma mansoni
-
pH 6.8, 25C
0.0000085
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.00008
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
Schistosoma mansoni
-
pH 6.8, 25C
0.00008
Boc-Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.00027
Boc-Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Ixodes ricinus
-
pH 6.8, 25C
0.0000045
Cbz-Ala-Ala-azaAsn-CH=CH-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.000031
Cbz-Ala-Ala-azaAsn-CH=CH-COOEt
Schistosoma mansoni
-
pH 6.8, 25C
0.00000052
Cbz-Ala-Ile-azaAsn-CH=CH-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.00028
Cbz-Ala-Ile-azaAsn-CH=CH-COOEt
Schistosoma mansoni
-
pH 6.8, 25C
0.0005
Cbz-Ala-Phe-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Ixodes ricinus
-
pH 6.8, 25C
0.0018
Cbz-Ala-Phe-azaAsn-CH=CH-CONHCH2-furyl
Ixodes ricinus
-
pH 6.8, 25C
0.000013
Cbz-Ala-Val-azaAsn-CH=CH-CO-tetrahydroquinoline
Ixodes ricinus
-
pH 6.8, 25C
0.000138
Cbz-Ala-Val-azaAsn-CH=CH-CO-tetrahydroquinoline
Schistosoma mansoni
-
pH 6.8, 25C
0.0005
Cbz-Ala-Val-azaAsn-CH=CH-CO-tetrahydroquinoline
Ixodes ricinus
-
pH 6.8, 25C
0.00035
Cbz-Ala-Val-azaAsn-CH=CH-CONHCH2-1-naphthyl
Ixodes ricinus
-
pH 6.8, 25C
0.00105
Cbz-Ala-Val-azaAsn-CH=CH-CONHCH2-1-naphthyl
Schistosoma mansoni
-
pH 6.8, 25C
0.000065
Cbz-Ala-Val-azaAsn-CH=CH-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.0001
Cbz-Ala-Val-azaAsn-CH=CH-COOEt
Schistosoma mansoni
-
pH 6.8, 25C
0.00000037
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Ixodes ricinus
-
pH 6.8, 25C
0.00005
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.00000035
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Ixodes ricinus
-
pH 6.8, 25C
0.00007
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Schistosoma mansoni
-
pH 6.8, 25C
0.00000014
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.00007
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
Schistosoma mansoni
-
pH 6.8, 25C
0.00075
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Schistosoma mansoni
-
pH 6.8, 25C
0.0008
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Ixodes ricinus
-
pH 6.8, 25C
0.00075
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroquinoline
Schistosoma mansoni
-
pH 6.8, 25C
0.00085
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroquinoline
Ixodes ricinus
-
pH 6.8, 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
0.02
FaCPI-1
Hordeum vulgare
-
endosperm
-
0.2
FaCPI-1
Hordeum vulgare
-
root extract
-
0.038
HvCPI-4
Hordeum vulgare
-
endosperm
-
0.12
HvCPI-4
Hordeum vulgare
-
root extract
-
0.018
HvCPI-4-deltaT143-Cterm
Hordeum vulgare
-
endosperm
-
0.068
HvCPI-4-deltaT143-Cterm
Hordeum vulgare
-
root extract
-
0.022
HvCPI-4-deltaT151-Cterm
Hordeum vulgare
-
endosperm
-
0.091
HvCPI-4-deltaT151-Cterm
Hordeum vulgare
-
root extract
-
0.033
HvCPI-4-Q86P
Hordeum vulgare
-
endosperm
-
0.000065
Mu-Ala-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Ixodes ricinus
-
pH 6.8, 25C
0.000103
Mu-Ala-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Schistosoma mansoni
-
pH 6.8, 25C
0.0000033
Mu-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Ixodes ricinus
-
pH 6.8, 25C
0.000045
Mu-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.00145
Mu-Ala-Ala-azaAsn-CH=CH-CONHCH2CH2CH2Ph
Schistosoma mansoni
-
pH 6.8, 25C
0.00000023
Mu-Ala-Ala-azaAsn-CH=CH-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.000101
Mu-Ala-Ala-azaAsn-CH=CH-COOEt
Schistosoma mansoni
-
pH 6.8, 25C
0.0000017
Mu-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Ixodes ricinus
-
pH 6.8, 25C
0.00009
Mu-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.000006
Mu-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
Ixodes ricinus
-
pH 6.8, 25C
0.00006
Mu-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
Schistosoma mansoni
-
pH 6.8, 25C
0.0006
Mu-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Ixodes ricinus
-
pH 6.8, 25C
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
Q6EHZ7
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
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
Q6EHZ7
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
Q6EHZ7
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
Q6EHZ7
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
0.0075
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
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
Q6EHZ7
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
Q6EHZ7
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
0.008 - 0.01
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
Trichomonas vaginalis
Q6EHZ7
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
Q6EHZ7
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
Q6EHZ7
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
0.0000055
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
Q6EHZ7
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
Q6EHZ7
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
Q6EHZ7
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
0.00000055
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
Q6EHZ7
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
Q6EHZ7
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
Q6EHZ7
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
Q6EHZ7
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
0.002
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
Q6EHZ7
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
Q6EHZ7
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
Q6EHZ7
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
0.00007
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
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
Q6EHZ7
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
Q6EHZ7
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
0.00006
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
0.000006
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
Q6EHZ7
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
0.000005
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
Trichomonas vaginalis
Q6EHZ7
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
0.0000024
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)-CH2-1-naphthyl
Ixodes ricinus
-
pH 6.8, 25C
0.0001
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)-CH2-1-naphthyl
Schistosoma mansoni
-
pH 6.8, 25C
0.000017
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
Ixodes ricinus
-
pH 6.8, 25C
0.00008
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.000008
Pip-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Ixodes ricinus
-
pH 6.8, 25C
0.000057
Pip-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.0004
Pip-Ala-Ala-azaAsn-CH=CH-CONHCH2CH2Ph
Ixodes ricinus
-
pH 6.8, 25C
0.00075
Pip-Ala-Ala-azaAsn-CH=CH-CONHCH2CH2Ph
Schistosoma mansoni
-
pH 6.8, 25C
0.000015
Pip-Ala-Ala-azaAsn-CH=CH-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.00008
Pip-Ala-Ala-azaAsn-CH=CH-COOEt
Schistosoma mansoni
-
pH 6.8, 25C
0.000012
Pip-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Ixodes ricinus
-
pH 6.8, 25C
0.000072
Pip-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.0000085
Pip-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
Ixodes ricinus
-
pH 6.8, 25C
0.00016
Pip-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
Schistosoma mansoni
-
pH 6.8, 25C
0.00003
Pip-Ala-Ala-azaAsn-EP(S,S)-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.00022
Pip-Ala-Ala-azaAsn-EP(S,S)-COOEt
Schistosoma mansoni
-
pH 6.8, 25C
0.00015
Pip-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Ixodes ricinus
-
pH 6.8, 25C
0.0006
Pip-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Schistosoma mansoni
-
pH 6.8, 25C
0.000031
Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
Ixodes ricinus
-
pH 6.8, 25C
0.00009
Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.0000026
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Ixodes ricinus
-
pH 6.8, 25C
0.00007
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Schistosoma mansoni
-
pH 6.8, 25C
0.0000038
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Ixodes ricinus
-
pH 6.8, 25C
0.00004
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Schistosoma mansoni
-
pH 6.8, 25C
0.000013
Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
Ixodes ricinus
-
pH 6.8, 25C
0.00025
Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
Schistosoma mansoni
-
pH 6.8, 25C
0.0000085
Piz-Ala-Ala-azaAsn-CH=CH-COOEt
Ixodes ricinus
-
pH 6.8, 25C
0.0003
Piz-Ala-Ala-azaAsn-CH=CH-COOEt
Schistosoma mansoni
-
pH 6.8, 25C
0.000011
Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Ixodes ricinus
-
pH 6.8, 25C
0.00015
Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Schistosoma mansoni
-
pH 6.8, 25C
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
0.11
HvCPI-4-Q86P
Hordeum vulgare
-
root extract
-
additional information
additional information
Hordeum vulgare
-
inhibitory doses for 50% proteinase activity inhibition higher for root legumain activity than for endosperm one
-
additional information
additional information
Ixodes ricinus
Q6PRC7
IC50 concentration of the aza-peptide Michael acceptor Aza-Asn-11a in a range of about 500 nM determined
-
0.00075
Mu-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Schistosoma mansoni
-
pH 6.8, 25C
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)-4-oxo-4-phenylbut-2-enoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
Trichomonas vaginalis
Q6EHZ7
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,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
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
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
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
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-(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
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
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
Trichomonas vaginalis
Q6EHZ7
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
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
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
0.001
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
Trichomonas vaginalis
Q6EHZ7
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-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
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
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
Q6EHZ7
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
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
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Trichomonas vaginalis
Q6EHZ7
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
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
additional information
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Trichomonas vaginalis
Q6EHZ7
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
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
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
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
additional information
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
Trichomonas vaginalis
Q6EHZ7
IC50 is below 0.00001 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
SplaateSpecific_Activity, Specific_Activity_Maximum, Organism ,Commentary, Literature
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, 37C, 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
1.35
membrane-bound fraction
1.53
-
purified enzyme
4.5
-
purified enzyme
7
-
purified enzyme
7.04
purified enzyme, substrate casein
8.1
-
purified enzyme, substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide, pH 5.8, 30C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
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 endogenous legumain activity present in barley protein extracts analyzed, 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; 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; role of legumain in the pathophysiology of atherosclerosis analyzed, human monocyte legumain activity assay described, migration/proliferation and invasion assay described
additional information
-
expression determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed; 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
-
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
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
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
activity profile shown, specificity profile using a positional scanning synthetic combinatorial library indicated
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
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; 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
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
-
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; 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
the specific activity of recombinant asparaginyl endopeptidase is lower than that detected for excretory-secretory products of adult worm
additional information
-
asparaginyl endopeptidase deficiency provokes extramedullary hematopoiesis in the spleen and abnormally enlarged histiocytes with ingested red blood cells in bone marrow; asparaginyl endopeptidase depletion evidently enhances the phagocytic activity, suggesting that phagocytic activity of macrophages in asparaginyl endopeptidase-/- mice is elevated; 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; in contrast to the enhanced macrophage activity, the natural killer cell activity in the asparaginyl endopeptidase-null animal is significantly reduced; mutant mice lacking asparaginyl endopeptidase develop fever, cytopenia, hepatosplenomegaly and hemophagocytosis, which are primary pathological manifestations of hemophagocytic syndrome/hemophagocytic lymphohistiocytosis; 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; red blood cells from asparaginyl endopeptidase-null mice are defective in plasma membrane components; the liver is significantly enlarged in asparaginyl endopeptidase deficient mice as compared with the normal counterparts; 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; 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; the spleens from asparaginyl endopeptidase-null mice are 5-10times larger than those of wild type controls
SplaatepH_Optimum, pH_Optimum_Maximum, Organism, Commentary, Literature
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
Legumain activity shows a pH optimum of 4.0 towards substrates with Asp at the P1 position; superactivation of prolegumain requires its incubation at pH 4.0
5
-
benzyloxycarbonyl-Ala-Ala-Asn 4-methylcoumarin 7-amide
5
-
assay at
5
-
with substrate acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide
5.1
-
vicilin
5.4
-
with substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
5.4
activity assay at, maximum of activity observed at pH 5-6; activity assay at, maximum of activity observed at pH 56
5.5
-
Ser-Glu-Ser-Glu-Asn-Gly-Leu-Glu-Glu-Thr
5.5
-
assay at
5.5
activity lowered above pH 6.0
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
5.6
-
assay at
5.8
-
aasy at
5.8
-
with substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
5.8
-
assay at
5.8
-
assay at
5.8
-
at 30C
5.8
-
assay at
6.1
-
recombinant enzyme, dependent on buffer system
6.4
-
at 25C
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
in 0.1 M sodium phosphate
7
the rHlLgm2 is more active in neutral to slightly alkaline condition
7
-
recombinant enzymes digested hemoglobin and bovine serum albumin optimally at pH 7
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
-
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
-
legumain activity is pH-dependent and substrate-dependent
SplaatepH_Range,pH_Range_Maximum, Organism,Commentary, Literature
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
assay under different pH conditions tested in 0.2 M sodium citrate/citric acid, 1 mM DTT at 37C, no enzyme activity observed at pH 4 and below, activity dropped to 55% at pH 7; assay under different pH conditions tested in 0.2 M sodium citrate/citric acid, 1 mM DTT at 37C, no enzyme activity observed at pH 4 and below, activity drops to 55% at pH 7
3 - 11
assay under different pH conditions tested
3 - 6
-
-
4 - 6
-
-
4 - 6
activity under different pH conditions measured
4 - 8
no activity below pH 4.0 or above pH 8.0
5.5 - 6.8
recombinant enzyme
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 37C
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
SplaateTemperature_Optimum, Temperature_Optimum_Maximum, Organism, Commentary, Literature
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
25
-
assay at
25
-
assay at
30
-
assay at
35
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
assay at
37
-
activity assay at
37
assay of legumain activity at
37
activity assay at
37
activity assay at; activity assay at
37
-
assay at
SplaateTemperature_Range, Temperature_Range_Maximum, Organism, Commentary, Literature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 70
assay under different temperature conditions tested
30
high activity (90%) is observed at 30C, while a gradual loss of activity is observed after the prolonged exposure to higher temperatures
SplaatepI_Value,pI_Value_Maximum, Organism,Commentary, Literature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
predicted preprotein
7.1
predicted preproprotein
SplaateSource_Tissue, Organism, Commentary, Literature, Textmining
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
-
WT51 cell, EBV-transformed
Manually annotated by BRENDA team
for generation of transformed plants, GFP reporter analysis indicated
Manually annotated by BRENDA team
-
high enzyme expression level
Manually annotated by BRENDA team
-
inhibitory effects by phytocystatins against commercial human legumain analyzed
Manually annotated by BRENDA team
-
recombinant legumain
Manually annotated by BRENDA team
inflamed areas in advanced human coronary atherosclerotic plaques
Manually annotated by BRENDA team
germinated, developmental pattern
Manually annotated by BRENDA team
-
resting and maturing
Manually annotated by BRENDA team
-
late stage of seed maturation
Manually annotated by BRENDA team
-
developing endosperms of 18 days after flowering, inhibitory effects by cystatins against endogenous legumain activity in barley protein extracts analyzed
Manually annotated by BRENDA team
-
attached to storage-protein substrates in ER bodies
Manually annotated by BRENDA team
anthere only; anthere, ovules, filaments; anthere, ovules, filaments; anthere, ovules, filaments; anthere, ovules, filaments; anthere, ovules, filaments; anthere, ovules, filaments
Manually annotated by BRENDA team
expression in, localized in digestive vesicles of gut cells and within the peritrophic matrix, function associated with the degradation of host hemoglobin suggested
Manually annotated by BRENDA team
human umbilical vascular endothelial cells (HUVECs) tested in migration/proliferation and invasion assays
Manually annotated by BRENDA team
caecal epithelium, 2-6 week old juveniles and adults, mRNA expression also in metacercariae; caecal epithelium, 2-6 week old juveniles and adults, mRNA expression also in metacercariae
Manually annotated by BRENDA team
protein from kidney tissues used for western blot analysis, unilateral ureteral obstruction in legumain-deficient mice
Manually annotated by BRENDA team
-
wounded or senescing, alpha-VPE and beta-VPE
Manually annotated by BRENDA team
enhanced expression in senescent leaves
Manually annotated by BRENDA team
-
leaf extracts, assay for asparaginyl bond hydrolysis in, analysis of backbone cyclization of endogenous cyclotides in
Manually annotated by BRENDA team
-
leaf extracts, assay for asparaginyl bond hydrolysis in
Manually annotated by BRENDA team
-
in the leaf tissue the Leg1 is the highest expressed isoform, followed by Leg3
Manually annotated by BRENDA team
-
LGMN expression is increased in hepatocellular carcinoma cells relative to normal hepatocytes in the same specimens
Manually annotated by BRENDA team
M-CSF differentiated primary macrophages, in vitro expression, also detected in the culture media
Manually annotated by BRENDA team
-
of atherosclerotic aorta of aging Apolipoprotein E deficient mice, mRNA expression increases with development of atherosclerosis
Manually annotated by BRENDA team
-
metastatic oral cancer cell line
Manually annotated by BRENDA team
lmidgut epithelium shown by immunohistochemistry
Manually annotated by BRENDA team
Haemaphysalis longicornis Okayama
-
lmidgut epithelium shown by immunohistochemistry
-
Manually annotated by BRENDA team
-
from peripheral blood, normal and endotoxin-tolerant cells
Manually annotated by BRENDA team
fluorimetric assay measuring legumain protease activity applied
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
germinating, lateral
Manually annotated by BRENDA team
mature; mature; mature; mature; mature
Manually annotated by BRENDA team
-
undergoing controlled cell death, alpha-VPE
Manually annotated by BRENDA team
-
collected from plants germinated at 22C in the dark for 7 days
Manually annotated by BRENDA team
-
in root tissues the isoform Leg1 has the greatest mRNA levels, whereas Leg2 has the lowest ones
Manually annotated by BRENDA team
6-week-old, male parasites
Manually annotated by BRENDA team
-
activity increases during germination
Manually annotated by BRENDA team
-
in endosperm of late stage of seed maturation
Manually annotated by BRENDA team
-
isoforms Leg2 and Leg3 are highly expressed in dry seeds
Manually annotated by BRENDA team
control plants and transformed plants, GFP reporter analysis indicated
Manually annotated by BRENDA team
additional information
-
no activity in native HEK 293 cell
Manually annotated by BRENDA team
additional information
-
no activity in blood leukocytes
Manually annotated by BRENDA team
additional information
-
tissue distribution, low expression level in all tissues tested, no expression in MG63 osteosarcoma cells
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
in all vegetative organs, the precursor enzyme is synthesized at membrane-bound polysomes in the cytoplasm
Manually annotated by BRENDA team
additional information
-
the precursor enzyme is synthesized at membrane-bound polysomes in the cytoplasm
Manually annotated by BRENDA team
additional information
-
expression of enzyme in healthy and in cancer cells, the expression is increased in cancer cells, overview
Manually annotated by BRENDA team
additional information
activity only in adult worms
Manually annotated by BRENDA team
additional information
activity only in adult worms; activity only in adult worms
Manually annotated by BRENDA team
additional information
-
the alpha and gamma vacuolar processing enzyme occurs only in vegetative organs
Manually annotated by BRENDA team
additional information
tissue-specific and developmental expression patterns, overview; tissue-specific and developmental expression patterns, overview; tissue-specific and developmental expression patterns, overview; tissue-specific and developmental expression patterns, overview; tissue-specific and developmental expression patterns, overview; tissue-specific and developmental expression patterns, overview; tissue-specific and developmental expression patterns, overview
Manually annotated by BRENDA team
additional information
expression pattern of SPAE
Manually annotated by BRENDA team
additional information
-
legumain is not detected in salivary glands, ovaries, cuticles, tracheae, Malpighian tubules and synganglia
Manually annotated by BRENDA team
SplaateLocalization, Organism, Commentary, id_go, Literature, Textmining
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
Manually annotated by BRENDA team
the enzyme is secreted into the digestive tract of host animals
-
Manually annotated by BRENDA team
the enzyme is secreted into the digestive tract of host animals; the enzyme is secreted into the digestive tract of host animals
-
Manually annotated by BRENDA team
crude worm protein extracts but not in excretion-secretion products of adult parasites, polyclonal antisera and activity assay; crude worm protein extracts but not in excretion-secretion products of adult parasites, polyclonal antisera and activity assay
Manually annotated by BRENDA team
lysosomes of renal proximal tubular cells
Manually annotated by BRENDA team
association of with microvilli shown
Manually annotated by BRENDA team
Haemaphysalis longicornis Okayama
-
bound
-
Manually annotated by BRENDA team
-
protein storage vacuoles
Manually annotated by BRENDA team
protein storage vacuoles
Manually annotated by BRENDA team
-
protein storage vacuoles
Manually annotated by BRENDA team
-
the alpha and gamma vacuolar processing enzyme occurs only in vegetative organs, while the beta VPE occurs in seeds
Manually annotated by BRENDA team
vacuoles within the sugarcane storage parenchyma tissue, bioinformatical studies on vacuolar targeting, GFP-constructs sucessfully targeted to lytic vacuolar compartments of Saccharum officinarum
Manually annotated by BRENDA team
-
digestive vacuoles of gut epithelial cells
Manually annotated by BRENDA team
-
PrVPE1 localizes to a reticulate compartment resembling the vacuole
Manually annotated by BRENDA team
surface, of intestinal cells
Manually annotated by BRENDA team
additional information
proenzyme is probably attached to its storage-protein substrates
-
Manually annotated by BRENDA team
additional information
-
proenzyme is probably attached to its storage-protein substrates
-
Manually annotated by BRENDA team
SplaatePDB,PDB,PDB,Organism,Uniprot_ID
SplaateMolecular_Weight, Molecular_Weight_Maximum, Organism, Commentary, Literature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23500
-
Vigna radiata, gel filtration
30308
23800
-
Phaseolus vulgaris, gel filtration
30309
31000
-
gel filtration
650376
35000
-
mature form in uterine luminal fluid, determined by SDS-PAGE
700314
35300
-
glycosylated native enzyme, gel filtration
651931
36000
-
mature, active form, determined by SDS-PAGE and Westen blot analysis
696499
37000
-
active protein
717402
38000
removal of a peptide of 9000 Dalton from the preprotein
683541
38000
endogenous HlLgm2, predicted and confirmed by SDS-PAGE and immunoblot analysis
699391
42000
-
mature processed protein of 42 kDa, Western blot
718221
42500
His-tagged rHlLgm2, determined by SDS-PAGE
699391
45000
-
soybean, HPLC size exclusion chromatography
30314
45000
-
pro-protein of 53 kDa, Western blot
718221
46000
-
non-mature, active form, determined by SDS-PAGE and Westen blot analysis
696499
47000
preprotein, deduced from sequence
683541
47000
determined by SDS-PAGE
698344
47490
predicted preprotein
699391
49000
-
active form, determined by SDS-PAGE
700314
49630
predicted preproprotein
699391
53000
-
pre-pro-protein of 53 kDa, Western blot
718221
56000
-
inactive proform, determined by SDS-PAGE and Westen blot analysis
696499
56000
-
proform, determined by SDS-PAGE
700314
SplaateSubunits, Organism, Commentary, Literature
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 37000, Ricinus communis, SDS-PAGE
?
x * 38100, mature enzyme, SDS-PAGE, x * 53400, pre-proenzyme, SDS-PAGE
?
-
x * 48000, autocatalytically processed enzyme, SDS-PAGE
?
-
x * 35000, wild-type and mutants enzymes, SDS-PAGE
?
-
x * 34000, glycosylated enzyme, SDS-PAGE, x * 31000, deglycosylated 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 * 49000, proenzyme, x * 31000, mature, deglycosylated enzyme
?
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 * 49000, about, amino acid sequence calculation, x * 75000, recombinant GST-fusion enzyme, SDS-PAGE
?
x * 32000, SDS-PAGE, no signals after RNA interference of the SMAE gene encoding schistosome legumain
?
x * 30000, 2-D electrophoresis
?
x * 30000, 2-D electrophoresis
?
-
x * 46000-47000, active enzyme form, SDS-PAGE; x * 56000, pro-enzyme form, SDS-PAGE
?
-
x * 41000, recombinant enzyme, SDS-PAGE
?
x * 60000, SDS-PAGE
monomer
-
1 * 22500, Vigna radiata, SDS-PAGE
monomer
-
1 * 34000, reducing SDS-PAGE
monomer
-
1 * 33100, glycosylated native enzyme, SDS-PAGE
monomer
-
1 * 33000-33800
monomer
-
1 * 23400
monomer
-
1 * 33000
additional information
-
comparison of the tertiary structure of the enzyme with other cysteine endopeptidases
additional information
structure analysis, overview
additional information
structure analysis, overview; structure analysis, overview
additional information
-
primary structure determination
SplaatePosttranslational_Modification, Organism, Commentary, Literature
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
glycoprotein
-
putative Asn-glycosylation sites at Asn85 and Asn270
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; N-terminal and C-terminal cleavage sites predicted, N-terminal sequence indicated
glycoprotein
-
-
glycoprotein
asparagine-linked glycosylation
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
Haemaphysalis longicornis Okayama
-
cleavage site at asparagines 364-365 at the C-terminus identified in endogenous and in recombinant protein
-
glycoprotein
-
4 potential N-glycosylation sites at Asn91, ASn167, Asn263, and Asn272
glycoprotein
-
-
proteolytic modification
-
the 56 kDa proform is cleavaed to the active 46 kDa and 36 kDa forms
proteolytic modification
-
autolytic activation upon exposure to acidic pH
proteolytic modification
-
autocatalytic activation by cleavage of aspartic acid residues, overview
proteolytic modification
-
autoactivation/maturation by cleavage at Asn323
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
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
glycoprotein
potential N-linked glycosylation sites (NXS/T) are detected at Asn-68 and Asn-173
proteolytic modification
-
different processed forms of Papaver VPE exist
no glycoprotein
but enzyme contains 1 putative N-glycosylation site at N326
proteolytic modification
putative cleavage site is N367-E368
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
autoactivation
proteolytic modification
autoactivation; autoactivation at 37C, pH 4.5
glycoprotein
-
4 potential N-glycosylation sites at Asn91, ASn167, Asn263, and Asn272
glycoprotein
-
N-glycosylation, deglycosylation by N-glycosidase F
proteolytic modification
-
autoactivation/maturation by cleavage at Asn323
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
glycoprotein
-
probably N-glycosylated
proteolytic modification
-
autoactivation by removal of the propeptide, activation after arrival in the vacuole
SplaateCommentary, Organism, Literature
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
-
SplaatepH_Stability,pH_Stability_Maximum, Organism, Commentary, Literature
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
stable, irreversible denaturation at higher pH
668775
3 - 7
-
26.5C, very stable
30313
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 60C. At pH values higher than 6.0 the melting temperature Tm decreased to below 30C
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
7.5
-
even with additives the enzyme is labile above
30311
additional information
no activity at pH 6.0
698344
SplaateTemperature_Stability,Temperature_Stability_Maximum, Organism, Commentary, Literature
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
the enzyme is less affected when incubated at 4 or 10C for 1 h
732644
26.5
-
pH 3.0-7.0, very stable
30313
35
-
10 min, stable up to
30308
45
-
10 min, stable up to
650376
50
-
10 min, complete inactivation
30308
SplaateGeneral_Stability, Organism, Literature
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol is essentially required for stability
-
enzyme is resitant to freezing and thawing
-
2-mercaptoethanol stabilizes
-
Brij 35, 0.005-0.05%, stabilizes
-
DTT stabilizes
-
Easily inactivated after freeze thawing
-
enzyme tends to be absorbed to any solid material at low salt concentration
-
SplaateOrganic_Solvent, Organism, Commentary, Literature
SplaateOxidation_Stability,Organism,Literature
SplaateStorage_Stability, Organism, Literature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 50 mM sodium citrate-buffered saline, pH 5.0, 2 mM 2-mercaptoethanol, a few weeks, stable
-
4C to -20C, 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
-
4C, purified native enzyme from kidney, pH 5.8, little loss of activity over several months
-
SplaateCommentary, Organism, Literature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography (glutathione-Sepharose)
affinity chromatography (glutathione-Sepharose)
1045fold to homogeneity from kidney
-
native enzyme from dry seeds, to homogeneity
-
recombinant His-tagged enzyme from Escherichia coli, gel filtration and SDS-PAGE; recombinant His-tagged enzyme from Escherichia coli, gel filtration and SDS-PAGE
native enzyme from dry seeds, to homogeneity
-
recombinant protein is purified using Ni-Sepharos under native conditions
recombinant enzyme
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant IgG-fusion protein from cell line COP5
-
using NiNTA chromatography
-
ammonium sulfate precipitation
-
recombinnat His-tagged enzyme
recombinant His-tagged enzyme from Escherichia coli, SDS-PAGE
recombinant enzyme is purified by affinity chromatography using His-Trap nickel columns
native enzyme from germinated seeds, to homogeneity
-
native enzyme from dry seeds, to homogeneity
-
recombinant His-tagged enzyme from Escherichia coli, SDS-PAGE
native enzyme to homogeneity; soluble recombinant C197 from Pichia pastoris, native enzyme to homogeneity
2200fold from kidney, to homogeneity
-
native enzyme from kidney, overview
-
from cotyledon
-
native enzyme from germinated seeds, to homogeneity
-
SplaateCommentary, Organism, Literature
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione S-transferase-fusion protein expressed in Escherichia coli BL21(DE3)
glutathione S-transferase-fusion protein expressed in Escherichia coli BL21(DE3)
DNA and amino acid sequence determination and analysis
-
recombinantly expressed in yeast
-
precursor of asparaginyl endopeptidase
-
inserted in pET20b(+), transformed into the Escherichia coli BL21(DE3)pLysS strain; inserted in pET20b(+), transformed into the Escherichia coli BL21(DE3)pLysS strain
expressed in Escherichia coli
plasmid pTrcHisB/HlLgm transformed into the Escherichia coli Top10F0 strain
gene leg-1, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree, expression in Escherichia coli as GST-fusion protein
DNA sequence determination and analysis
-
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 HEK-293 cells
-
gene PRSC1, DNA and amino acid sequence determination and analysis, localization on chromosome 14q32.1, expression in insect cells
-
His-tagged fusion protein stably transfected in LEXSY P10 host strain
-
overexpression in CHO cells
-
overexpression in murine cell line COP5 as a C-terminally IgG-fusion protein
-
stable overexpression in HEK 293 cells and in C13 cells
-
expressed in Pichia pastoris KM71H cells
-
gene SPAE or Y192, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression of His-tagged enzyme
expressed in Pichia pastoris
-
in Escherichia coli, Champion-pET directional expression kit, pET100/D-TOPO expression vector, functionally expression of recombinant protein in Pichia pastoris, expression vector pPICZaB
expressed in Escherichia coli
-
AEP -/-, +/- and +/+ mice on a mixed 129/Ola and C57BL/6 background are generated
-
DNA and amino acid sequence determination and analysis
-
DNA sequence and structure determination and analysis, expression in mammalian cells
-
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
-
expression of vegetative enzyme in seeds and of seed enzyme in stamen, phylogenetic tree; expression of vegetative enzyme in seeds and of seed enzyme in stamen, phylogenetic tree; expression of vegetative enzyme in seeds and of seed enzyme in stamen, phylogenetic tree; expression of vegetative enzyme in seeds and of seed enzyme in stamen, phylogenetic tree; expression of vegetative enzyme in seeds and of seed enzyme in stamen, phylogenetic tree; expression of vegetative enzyme in seeds and of seed enzyme in stamen, phylogenetic tree; expression of vegetative enzyme in seeds and of seed enzyme in stamen, phylogenetic tree
recombinant Ov-AEP-1 is expressed as hexa-His tag in Escherichia coli in inclusion bodies
DNA and amino acid sequence determination and analysis
DNA and amino acid sequence determination
-
expression of inactive precursor enzyme in yeast and insect cells, expression of a processing-site mutant in yeast and subsequent in vitro processing study
-
in Escherichia coli, construct pCvsEndoexp1 transformed into callus derived from Q117 meristematic tissue, transgenic plants regenerated
expressed in Pichia pastoris
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
partial DNA sequence determination
-
asparaginyl endopeptidase is expressed in Pichia pastoris
SplaateCommentary, Organism, Literature
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
secretion of pro-legumain is inhibited by treatment with brefeldin A
-
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
-
bafilomycin A1 enhances the secretion of the the enzyme, which is also is up-regulated in tumour and tumour-associated cells
-
legumain expression is increased during monocyte-to-macrophage differentiation
-
isoform Leg-4 is repressed after abscisic acid exposure
-
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 Leg4 mRNA levels do not increase when the plants are submitted to NaCl
-
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
-
the enzyme expression is down-regulated in plantlets treated with salicylic acid
enzyme expression is not affected by jasmonic acid and gibberellic acid
the enzyme expression is up-regulated in plantlets treated with abscisic acid
SplaateEngineering, Organism, Commentary, Literature
ENGINEERING
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
C52A
-
reduced autocatalytic activity, no activity against other substrates
D147G
-
the mutant shows reduced proteolytic activity
D147S
-
the mutant shows reduced proteolytic activity
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
-
reduced autocatalytic activity, no activity against other substrates
H47A
-
reduced autocatalytic activity, no activity against other substrates
C191S
-
site-directedd mutagenesis, completely inactive
C52S
-
site-directed mutagenesis, as active as the wild-type
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
H164A
-
site-directed mutagenesis, control mutant, as active as the wild-type
S195A
-
site-directed mutagenesis, control mutant, as active as the wild-type
N197C
-
site-directed mutagenesis, the mutation renders the enzyme of Sm32 active
H47A
-
site-directed mutagenesis, 54% activity compared to the wild-type
additional information
-
construction of null-legumain mice
SplaateCommentary, Organism, Literature
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
SplaateApplication,Organism,Commentary,Literature
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
enzyme serves as a promising candidate for prodrug tumor therapy
medicine
studies on a functional role of legumain in atherogenesis
medicine
-
studies on a functional role of legumain in atherogenesis
diagnostics
potential for serodiagnosis of human opisthorchiasisas immunodiagnostic antigen
biotechnology
studies on vacuolar targeting, targeting motif of legumain as a potential tool for plant engineering analyzed