Information on EC 3.4.22.34 - Legumain

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.4.22.34
-
RECOMMENDED NAME
GeneOntology No.
Legumain
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
active site His151
P09841, Q9NFY9
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
show the reaction diagram
active site His151 and Cys197
P09841, Q9NFY9
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
show the reaction diagram
the enzyme contains essential catalytic His and Cys residues
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Antigen Sj32
-
-
-
-
Antigen SM32
-
-
-
-
Asparaginyl endopeptidase
-
-
-
-
Bean endopeptidase
-
-
-
-
Phaseolin
-
-
-
-
Proteinase B
-
-
-
-
Vicilin peptidohydrolase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
149371-18-6
-
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
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
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
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
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
Q9XG75
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
Q9XG75
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
A9CQC1
-
-
-
?
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
Q95M12
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
A6Y9U8, A6Y9U9
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
Q95M12
-
-
?
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
A4PF00
recombinant protein
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
Q6PRC7
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
O89017
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
Q99538
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
A4PF00
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
A9CQC1
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
C1K3M8
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
D1M8Z4
-
-
-
?
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
Q95M12
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
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
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
Haemaphysalis longicornis, Haemaphysalis longicornis Okayama
A4PF00
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
O24325
-
-
?
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
Q6PRC7
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
Q6EHZ7
-
-
-
?
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
-
?
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
Q95M12
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
P42665
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
P09841, Q9NFY9
the enzyme is involved in host hemoglobin degradation
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
P42665
the enzyme is involved in host hemoglobin degradation
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
P09841, Q9NFY9
the recombinant beta-galactosidase fusion enzyme shows hemoglobinase activity
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
Q6PRC7
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
A4PF00
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
O24325
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
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
-
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
Q95M12
-
-
?
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
Q95M12
-
-
?
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
Q95M12
cleavage sites are, besides others, N150-Y151, and N83-S84
-
?
vitamin D-binding protein + H2O
?
show the reaction diagram
Q95M12
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
P09841, Q9NFY9
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
Q2UVF3
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
Q208S4
-
-
-
?
Z-Ala-Pro-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Pro-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
P09841, Q9NFY9
-
-
-
?
Z-Ala-Ser-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ser-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
P09841, Q9NFY9
-
-
-
?
ZN-alpha2-glycoprotein + H2O
?
show the reaction diagram
Q95M12
-
-
?
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
?
-
Q95M12
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
?
-
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
?
-
-
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
?
-
P09841, Q9NFY9
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
?
-
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
?
-
P09841
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
?
-
Q0ZHB0
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
?
-
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
-
-
-
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
-
-
?
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
P09841, Q9NFY9
no effect by DTT
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
Q2UVF3
27.5% inhibition at 5 mM
1,10-phenanthroline
A6Y9U8, A6Y9U9
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
Q2UVF3
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
A9CQC1
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
-
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
A6Y9U8, A6Y9U9
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+
A9CQC1
moderate inhibition
carbobenzyloxy-Ala-Ala-(aza-Asn)-epoxycarboxylate ethyl ester
D1M8Z4
-
carbobenzyloxy-Ala-Ala-(aza-Asn)-epoxycarboxylate ethyl ester
C1K3M8
-
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+
A9CQC1
strong inhibition
Cu2+
-
-
Cu2+
-
strong inhibition
Cu2+
A9CQC1
strong inhibition
Cystatin
-
-
-
Cystatin
-
-
-
Cystatin
-
from chicken egg white
-
Cystatin
A9CQC1
from egg white, 62.3% inhibition at 0.003 mM concentration relative to control
-
Cystatin
-
from egg-white
-
cystatin C
-
-
-
cystatin C
-
endogenous inhibitor
-
cystatin C
-
-
-
cystatin C
-
human
-
cystatin E
-
high affinity inhibitor of legumain
-
cystatin E/M
-
-
-
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
A9CQC1
papain-like cysteine proteinase inhibitor, 7.51% inhibition at 0.3 mM concentration relative to control
E64
P09841, Q9NFY9
slight inhibition at 1 mM
E64
Q2UVF3
17.1% inhibition at 0.001 mM
egg white cystatin
A4PF00
concentration of 2 microM, 45.13% inhibition of recombinant protein activity
-
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
FaCPI-1
-
strawberry cystatin, phytocystatin of Fragaria sp.
-
Fe2+
A9CQC1
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
O24325
11.6% remaining activity
iodoacetamide
-
-
iodoacetamide
P09841, Q9NFY9
-
iodoacetamide
A4PF00
concentration of 3 mM, 100% inhibition of recombinant protein activity, BSA cleavage inhibited by 5 mM iodoacetamide
iodoacetamide
A6Y9U8, A6Y9U9
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
Q208S4
complete inhibition at 5 mM inhibitor concentration
iodoacetamide
A9CQC1
100% inhibition at 3 mM concentration relative to control
iodoacetamide
-
-
iodoacetate
-
-
iodoacetate
-
-
iodoacetate
O24325
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
P09841, Q9NFY9
slight inhibition at 1 mM
Leupeptin
Q2UVF3
47.3% inhibition at 1 mM
Leupeptin
A4PF00
concentration of 300 microM, 16.07% inhibition of recombinant protein activity
Leupeptin
A9CQC1
papain-like cysteine proteinase inhibitor, 3.9% inhibition at 0.3 mM concentration relative to control
low molecular mass kininogen
-
-
-
Mg2+
A9CQC1
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
O24325
16.6% remaining activity
N-ethylmaleimide
-
-
N-ethylmaleimide
P09841, Q9NFY9
-
N-ethylmaleimide
-
-
N-ethylmaleimide
Q2UVF3
complete inhibition at 2 mM
N-ethylmaleimide
A4PF00
concentration of 3 mM, 95.74% inhibition of recombinant protein activity
N-ethylmaleimide
A9CQC1
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
Q6EHZ7
-
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
Q6EHZ7
-
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
Q6PRC7
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
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
Q6EHZ7
-
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
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2-furyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2-furyl)propenoyl)hydrazine
Q6EHZ7
-
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
Q6EHZ7
-
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
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
Q6EHZ7
-
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
Q6EHZ7
-
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
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
Q6EHZ7
-
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
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
Q6EHZ7
-
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
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
Q6EHZ7
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
-
-
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
Q6EHZ7
-
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
-
-
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
Q6EHZ7
-
Ni2+
A9CQC1
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
A4PF00
concentration of 500 microM, 7.8% inhibition of recombinant protein activity
pepstatin A
Q2UVF3
8.4% inhibition at 0.1 mM
pepstatin A
-
no effect on ability to cleave the Asn-containing substrate
pepstatin A
A9CQC1
aspartic peptidase inhibitor has minimal effects on the enzyme activity, 12.22% inhibition at 0.3 mM concentration relative to control
phenylmethanesulfonyl fluoride
A4PF00
PMSF, concentration of 5 mM, 19% inhibition of recombinant protein activity
phenylmethanesulfonyl fluoride
A6Y9U8, A6Y9U9
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
A9CQC1
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
A4PF00
E-64, concentration of 500 microM, 8.88% inhibition of recombinant protein activity
Z-Phe-Ala-CHN2
Q2UVF3
i.e. benzyloxycarbonyl-phenylalanyl-alanyl-diazomethane, 40.8% inhibition at 0.01 mM
Zn2+
A9CQC1
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+
A9CQC1
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
O24325
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
P09841, Q9NFY9
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
A6Y9U8, A6Y9U9
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
-
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
Q9M4R6
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
A9CQC1
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
-
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
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.9
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
-
pH 5.0, 37C
46
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
-
pH 5.8, 30C
0.1
benzyloxycarbonyl-Ile-Ser-Asn-4-methylcoumarin-7-amide
-
pH 5.0, 37C
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
-
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
pH 5.8, temperature not specified in the publication
0.00075
Boc-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.00003
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
-
pH 6.8, 25C
0.000045
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
-
pH 6.8, 25C
0.000005
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.000068
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.00002
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
-
pH 6.8, 25C
0.000058
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
-
pH 6.8, 25C
0.0000075
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
-
pH 6.8, 25C
0.000045
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
-
pH 6.8, 25C
0.0000085
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.00008
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.00008
Boc-Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
pH 6.8, 25C
0.00027
Boc-Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
pH 6.8, 25C
0.0000045
Cbz-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.000031
Cbz-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.00000052
Cbz-Ala-Ile-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.00028
Cbz-Ala-Ile-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.0005
Cbz-Ala-Phe-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
pH 6.8, 25C
0.0018
Cbz-Ala-Phe-azaAsn-CH=CH-CONHCH2-furyl
-
pH 6.8, 25C
0.000013
Cbz-Ala-Val-azaAsn-CH=CH-CO-tetrahydroquinoline
-
pH 6.8, 25C
0.000138
Cbz-Ala-Val-azaAsn-CH=CH-CO-tetrahydroquinoline
-
pH 6.8, 25C
0.0005
Cbz-Ala-Val-azaAsn-CH=CH-CO-tetrahydroquinoline
-
pH 6.8, 25C
0.00035
Cbz-Ala-Val-azaAsn-CH=CH-CONHCH2-1-naphthyl
-
pH 6.8, 25C
0.00105
Cbz-Ala-Val-azaAsn-CH=CH-CONHCH2-1-naphthyl
-
pH 6.8, 25C
0.000065
Cbz-Ala-Val-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.0001
Cbz-Ala-Val-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.00000037
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.00005
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.00000035
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
-
pH 6.8, 25C
0.00007
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
-
pH 6.8, 25C
0.00000014
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.00007
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.00075
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
pH 6.8, 25C
0.0008
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
pH 6.8, 25C
0.00075
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroquinoline
-
pH 6.8, 25C
0.00085
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroquinoline
-
pH 6.8, 25C
0.0000115
ethyl (2S,3S)-3-[[2-[[(2S)-1-acetylpyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
-
pH 7.4
0.02
FaCPI-1
-
endosperm
-
0.2
FaCPI-1
-
root extract
-
0.038
HvCPI-4
-
endosperm
-
0.12
HvCPI-4
-
root extract
-
0.018
HvCPI-4-deltaT143-Cterm
-
endosperm
-
0.068
HvCPI-4-deltaT143-Cterm
-
root extract
-
0.022
HvCPI-4-deltaT151-Cterm
-
endosperm
-
0.091
HvCPI-4-deltaT151-Cterm
-
root extract
-
0.033
HvCPI-4-Q86P
-
endosperm
-
0.000065
Mu-Ala-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
pH 6.8, 25C
0.000103
Mu-Ala-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
pH 6.8, 25C
0.0000033
Mu-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.000045
Mu-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.00145
Mu-Ala-Ala-azaAsn-CH=CH-CONHCH2CH2CH2Ph
-
pH 6.8, 25C
0.00000023
Mu-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.000101
Mu-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.0000017
Mu-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
pH 6.8, 25C
0.00009
Mu-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
pH 6.8, 25C
0.000006
Mu-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
-
pH 6.8, 25C
0.00006
Mu-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
-
pH 6.8, 25C
0.0006
Mu-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
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
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
-
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
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
-
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
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
-
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
-
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
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
-
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
-
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
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
-
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
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
-
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
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
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
-
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
-
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
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
-
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
-
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
-
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
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
-
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
-
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
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
-
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
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
-
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
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
-
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
-
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
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
-
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
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
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
-
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
-
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
-
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
-
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
-
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
-
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
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
-
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
-
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
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
-
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
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
-
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
-
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
-
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
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
-
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
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
-
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
-
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
-
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
-
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
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
-
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
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
-
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
-
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
-
pH 6.8, 25C
0.0001
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)-CH2-1-naphthyl
-
pH 6.8, 25C
0.000017
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
-
pH 6.8, 25C
0.00008
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
-
pH 6.8, 25C
0.000008
Pip-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.000057
Pip-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.0004
Pip-Ala-Ala-azaAsn-CH=CH-CONHCH2CH2Ph
-
pH 6.8, 25C
0.00075
Pip-Ala-Ala-azaAsn-CH=CH-CONHCH2CH2Ph
-
pH 6.8, 25C
0.000015
Pip-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.00008
Pip-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.000012
Pip-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
pH 6.8, 25C
0.000072
Pip-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
pH 6.8, 25C
0.0000085
Pip-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
-
pH 6.8, 25C
0.00016
Pip-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
-
pH 6.8, 25C
0.00003
Pip-Ala-Ala-azaAsn-EP(S,S)-COOEt
-
pH 6.8, 25C
0.00022
Pip-Ala-Ala-azaAsn-EP(S,S)-COOEt
-
pH 6.8, 25C
0.00015
Pip-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
pH 6.8, 25C
0.0006
Pip-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
pH 6.8, 25C
0.000031
Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
-
pH 6.8, 25C
0.00009
Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
-
pH 6.8, 25C
0.0000026
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.00007
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
-
pH 6.8, 25C
0.0000038
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
-
pH 6.8, 25C
0.00004
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
-
pH 6.8, 25C
0.000013
Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
-
pH 6.8, 25C
0.00025
Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
-
pH 6.8, 25C
0.0000085
Piz-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.0003
Piz-Ala-Ala-azaAsn-CH=CH-COOEt
-
pH 6.8, 25C
0.000011
Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
pH 6.8, 25C
0.00015
Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
pH 5.8, temperature not specified in the publication
0.11
HvCPI-4-Q86P
-
root extract
-
additional information
additional information
-
inhibitory doses for 50% proteinase activity inhibition higher for root legumain activity than for endosperm one
-
additional information
additional information
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
-
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
-
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
-
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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
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
-
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
-
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
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
-
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
-
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
-
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
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
-
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
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
-
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
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
-
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
-
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
-
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
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000133
A9CQC1
hydrolysis of substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methyl-coumaryl-7-amide
0.00041
A9CQC1
hydrolysis of substrate acetyl-aspartyl-asparaginyl-leucyl-aspartic acid alpha-(4-methylcoumaryl-7-amide)
0.642
A4PF00
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
Q2UVF3
membrane-bound fraction
1.53
-
purified enzyme
4.5
-
purified enzyme
7
-
purified enzyme
7.04
O24325
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
P09841, Q9NFY9
-
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
Q99538
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
O89017
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
Q0ZHB0
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
Q6PRC7
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
A6Y9U8, A6Y9U9
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
P09841
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
Q208S4
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
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
A6Y9U8, A6Y9U9
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
Q6PRC7
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
O24325
assay at
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
6.8
P09841, Q9NFY9
-
7
A4PF00
activity assay at
7
Q208S4
in 0.1 M sodium phosphate
7
A9CQC1
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
D1M8Z4
biphasic pH optima with peaks at pH 4 (about 70% activity) and pH 7.5 (100% activity)
7.5
C1K3M8
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
Q6EHZ7
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
A6Y9U8, A6Y9U9
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
A4PF00
assay under different pH conditions tested
3 - 6
-
-
3.5 - 8
D1M8Z4
-
4 - 6
-
-
4 - 6
Q6PRC7
activity under different pH conditions measured
5.5 - 6.8
P09841, Q9NFY9
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
25
-
assay at
25
-
assay at
30
-
assay at
30
O24325
assay at
35
-
assay at
37 - 45
P09841, Q9NFY9
-
37
-
assay at
37
-
assay at
37
-
assay at
37
Q99538
assay at
37
-
activity assay at
37
O89017
assay of legumain activity at
37
A4PF00
activity assay at
37
A6Y9U8, A6Y9U9
activity assay at; activity assay at
37
Q208S4
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 70
A4PF00
assay under different temperature conditions tested
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
A9CQC1
predicted preprotein
7.1
A9CQC1
predicted preproprotein
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q707T9, Q852T0, Q852T1, Q852T2, Q852T3, Q9XG75, Q9XG76
specific for
Manually annotated by BRENDA team
-
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
Q0ZHB0
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
Q99538
inflamed areas in advanced human coronary atherosclerotic plaques
Manually annotated by BRENDA team
O24325
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
Q707T9, Q852T0, Q852T1, Q852T2, Q852T3, Q9XG75, Q9XG76
anthere only
Manually annotated by BRENDA team
Q6PRC7
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
Q99538
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
Manually annotated by BRENDA team
Q2UVF3
microvillar surface
Manually annotated by BRENDA team
O89017
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
Q9M4R6
enhanced expression in senescent leaves
Manually annotated by BRENDA team
-
leaf extracts, assay for asparaginyl bond hydrolysis in
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
-
LGMN expression is increased in hepatocellular carcinoma cells relative to normal hepatocytes in the same specimens
Manually annotated by BRENDA team
Q99538
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
A4PF00
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
Q99538
fluorimetric assay measuring legumain protease activity applied
Manually annotated by BRENDA team
-
low activity
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
P09841
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
Q0ZHB0
control plants and transformed plants, GFP reporter analysis indicated
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
additional information
Q9XG75
in all vegetative organs, the precursor enzyme is synthesized at membrane-bound polysomes in the cytoplasm
Manually annotated by BRENDA team
additional information
-
no activity in blood leukocytes
Manually annotated by BRENDA team
additional information
-
no activity in native HEK 293 cell
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
-
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
P42665
activity only in adult worms
Manually annotated by BRENDA team
additional information
-
activity only in adult worms
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
Q9M4R6
expression pattern of SPAE
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
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
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
P42665
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
-
Manually annotated by BRENDA team
-
crude worm protein extracts but not in excretion-secretion products of adult parasites, polyclonal antisera and activity assay
Manually annotated by BRENDA team
O89017
lysosomes of renal proximal tubular cells
Manually annotated by BRENDA team
Q6PRC7
association of with microvilli shown
Manually annotated by BRENDA team
Haemaphysalis longicornis Okayama
-
bound
-
Manually annotated by BRENDA team
Q9XG75
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
Q0ZHB0
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
Q2UVF3
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
Q9XG75
proenzyme is probably attached to its storage-protein substrates
-
Manually annotated by BRENDA team
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
A4PF00
removal of a peptide of 9000 Dalton from the preprotein
683541
38000
A9CQC1
endogenous HlLgm2, predicted and confirmed by SDS-PAGE and immunoblot analysis
699391
42000
-
mature processed protein of 42 kDa, Western blot
718221
42500
A9CQC1
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
A4PF00
preprotein, deduced from sequence
683541
47000
Q208S4
determined by SDS-PAGE
698344
47490
A9CQC1
predicted preprotein
699391
49000
-
active form, determined by SDS-PAGE
700314
49630
A9CQC1
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 37000, Ricinus communis, SDS-PAGE
?
-
x * 34000, glycosylated enzyme, SDS-PAGE, x * 31000, deglycosylated enzyme, SDS-PAGE
?
-
x * 35000, wild-type and mutants enzymes, SDS-PAGE
?
O24325
x * 38100, mature enzyme, SDS-PAGE, x * 53400, pre-proenzyme, 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 * 48000, autocatalytically processed enzyme, SDS-PAGE
?
P42665
x * 31000, SDS-PAGE, x * 50000, amino acid sequence calculation of the proenzyme
?
P09841, Q9NFY9
x * 32000, SDS-PAGE, x * 50000, amino acid sequence calculation
?
P09841, Q9NFY9
x * 32000, SDS-PAGE, x * 50000, amino acid sequence calculation of the proenzyme
?
Q2UVF3
x * 49000, about, amino acid sequence calculation, x * 75000, recombinant GST-fusion enzyme, SDS-PAGE
?
-
x * 49000, proenzyme, x * 31000, mature, deglycosylated enzyme
?
P09841
x * 32000, SDS-PAGE, no signals after RNA interference of the SMAE gene encoding schistosome legumain
?
C1K3M8
x * 30000, 2-D electrophoresis
?
D1M8Z4
x * 30000, 2-D electrophoresis
monomer
-
1 * 33000
monomer
-
1 * 22500, Vigna radiata, SDS-PAGE
monomer
-
1 * 33100, glycosylated native enzyme, SDS-PAGE
monomer
-
1 * 34000, reducing SDS-PAGE
monomer
-
1 * 23400
monomer
-
1 * 33000-33800
additional information
-
comparison of the tertiary structure of the enzyme with other cysteine endopeptidases
additional information
-
primary structure determination
additional information
P42665
structure analysis, overview
additional information
-
structure analysis, overview
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
A6Y9U8, A6Y9U9
N-terminal and C-terminal cleavage sites predicted, N-terminal sequence
proteolytic modification
A6Y9U8, A6Y9U9
N-terminal and C-terminal cleavage sites predicted, N-terminal sequence indicated
glycoprotein
-
-
glycoprotein
A9CQC1
asparagine-linked glycosylation
proteolytic modification
A4PF00
cleavage site at asparagines 364-365 at the C-terminus identified in endogenous and in recombinant protein
proteolytic modification
A9CQC1
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
-
-
glycoprotein
-
4 potential N-glycosylation sites at Asn91, ASn167, Asn263, and Asn272
proteolytic modification
-
autocatalytic activation by cleavage of aspartic acid residues, overview
proteolytic modification
-
autolytic activation upon exposure to acidic pH
proteolytic modification
-
the 56 kDa proform is cleavaed to the active 46 kDa and 36 kDa forms
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
Q6PRC7
C-terminus, in endogenous and in recombinant protein
proteolytic modification
Q9XG75
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
Q208S4
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
O24325
but enzyme contains 1 putative N-glycosylation site at N326
proteolytic modification
O24325
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
Q0ZHB0
C-terminus, in endogenous and in recombinant protein
proteolytic modification
P42665
autoactivation
proteolytic modification
P09841, Q9NFY9
autoactivation
proteolytic modification
P09841, Q9NFY9
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
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
-
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
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
Q208S4
no activity at pH 6.0
698344
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography (glutathione-Sepharose)
D1M8Z4
affinity chromatography (glutathione-Sepharose)
C1K3M8
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
A6Y9U8, A6Y9U9
native enzyme from dry seeds, to homogeneity
-
recombinant protein is purified using Ni-Sepharos under native conditions
A9CQC1
recombinant enzyme
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant IgG-fusion protein from cell line COP5
-
using NiNTA chromatography
-
recombinnat His-tagged enzyme
Q9M4R6
recombinant His-tagged enzyme from Escherichia coli, SDS-PAGE
Q6PRC7
recombinant enzyme is purified by affinity chromatography using His-Trap nickel columns
Q208S4
44fold
O24325
native enzyme from germinated seeds, to homogeneity
-
native enzyme from dry seeds, to homogeneity
-
recombinant His-tagged enzyme from Escherichia coli, SDS-PAGE
Q0ZHB0
native enzyme to homogeneity; soluble recombinant C197 from Pichia pastoris, native enzyme to homogeneity
P09841, Q9NFY9
SDS-PAGE
P09841
2200fold from kidney, to homogeneity
-
native enzyme from kidney, overview
-
from cotyledon
-
native enzyme from germinated seeds, to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione S-transferase-fusion protein expressed in Escherichia coli BL21(DE3)
D1M8Z4
glutathione S-transferase-fusion protein expressed in Escherichia coli BL21(DE3)
C1K3M8
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
A6Y9U8, A6Y9U9
expressed in Escherichia coli
A9CQC1
plasmid pTrcHisB/HlLgm transformed into the Escherichia coli Top10F0 strain
A4PF00
gene leg-1, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic tree, expression in Escherichia coli as GST-fusion protein
Q2UVF3
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
-
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
-
gene SPAE or Y192, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression of His-tagged enzyme
Q9M4R6
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
Q6PRC7
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
Q707T9, Q852T0, Q852T1, Q852T2, Q852T3, Q9XG75, Q9XG76
recombinant Ov-AEP-1 is expressed as hexa-His tag in Escherichia coli in inclusion bodies
Q208S4
DNA and amino acid sequence determination and analysis
O24325
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
Q0ZHB0
expressed in Escherichia coli, RNA interference applied to silence expression of the SmAE gene encoding schistosome legumain
P09841
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
P09841, Q9NFY9
partial DNA sequence determination
-
asparaginyl endopeptidase is expressed in Pichia pastoris
Q6EHZ7
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
-
LGMN expression is increased in hepatocellular carcinoma cells relative to normal hepatocytes in the same specimens
-
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
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
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
Q208S4
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
enzyme serves as a promising candidate for prodrug tumor therapy
medicine
Q99538
studies on a functional role of legumain in atherogenesis
medicine
-
studies on a functional role of legumain in atherogenesis
diagnostics
Q208S4
potential for serodiagnosis of human opisthorchiasisas immunodiagnostic antigen
biotechnology
Q0ZHB0
studies on vacuolar targeting, targeting motif of legumain as a potential tool for plant engineering analyzed