Information on EC 3.4.22.34 - Legumain

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
3.4.22.34
-
RECOMMENDED NAME
GeneOntology No.
Legumain
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
149371-18-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
gene SPAE or Y192
SwissProt
Manually annotated by BRENDA team
no endogenous cyclotides, transiently transformed with the cyclotide kalata B1
-
-
Manually annotated by BRENDA team
endogenous cyclotides as potential substrates for backbone cyclization by legumain analyzed
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
encoded by VPE-1 gene; sugarcane, transgenic plants regenerated from callus culture
SwissProt
Manually annotated by BRENDA team
sugarcane cultivar SP80-3280
UniProt
Manually annotated by BRENDA team
the enzyme contains a Cys at position 197
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
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 hide
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
11S proglobulin + H2O
?
show the reaction diagram
Ac-Asp-Asn-Leu-Asp alpha-(4-methylcoumaryl-7-amide) + H2O
Ac-Asp-Asn-Leu-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Ac-Tyr-Val-Ala-Asp-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Pro-Thr-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Pro-Thr-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-Thr-Ala-Asn-4-methylcoumarin-7-amide + H2O
acetyl-Thr-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide + H2O
acetyl-Tyr-Val-Ala-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
AGTHNGQIGA + H2O
AGTHN + GQIGA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived, low activity
-
?
AHIDNEEDIA + H2O
AHIDN + EEDIA
show the reaction diagram
-
low activity, the peptide sequence is also cleaved in tetanus toxoid C fragment of which it is derived
-
?
AHIDNESDIA + H2O
AHIDN + ESDIA
show the reaction diagram
-
low activity
-
?
ALKGNNLIWA + H2O
ALKGN + NLIWA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
allatotropin + H2O
?
show the reaction diagram
-
-
-
?
annexin II + H2O
?
show the reaction diagram
cleavage of the N-terminus, enzyme plays a role in inactivation and degradation of annexin II in endosomes and lysosomes
-
?
AQLKNITDYA + H2O
AQLKN + ITDYA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
AREDNNITLA + H2O
AREDN + NITLA
show the reaction diagram
-
low activity, the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
ARLYNGLKFA + H2O
ARLYN + GLKFA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
ASGFNSSVIA + H2O
ASGFN + SSVIA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
ATITNDRLSA + H2O
ATITN + DLRSA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
AYGTNEYSIA + H2O
AYGTN + EYSIA
show the reaction diagram
-
the peptide sequence is not cleaved in tetanus toxoid C fragment of which it is derived
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
?
azocasein + H2O
fragments of azocasein
show the reaction diagram
-
-
-
-
benzoyl-Asn-4-nitroanilide + H2O
benzoyl-Asn + 4-nitroaniline
show the reaction diagram
benzoyl-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-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-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-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-Ile-Ser-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ile-Ser-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
low activity with
-
?
benzyloxycarbonyl-Leu-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
Benzyloxycarbonyl-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-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-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-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
Boc-Asn-4-nitrophenyl ester + H2O
Boc-Asn + 4-nitrophenol
show the reaction diagram
bombesin + H2O
?
show the reaction diagram
-
-
-
?
bovine albumin + H2O
peptides containing C-terminal Asn
show the reaction diagram
-
-
-
?
bovine haemoglobin + H2O
peptides containing C-terminal Asn
show the reaction diagram
exhibited strict specificity for the asparaginyl bonds on the carboxy-terminal side of a peptide
-
-
?
bovine serum albumin + H2O
3 fragments
show the reaction diagram
-
SDS-denatured substrate, cleavage site are at positions 324 and 404
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
carbobenzyloxy-Ala-Ala-Asn-ethylenediamine-etoposide + H2O
etoposide-ethylenediamine + carbobenzyloxy-Ala-Ala-Asn
show the reaction diagram
-
legumain releases the chemotherapeutic agent etoposide, as the active drug
-
-
?
casein + H2O
?
show the reaction diagram
-
-
?
casein 1 + H2O
2 fragments
show the reaction diagram
-
cleavage site is at position 95
-
?
cathepsin B proform + H2O
activated cathepsin B
show the reaction diagram
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-amido-4-methylcoumarin + H2O
CBZ-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Cbz-Ala-Ala-azaAsn-7-amido-4-methyl-coumarin + H2O
?
show the reaction diagram
chicken vasoactive intestinal peptide fragment 16-28 + H2O
?
show the reaction diagram
-
-
-
?
concanavalin A A-chain + H2O
3 fragments
show the reaction diagram
-
cleavage site are at positions 159 and 163
-
?
concanavalin A precursor + H2O
activated concanavalin A
show the reaction diagram
-
internal excision of the propeptide and transpeptidation that leads to the inverted fusion of the 2 fragments of the precursor
-
?
cystatin E + H2O
?
show the reaction diagram
-
-
-
-
?
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2 + H2O
Dinitrophenyl-Pro-Glu-Ala-Asn + NH4OH
show the reaction diagram
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
GSVKAYTNFDAERD + H2O
GSVKAYTN + FDAERD
show the reaction diagram
synthetic peptide, residues24-37, derived from the N-terminal sequence of bovine annexin II, cleavage at position N31-F32
-
?
Hemoglobin + H2O
?
show the reaction diagram
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
-
?
lysozyme C + H2O
3 fragments
show the reaction diagram
-
cleavage site are at positions 62 and 64
-
?
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 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
phaseolin + H2O
?
show the reaction diagram
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
progelatinase A + H2O
gelatinase
show the reaction diagram
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
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
rat alpha1-macroglobulin + H2O
3 fragments
show the reaction diagram
-
cleavage site are at positions 721 and 899
-
?
recombinant C-fragment of tetanus toxoid + H2O
?
show the reaction diagram
-
cleavage of 3 peptide bonds
-
?
Ser-Glu-Ser-Glu-Asn-Gly-Leu-Glu-Glu-Thr + H2O
Ser-Glu-Ser-Glu-Asn + Gly-Leu-Glu-Glu-Thr
show the reaction diagram
-
-
-
-
serum albumin + H2O
?
show the reaction diagram
-
-
?
SESENGLEET + H2O
SESEN + GLEET
show the reaction diagram
somatostatin + H2O
?
show the reaction diagram
-
-
-
?
succinyl-Tyr-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
succinyl-Tyr-Val-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
tert-butoxycarbonyl-Asn nitrophenyl ester + H2O
tert-butoxycarbonyl-Asn + 4-nitrophenol
show the reaction diagram
Tert-Butoxycarbonyl-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
3 fragments
show the reaction diagram
-
cleavage sites are at Asn26, Asn97, and Asn372, but not Asn337
-
?
tetanus toxoid C fragment + H2O
?
show the reaction diagram
-
cleavage site are at positions 26, 337, and 372
-
?
tetanus toxoid C fragment + H2O
tetanus toxoid fragments
show the reaction diagram
-
cleavage sites are at Asn26, Asn337, and Asn372
-
?
transferrin + H2O
5 fragments
show the reaction diagram
-
cleavage site are at positions 95, 529, 574, and 603
-
?
transferrin + H2O
?
show the reaction diagram
-
-
?
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
-
-
-
Vicilin + H2O
Hydrolyzed vicilin
show the reaction diagram
-
-
-
-
vitamin D-binding protein + H2O
?
show the reaction diagram
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
Z-Ala-Pro-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Pro-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Ala-Ser-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ser-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-ESEN-7-amido-4-methylcoumarin + H2O
Z-ESEN + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-Val-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Val-Ala-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
ZN-alpha2-glycoprotein + H2O
?
show the reaction diagram
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
11S proglobulin + 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
-
?
bovine albumin + H2O
peptides containing C-terminal Asn
show the reaction diagram
A9CQC1
-
-
-
?
bovine haemoglobin + H2O
peptides containing C-terminal Asn
show the reaction diagram
A9CQC1
exhibited strict specificity for the asparaginyl bonds on the carboxy-terminal side of a peptide
-
-
?
cathepsin L + H2O
?
show the reaction diagram
-
processing/activation
-
-
?
cystatin E + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
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
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
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
2,2-dimethyl-propionic acid 3-benzyloxycarbonylamino-4-carbamoyl-2-oxo-butyl ester
-
weak inhibition
2,6-dimethyl-benzoic acid 3-benzyloxycarbonylamino-4-carbamoyl-2-oxo-butyl ester
-
enters cells and causes complete, irreversible inhibition of the enzyme, inhibition of autocatalytic processing in vivo
2-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]piperidine-1-carboxylic acid
-
-
3-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]-3,4-dihydroisoquinoline-2(1H)-carboxylic acid
-
-
4-(2-aminoethyl) benzenesulfonyl fluoride
AEBSF, 45.8% inhibition at 5 mM
4-chloromercuribenzoate
-
-
4-[[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]carbonyl]-1,3-thiazolidine-3-carboxylic acid
-
-
Ac-Tyr-Val-Ala-Asp-chloromethylketone
-
the rate of inhibition by Asp-CMK is approximately 3times more rapid at pH 4.0 than at pH 5.5
acetyl-Glu-Ser-Glu-Asn-aldehyde
Acetyl-Tyr-Val-Ala-Asp-aldehyde
Ala-Ala-Asn-chloromethylketone
-
the rate of inhibition by Asn-CMK is approximately 1.3times more rapid at pH 5.5 than at pH 4.0
alpha-2-Macroglobulin
-
proteinase inhibitor, may be a candidate for the binding of legumain as it is an agent for the removal of endopeptidases from extracellular fluids
-
antipain
papain-like cysteine proteinase inhibitor, 28.77% inhibition at 0.1 mM concentration relative to control
asparaginyl endopeptidase inhibitor
-
i.e. AEPi or cysteine protease inhibitor
-
atorvastatin
-
-
benzoic acid 3-benzyloxycarbonylamino-4-carbamoyl-2-oxo-butyl ester
-
-
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-benzyloxymethylketone
-
moderate inhibition
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-bromoacetate
-
-
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-bromomethylketone
-
strong specific and irreversible inhibition
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-chloroacetate
-
-
benzyloxycarbonyl-L-Ala-L-Ala-azaAsn-chloromethylketone
Benzyloxycarbonyl-Phe-Ala-CHN2
-
-
Boc-azaAsn-CH=CH-COOEt
-
-
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Boc-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
Boc-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
Boc-Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Ca2+
moderate inhibition
carbobenzyloxy-Ala-Ala-(aza-Asn)-epoxycarboxylate ethyl ester
caspase 1 inhibitor V
-
-
-
Cbz-Ala-Ala-azaAsn-CH=CH-COOEt
Cbz-Ala-Ile-azaAsn-CH=CH-COOEt
Cbz-Ala-Phe-azaAsn-CH=CH-CO-tetrahydroisoquinoline
-
-
Cbz-Ala-Phe-azaAsn-CH=CH-CONHCH2-furyl
-
-
Cbz-Ala-Val-azaAsn-CH=CH-CO-tetrahydroquinoline
Cbz-Ala-Val-azaAsn-CH=CH-CONHCH2-1-naphthyl
Cbz-Ala-Val-azaAsn-CH=CH-COOEt
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Cbz-Piz-Ala-Ala-azaAsn-CH=CH-COOEt
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Cbz-Piz-Ala-azaAsn-CH=CH-CO-tetrahydroquinoline
Cd2+
-
-
Co2+
strong inhibition
Cystatin
cystatin 3
strong inhibition
-
cystatin C
cystatin CPI-4
-
-
-
cystatin E
-
high affinity inhibitor of legumain
-
cystatin E/M
cystatin M
diisopropyl fluorophosphate
E-64
papain-like cysteine proteinase inhibitor, 7.51% inhibition at 0.3 mM concentration relative to control
egg white cystatin
concentration of 2 microM, 45.13% inhibition of recombinant protein activity
-
ethyl (2E)-4-[1-(2-amino-2-oxoethyl)-2-[[(2S)-1-(2-oxopropanoyl)pyrrolidin-2-yl]carbonyl]hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[(2E)-2-(acetylamino)but-2-enoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)-3-(4-hydroxy-3-nitrophenyl)propanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)butanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)pent-4-ynoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[2-(acetylamino)-2-methylpropanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[2-(acetylamino)-3-methylbut-2-enoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[3-(acetylamino)benzoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-([(2S)-1-[4-(acetylamino)benzoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-[[(2S)-1-[[(2R)-1-acetylpiperidin-2-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-[[(2S)-1-[[(3S)-2-acetyl-1,2,3,4-tetrahydroisoquinolin-3-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-[[(2S)-1-[[(4S)-3-acetyl-1,3-thiazolidin-4-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2E)-4-[2-[[(2S)-1-[[1-(acetylamino)cyclopropyl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
-
-
ethyl (2S,3S)-3-[[1-(2-amino-2-oxoethyl)-2-[([2S)-1-(2-oxopropanoyl)pyrrolidin-2-yl]carbonyl]hydrazinyl]carbonyl]oxirane-2-carboxylate
-
-
ethyl (2S,3S)-3-[[2-([(2S)-1-[(2R)-2-(acetylamino)butanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
-
-
ethyl (2S,3S)-3-[[2-([(2S)-1-[(2R)-2-(acetylamino)pent-4-ynoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
-
-
ethyl (2S,3S)-3-[[2-[[(2S)-1-acetylpyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
-
starting structure for development of activity-based probes for in vivo imaging
ethyl (2S,3S)-3-[[2-[[(2S)-1-[[1-(acetylamino)cyclopropyl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
-
-
FaCPI-1
-
strawberry cystatin, phytocystatin of Fragaria sp.
-
Fe2+
strong inhibition
High molecular weight kininogen
-
-
-
High-molecular mass kininogen
-
kinin-free, F1.2-free
-
Human cystatin C
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
iodoacetate
L-3-carboxy-2,3-trans-epoxypropionyl-leucyl-amido(4-guanidino)butane
Leupeptin
low molecular mass kininogen
-
-
-
Mg2+
moderate inhibition
Mn2+
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-Phenylmaleimide
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E)-4-oxo-4-phenylbut-2-enoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
N-[(2S)-1-{2-(2-amino-2-oxoethyl)-2-[(2E,4E)-hexa-2,4-dienoyl]hydrazinyl}-1-oxopropan-2-yl]-N2-[(benzyloxy)carbonyl]-L-alaninamide
N-[(benzyloxy)carbonyl]-L-alanyl-N-[(1S,3E)-1-(2-amino-2-oxoethyl)-5-[methyl(naphthalen-1-yl)amino]-2,5-dioxopent-3-en-1-yl]-L-alaninamide
i.e. aza-peptide Michael acceptor Aza-Asn-11a, inhibition of trans-processing and activation of the zymogen form of Schistosoma mansoni cathepsin B1 by prior incubation with the legumain-specific inhibitor Aza-Asn-11a, reaction in CPS buffer, pH 5.5 for 30 min
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1,3-dihydroisoindol-2-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(1-piperidylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2,3-dihydroindol-1-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(2-furyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-1H-quinolin-2-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3,4-dihydro-2H-quinolin-1-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(3-pyridyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-fluorobenzyl)carbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(4-phenyl-5,6-dihydro-2H-pyridin-1-ylcarbonyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methyl-1-naphthylmethylcarbamoyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenethylcarbamoyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-(methylphenylcarbamoyl)propenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-benzylmethylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-bis-(2-furylmethyl)carbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibenzylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-dibutylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-diethylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenethylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylbenzylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-phenylcarbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-carbamoylmethyl-N1-trans-3-(N-methyl-N-(1-(N-methyl-N-phenethylcarbamoyl)phenylethyl)carbamoylpropenoyl)hydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl(4-fluorobenzyl)carbamoylpropenoyl)-N1-carbamoylmethylhydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-1-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyl-2-naphthylmethylcarbamoylpropenoyl)-N1-carbamoylmethylhydrazine
N2-(N-benzyloxycarbonylalanylalanyl)-N1-trans-(3-benzyloxycarbonylpropenoyl)-N1-carbamoylmethylhydrazine
N2-(N-biotinylalanylalanyl)-N1-carbamoylmethyl-N1-trans-(3-ethoxycarbonylpropenoyl)hydrazine
Ni2+
strong inhibition
ovocystatin
p-chloromercuribenzene sulfonic acid
-
-
p-chloromercuribenzene-sulfonic acid
-
-
p-chloromercuribenzoate
-
-
Pepstatin
concentration of 500 microM, 7.8% inhibition of recombinant protein activity
pepstatin A
phenylmethanesulfonyl fluoride
phenylmethylsulfonyl fluoride
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)-CH2-1-naphthyl
Pip-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
Pip-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Pip-Ala-Ala-azaAsn-CH=CH-CONHCH2CH2Ph
Pip-Ala-Ala-azaAsn-CH=CH-COOEt
Pip-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
Pip-Ala-Ala-azaAsn-EP(S,S)-CONHCH2-1-naphthyl
Pip-Ala-Ala-azaAsn-EP(S,S)-COOEt
Pip-Ala-azaAsn-CH=CH-CO-tetrahydroisoquinoline
Piz-Ala-Ala-azaAsn-CH=CH-CON(Bzl)2
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH2-1-naphthyl)2
Piz-Ala-Ala-azaAsn-CH=CH-CON(CH3)CH2-1-naphthyl
Piz-Ala-Ala-azaAsn-CH=CH-COOBzl
Piz-Ala-Ala-azaAsn-CH=CH-COOEt
Piz-Ala-Ala-azaAsn-EP(S,S)-CON(Bzl)2
PMSF
serine peptidase inhibitor, 13.84% inhibition at 5 mM concentration relative to control
rat alpha1-macroglobulin
-
-
-
tosyl-Phe-CH2Cl
-
-
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane
trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane
E-64, concentration of 500 microM, 8.88% inhibition of recombinant protein activity
Z-Phe-Ala-CHN2
i.e. benzyloxycarbonyl-phenylalanyl-alanyl-diazomethane, 40.8% inhibition at 0.01 mM
Zn2+
moderate inhibition
[(2S)-1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-3-[4-hydroxy-3-[hydroxy(oxo)ammonio]phenyl]-1-oxopropan-2-yl]carbamate
-
-
[(2Z)-1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-1-oxobut-2-en-2-yl]carbamic acid
-
-
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-1-oxobutan-2-yl]carbamic acid
-
-
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-1-oxopent-4-yn-2-yl]carbamic acid
-
-
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-2-methyl-1-oxopropan-2-yl]carbamic acid
-
-
[1-[(2S)-2-([2-(2-amino-2-oxoethyl)-2-[(2E)-4-ethoxy-4-oxobut-2-enoyl]hydrazinyl]carbonyl)pyrrolidin-1-yl]-3-methyl-1-oxobut-2-en-2-yl]carbamic acid
-
-
[1-[(2S)-2-[[2-(2-amino-2-oxoethyl)-2-[[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]hydrazinyl]carbonyl]pyrrolidin-1-yl]-1-oxobutan-2-yl]carbamic acid
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
10 mM, 300% activation
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.122 - 0.286
acetyl-Pro-Thr-Asn-4-methylcoumarin-7-amide
0.07 - 0.128
acetyl-Thr-Ala-Asn-4-methylcoumarin-7-amide
0.05 - 0.67
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
0.023 - 0.033
Dinitrophenyl-Pro-Glu-Ala-Asn-NH2
additional information
additional information
-
-
-