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Information on EC 3.4.22.34 - Legumain and Organism(s) Mus musculus and UniProt Accession O89017
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3.4.22.34 LegumainSpecify your search results
Word Map
- 3.4.22.34
- cathepsins
- phaseolus
- vulgaris
- vacuole
- cystatins
- proteinases
- metastasis
- papain
- cotyledon
- plasmodium
- globulin
- falciparum
- vicilins
- schistosoma
-
papain-like
- tau
-
legume
- endopeptidases
-
seed-specific
-
mesoamerican
- phytohemagglutinin
- falcipain-2
-
clan
- mansoni
-
andean
-
leguminous
-
procathepsins
- lunatus
-
cyclotides
-
jack
-
caspase-1-like
- drug development
- biotechnology
- medicine
- diagnostics
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
legumain, phaseolin, asparaginyl endopeptidase, lysosomal cysteine proteinase, vacuolar processing enzyme, hemoglobinase, asparagine endopeptidase, vicilin peptidohydrolase, hllgm, hllgm2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Antigen Sj32
-
-
-
-
Antigen SM32
-
-
-
-
Asparaginyl endopeptidase
Bean endopeptidase
-
-
-
-
Phaseolin
-
-
-
-
Proteinase B
-
-
-
-
Vicilin peptidohydrolase
-
-
-
-
Asparaginyl endopeptidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
the enzyme contains essential catalytic His and Cys residues
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
149371-18-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
effect of legumain on fibronectin degradation analyzed, role of legumain in control of extracellular matrix turnover determined
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Cbz-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Cbz-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
-
?
acetoacetyl-CoA synthetase + H2O
?
Asn547 is the specific cleavage site of acetoacetyl-CoA synthetase in mouse livers. The cleaved form of acetoacetyl-CoA synthetase (1-547) loses the ability to convert acetoacetate to acetoacetyl-CoA. Cleavage of acetoacetyl-CoA synthetase by legumain is critical for the regulation of enzymatic activity and results in gain-of-function changes. Acetoacetyl-CoA synthetase(1-547) increases the protein expression of caveolin-1, the principal component of the caveolae
-
-
?
acetoacetyl-CoA synthetase + H2O
?
Asn547 is the specific cleavage site of acetoacetyl-CoA synthetase in mouse livers. The cleaved form of acetoacetyl-CoA synthetase (1-547) loses the ability to convert acetoacetate to acetoacetyl-CoA
-
-
?
protein + H2O
peptides
-
substrate specificity is dominated by the interaction of the S1 subsite
-
?
additional information
?
-
role in extracellular matrix remodeling via degradation of fibronectin indicated
-
-
?
additional information
?
-
-
role in extracellular matrix remodeling via degradation of fibronectin indicated
-
-
?
additional information
?
-
-
the enzyme is not required for class II MHC antigen presentation but is essential for processing of cathepsin L in mice
-
-
?
additional information
?
-
-
asparaginyl endopeptidase plays a pivotal role in the endosome and lysosomal degradation system and is implicated in antigen processing and presentation
-
-
?
additional information
?
-
-
asparaginyl endopeptidaseprotein substrates on the C-terminal side of asparagine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetoacetyl-CoA synthetase + H2O
?
Asn547 is the specific cleavage site of acetoacetyl-CoA synthetase in mouse livers. The cleaved form of acetoacetyl-CoA synthetase (1-547) loses the ability to convert acetoacetate to acetoacetyl-CoA. Cleavage of acetoacetyl-CoA synthetase by legumain is critical for the regulation of enzymatic activity and results in gain-of-function changes. Acetoacetyl-CoA synthetase(1-547) increases the protein expression of caveolin-1, the principal component of the caveolae
-
-
?
additional information
?
-
role in extracellular matrix remodeling via degradation of fibronectin indicated
-
-
?
additional information
?
-
-
role in extracellular matrix remodeling via degradation of fibronectin indicated
-
-
?
additional information
?
-
-
the enzyme is not required for class II MHC antigen presentation but is essential for processing of cathepsin L in mice
-
-
?
additional information
?
-
-
asparaginyl endopeptidase plays a pivotal role in the endosome and lysosomal degradation system and is implicated in antigen processing and presentation
-
-
?
additional information
?
-
-
asparaginyl endopeptidaseprotein substrates on the C-terminal side of asparagine
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
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
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
asparaginyl endopeptidase activation is autocatalytic and requires sequential removal of C- and N-terminal propeptides at different pH thresholds
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000704
(3S)-3-[(1-acetyl-L-prolyl)amino]-5-[(2,6-dimethylbenzoyl)oxy]-4-oxopentanoic acid
Mus musculus
-
pH 7.4
0.0083
ethyl (2E)-4-[1-(2-amino-2-oxoethyl)-2-[[(2S)-1-(2-oxopropanoyl)pyrrolidin-2-yl]carbonyl]hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000141
ethyl (2E)-4-[2-([(2S)-1-[(2E)-2-(acetylamino)but-2-enoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.001
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)-3-(4-hydroxy-3-nitrophenyl)propanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0000065
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)butanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000017
ethyl (2E)-4-[2-([(2S)-1-[(2R)-2-(acetylamino)pent-4-ynoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000198
ethyl (2E)-4-[2-([(2S)-1-[2-(acetylamino)-2-methylpropanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000148
ethyl (2E)-4-[2-([(2S)-1-[2-(acetylamino)-3-methylbut-2-enoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.001
ethyl (2E)-4-[2-([(2S)-1-[3-(acetylamino)benzoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000267
ethyl (2E)-4-[2-([(2S)-1-[4-(acetylamino)benzoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000638
ethyl (2E)-4-[2-[[(2S)-1-[[(2R)-1-acetylpiperidin-2-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.001
ethyl (2E)-4-[2-[[(2S)-1-[[(3S)-2-acetyl-1,2,3,4-tetrahydroisoquinolin-3-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.000167
ethyl (2E)-4-[2-[[(2S)-1-[[(4S)-3-acetyl-1,3-thiazolidin-4-yl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0000093
ethyl (2E)-4-[2-[[(2S)-1-[[1-(acetylamino)cyclopropyl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]-4-oxobut-2-enoate
Mus musculus
-
in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0093
ethyl (2S,3S)-3-[[1-(2-amino-2-oxoethyl)-2-[([2S)-1-(2-oxopropanoyl)pyrrolidin-2-yl]carbonyl]hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0081
ethyl (2S,3S)-3-[[2-([(2S)-1-[(2R)-2-(acetylamino)butanoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0086
ethyl (2S,3S)-3-[[2-([(2S)-1-[(2R)-2-(acetylamino)pent-4-ynoyl]pyrrolidin-2-yl]carbonyl)-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
0.0000115
ethyl (2S,3S)-3-[[2-[[(2S)-1-acetylpyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
pH 7.4
0.0044
ethyl (2S,3S)-3-[[2-[[(2S)-1-[[1-(acetylamino)cyclopropyl]carbonyl]pyrrolidin-2-yl]carbonyl]-1-(2-amino-2-oxoethyl)hydrazinyl]carbonyl]oxirane-2-carboxylate
Mus musculus
-
IC50 above 0.001 mM, in 0.1 M citrate-phosphate, 4 mM dithiothreitol, pH 5.8, at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
assay of legumain activity described, fibronectin degradation by legumain shown, enhanced fibronectin processing by overexpression of legumain indicated, experimental design of unilateral ureteral obstruction reveals increased protein accumulation of fibronectin in the renal interstitial area in kidneys from legumain-deficient mice
additional information
-
assay of legumain activity described, fibronectin degradation by legumain shown, enhanced fibronectin processing by overexpression of legumain indicated, experimental design of unilateral ureteral obstruction reveals increased protein accumulation of fibronectin in the renal interstitial area in kidneys from legumain-deficient mice
additional information
expression determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
-
expression determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
-
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
-
asparaginyl endopeptidase deficiency provokes extramedullary hematopoiesis in the spleen and abnormally enlarged histiocytes with ingested red blood cells in bone marrow
additional information
-
asparaginyl endopeptidase depletion evidently enhances the phagocytic activity, suggesting that phagocytic activity of macrophages in asparaginyl endopeptidase-/- mice is elevated
additional information
-
disruption of asparaginyl endopeptidase leads to late endosomes and lysosomes augmentation and dislocation from the apical region of the kidney-proximal tubule cells and the abnormal lysosomes contained in electron-dense or membranous materials
additional information
-
in contrast to the enhanced macrophage activity, the natural killer cell activity in the asparaginyl endopeptidase-null animal is significantly reduced
additional information
-
mutant mice lacking asparaginyl endopeptidase develop fever, cytopenia, hepatosplenomegaly and hemophagocytosis, which are primary pathological manifestations of hemophagocytic syndrome/hemophagocytic lymphohistiocytosis
additional information
-
myeloid cells are also increased in the asparaginyl endopeptidase-null mice, e.g. 10.2% in asparaginyl endopeptidase-null mice versus 1.2% in wild-type
additional information
-
red blood cells from asparaginyl endopeptidase-null mice are defective in plasma membrane components
additional information
-
the liver is significantly enlarged in asparaginyl endopeptidase deficient mice as compared with the normal counterparts
additional information
-
the percentage of Ter-119+/CD45+ erythroid lineage cells in the spleen is increased in the asparaginyl endopeptidase-deficient mice, e.g. 18.2% in a representative asparaginyl endopeptidase-null mouse compared with just 0.4% in a wild type control
additional information
-
the processing of the lysosomal proteases cathepsins in kidney is completely defective in asparaginyl endopeptidase-deficient mice with accumulation of macromolecules in the lysosomes, which is typically seen in lysosomal disorders
additional information
-
the spleens from asparaginyl endopeptidase-null mice are 5-10times larger than those of wild type controls
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
asparaginyl endopeptidase activation requires sequential removal of C- and N-terminal propeptides at different pH thresholds
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
14-week-old male C57BL/6J wild-type and legumain-deficient mice analyzed
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
lesions at the aortic sinus and in injured carotid arteries of Apolipoprotein E deficient mice, mRNA expression increases with development of atherosclerosis in the aorta
protein from kidney tissues used for western blot analysis, unilateral ureteral obstruction in legumain-deficient mice
of atherosclerotic aorta of aging Apolipoprotein E deficient mice, mRNA expression increases with development of atherosclerosis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
cleavage of acetoacetyl-CoA synthetase by legumain is critical for the regulation of enzymatic activity and results in gain-of-function changes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LGMN_MOUSE
435
0
49373
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
comparison of the tertiary structure of the enzyme with other cysteine endopeptidases
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AEP -/-, +/- and +/+ mice on a mixed 129/Ola and C57BL/6 background are generated
-
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
ORGANISM
UNIPROT
LITERATURE
expression levels of legumain mRNA and protein and legumain activity are increased in DJ-1-knockout cells. Legumain expression and activation is regulated by DJ-1 through p53
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Halfon, S.; Patel, S.; Vega, F.; Zurawski, S.; Zurawski, G.
Autocatalytic activation of human legumain at aspartic acid residues
FEBS Lett.
438
114-118
1998
Homo sapiens, Mus musculus (O89017), Mus musculus
Chen, J.M.; Rawlings, N.D.; Stevens, R.A.E.; Barrett, A.J.
Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of endopeptidases
FEBS Lett.
441
361-365
1998
Mus musculus
Chen, J.; Dando, P.M.; Barrett, A.J.
Mammalian legumain
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1302-1305
2004
Homo sapiens, Mus musculus, Sus scrofa
-
Maehr, R.; Hang, H.C.; Mintern, J.D.; Kim, Y.M.; Cuvillier, A.; Nishimura, M.; Yamada, K.; Shirahama-Noda, K.; Hara-Nishimura, I.; Ploegh, H.L.
Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice
J. Immunol.
174
7066-7074
2005
Mus musculus
Clerin, V.; Shih, H.H.; Deng, N.; Hebert, G.; Resmini, C.; Shields, K.M.; Feldman, J.L.; Winkler, A.; Albert, L.; Maganti, V.; Wong, A.; Paulsen, J.E.; Keith, J.C.; Vlasuk, G.P.; Pittman, D.D.
Expression of the cysteine protease legumain in vascular lesions and functional implications in atherogenesis
Atherosclerosis
201
53-66
2008
Mus musculus (O89017), Mus musculus, Homo sapiens (Q99538), Homo sapiens
Morita, Y.; Araki, H.; Sugimoto, T.; Takeuchi, K.; Yamane, T.; Maeda, T.; Yamamoto, Y.; Nishi, K.; Asano, M.; Shirahama-Noda, K.; Nishimura, M.; Uzu, T.; Hara-Nishimura, I.; Koya, D.; Kashiwagi, A.; Ohkubo, I.
Legumain/asparaginyl endopeptidase controls extracellular matrix remodeling through the degradation of fibronectin in mouse renal proximal tubular cells. [Erratum to document cited in CA146:460121]
FEBS Lett.
581
3579
2007
Mus musculus (O89017), Mus musculus
Chan, C.B.; Abe, M.; Hashimoto, N.; Hao, C.; Williams, I.R.; Liu, X.; Nakao, S.; Yamamoto, A.; Li, S.Y.; Hara-Nishimura, I.; Asano, M.; Ye, K.
Mice lacking asparaginyl endopeptidase develop disorders resembling hemophagocytic syndrome
Proc. Natl. Acad. Sci. USA
106
468-473
2009
Mus musculus
Lee, J.; Bogyo, M.
Development of near-infrared fluorophore (NIRF)-labeled activity-based probes for in vivo imaging of legumain
Chem. Biol.
5
233-243
2010
Mus musculus
Lee, J.; Bogyo, M.
Synthesis and evaluation of aza-peptidyl inhibitors of the lysosomal asparaginyl endopeptidase, legumain
Bioorg. Med. Chem. Lett.
22
1340-1343
2011
Homo sapiens, Mus musculus
Hasegawa, S.; Inoue, D.; Yamasaki, M.; Li, C.; Imai, M.; Takahashi, N.; Fukui, T.
Site-specific cleavage of acetoacetyl-CoA synthetase by legumain
FEBS Lett.
590
1592-1601
2016
Mus musculus (O89017), Mus musculus
Yamane, T.; Yamamoto, Y.; Nakano, Y.; Nakagaki, T.; Ohkubo, I.; Ariga, H.
Expression and protease activity of mouse legumain are regulated by the oncogene/transcription co-activator, DJ-1 through p53 and cleavage of annexin A2 is increased in DJ-1-knockout cells
Biochem. Biophys. Res. Commun.
467
472-477
2015
Mus musculus (O89017), Mus musculus
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