3.4.22.34: Legumain
This is an abbreviated version!
For detailed information about Legumain, go to the full flat file.
Word Map on EC 3.4.22.34
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3.4.22.34
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cathepsins
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phaseolus
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vulgaris
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vacuole
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cystatins
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proteinases
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metastasis
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papain
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cotyledon
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plasmodium
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globulin
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falciparum
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vicilins
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schistosoma
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papain-like
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tau
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legume
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endopeptidases
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seed-specific
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mesoamerican
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phytohemagglutinin
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falcipain-2
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clan
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mansoni
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andean
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leguminous
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procathepsins
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lunatus
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cyclotides
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jack
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caspase-1-like
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drug development
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biotechnology
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medicine
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diagnostics
- 3.4.22.34
- cathepsins
- phaseolus
- vulgaris
- vacuole
- cystatins
- proteinases
- metastasis
- papain
- cotyledon
- plasmodium
- globulin
- falciparum
- vicilins
- schistosoma
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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
Reaction
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds =
Synonyms
AEP, Antigen Sj32, Antigen SM32, As-specific vacuolar cysteine proteinase, Asn-specific vacuolar cysteine proteinase, asparagine endopeptidase, asparaginly endopeptidase, asparaginyl endopepidase, Asparaginyl endopeptidase, asparaginyl endopeptidase legumain, asparaginyl endopeptidase,, asparaginyl proteinase, asparaginyl-specific cysteine endopeptidase, asparagyl-endopeptidase, aspartate-specific endopeptidase, AtLEGgamma, Bean endopeptidase, C197 legumain, c197 Sm32, cysteine protease 1, hemoglobinase, HlLgm, HlLgm2, IrAE, IrAE protein, isae1, isae2, LeG, LEG-1, Leg-2, Leg-4, Leg1, Leg2, Leg3, Leg4, Leg5, legumain, legumain-1, LGMN, lysosomal asparaginycysteine endopeptidase, lysosomal asparaginyl endopeptidase, lysosomal cysteine proteinase, More, N197 legumain, osteoclast inhibitory peptide 2, Ov-aep-1, Phaseolin, Proteinase B, PrVPE1, schistosome legumain, Sj32, Sm32, SmAE, SmAE protein, SPAE, TcLEG3, TcLEG6, TcLEG9, TvAE1, vacuolar processing enzyme, vacuolar processing enzyme 1a, vacuolar processing enzyme 1b, vacuolar processing enzyme 2, vacuolar processing enzyme 3, Vicilin peptidohydrolase, VPE, VPE1a, VPE1b, VPE2, VPE3
ECTree
3.4.22.34 LegumainAdvanced search results
results (
results (Specific Activity
Specific Activity on EC 3.4.22.34 - Legumain
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SPECIFIC ACTIVITY [µmol/min/mg] 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
0.000133
hydrolysis of substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methyl-coumaryl-7-amide
0.00041
hydrolysis of substrate acetyl-aspartyl-asparaginyl-leucyl-aspartic acid alpha-(4-methylcoumaryl-7-amide)
0.642
recombinant protein, 37°C, pH 7, benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide, activity profile shown, inhibition assay described, up-regulation by the host blood-feeding process shown by in vitro proteolysis assay
8.1
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purified enzyme, substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide, pH 5.8, 30°C
additional information
additional information
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay described, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing indicated
additional information
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay described, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing indicated
additional information
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activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay described, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing indicated
additional information
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing
additional information
activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing
additional information
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activity profile shown in crude worm protein extracts but not in excretion-secretion products of adult parasites, inhibition assay, exon boundaries, landmark residues/motifs, and target areas for N- and C-terminal processing
additional information
ability of carboxy-terminal extensions and mutants of phytocystatin to inhibit in vitro human legumain shown, inhibitory activity measured by the inhibition of legumain proteinase activity, assay described
additional information
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ability of carboxy-terminal extensions and mutants of phytocystatin to inhibit in vitro human legumain shown, inhibitory activity measured by the inhibition of legumain proteinase activity, assay described
additional information
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
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expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed
additional information
expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed, human monocyte legumain activity assay described, migration/proliferation and invasion assay described
additional information
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expression in atherosclerotic tissues determined by RT-PCR, in situ hybridization and immunohistochemical analysis, role of legumain in the pathophysiology of atherosclerosis analyzed, human monocyte legumain activity assay described, migration/proliferation and invasion assay described
additional information
positional scanning combinatorial library of peptide acyloxymethyl ketones (AOMKs) to probe subsite specificity of legumain, design of fluorescent activity-based probes indicating high selectivity and cell-permeability for monitoring legumain activity in complex proteome structures, selectivity of optimized legumain probes in intact cells shown, structure of developed probes indicated
additional information
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positional scanning combinatorial library of peptide acyloxymethyl ketones (AOMKs) to probe subsite specificity of legumain, design of fluorescent activity-based probes indicating high selectivity and cell-permeability for monitoring legumain activity in complex proteome structures, selectivity of optimized legumain probes in intact cells shown, structure of developed probes indicated
additional information
role of legumain in the pathophysiology of atherosclerosis analyzed, human monocyte legumain activity assay described, migration/proliferation and invasion assay described
additional information
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role of legumain in the pathophysiology of atherosclerosis analyzed, human monocyte legumain activity assay described, migration/proliferation and invasion assay described
additional information
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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
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HEK-293-overexpressing legumain cells cleave 100% of the prodrug carbobenzyloxy-Ala-Ala-Asn-ethylenediamine-etoposide, whereas HEK-293 cells, which express low levels of legumain, cleave only 33% of it
additional information
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ability of carboxy-terminal extensions and mutants of phytocystatin to inhibit endogenous legumain activity present in barley protein extracts analyzed, inhibitory activity measured by the inhibition of legumain proteinase activity, assay described
additional information
activity profile shown, specificity profile using a positional scanning synthetic combinatorial library indicated
additional information
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activity profile shown, specificity profile using a positional scanning synthetic combinatorial library indicated
additional information
assay of legumain activity described, fibronectin degradation by legumain shown, enhanced fibronectin processing by overexpression of legumain indicated, experimental design of unilateral ureteral obstruction reveals increased protein accumulation of fibronectin in the renal interstitial area in kidneys from legumain-deficient mice
additional information
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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
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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
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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
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asparaginyl endopeptidase deficiency provokes extramedullary hematopoiesis in the spleen and abnormally enlarged histiocytes with ingested red blood cells in bone marrow
additional information
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asparaginyl endopeptidase depletion evidently enhances the phagocytic activity, suggesting that phagocytic activity of macrophages in asparaginyl endopeptidase-/- mice is elevated
additional information
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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
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in contrast to the enhanced macrophage activity, the natural killer cell activity in the asparaginyl endopeptidase-null animal is significantly reduced
additional information
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mutant mice lacking asparaginyl endopeptidase develop fever, cytopenia, hepatosplenomegaly and hemophagocytosis, which are primary pathological manifestations of hemophagocytic syndrome/hemophagocytic lymphohistiocytosis
additional information
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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
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red blood cells from asparaginyl endopeptidase-null mice are defective in plasma membrane components
additional information
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the liver is significantly enlarged in asparaginyl endopeptidase deficient mice as compared with the normal counterparts
additional information
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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
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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
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the spleens from asparaginyl endopeptidase-null mice are 5-10times larger than those of wild type controls
additional information
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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
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involvement of legumain in backbone cyclization of plant-produced cyclotides analyzed, assay for asparaginyl bond hydrolysis in leaf extracts described
additional information
the specific activity of recombinant asparaginyl endopeptidase is lower than that detected for excretory-secretory products of adult worm
additional information
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the specific activity of recombinant asparaginyl endopeptidase is lower than that detected for excretory-secretory products of adult worm
additional information
cleavage sites for N- and C-terminus indicated, predicted motif for vacuolar proteins analyzed, targeting ability sucessfully tested in Saccharum officinarum and in other plant species by transient expression analysis after biolistic bombardment using the construct pCvsEndoexp1
additional information
expression of the SmAE gene in adult Schistosoma mansoni suppressed by RNA interference, full processing and activity of cathepsin B1 in the absence of detectable SmAE protein observed, experimental data indicate that schistosome legumain is not essential to activate cathepsin B1 in vivo
additional information
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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
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involvement of legumain in backbone cyclization of plant-produced cyclotides analyzed, assay for asparaginyl bond hydrolysis in leaf extracts described
