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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

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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.34 Legumain

Expression

Expression on EC 3.4.22.34 - Legumain

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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
bafilomycin A1 enhances the secretion of the the enzyme, which is also is up-regulated in tumour and tumour-associated cells
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enzyme expression is not affected by jasmonic acid and gibberellic acid
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
in the cotyledons of germinating seeds, the accumulation of transcripts of gene TcLeg3 decreases 90fold from the initial time (quiescent seed) to the 30th day
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in the cotyledons of germinating seeds, the TcLeg9 expression rises from time zero to the 20th day, with an approximate 64fold increase as compared to the control
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IsAE1 expression was strongly upregulated by feeding when the mRNA levels in unfed and fully fed samples are compared. However, IsAE1 mRNA is also detectable at relatively high levels in unfed larvae, almost comparable with fully fed females
isoform Leg-2 mRNA expression responds in leaves to biotic and abiotic stimuli, such as salicylic acid, jasmonic acid, nitric oxide, abscisic acid, and aphid infestation, and is induced by gibberellic acid in seeds. Isoform Leg-4 responds in leaves to wounding, nitric oxide, and abscisic acid treatments
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isoform Leg-4 is repressed after abscisic acid exposure
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isoform Leg1 mRNA is strongly induced in senescent leaves. Wounding is capable of inducing all the four expressed genes Leg1, 2, 3 and 4. Inthe leaf tissues there is a high increase in the expression of Leg2 and Leg4 after 24 h of the abscisic acid treatment, while for Leg1 an increase in the mRNA levels is observed in 4 h and decreases in 24 h after treatment. Isoform Leg4 mRNA levels increase with nicotinamide
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isoform Leg4 mRNA levels do not increase when the plants are submitted to NaCl
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legumain expression is increased during monocyte-to-macrophage differentiation
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legumain mRNA is down-regulated in monocytes isolated from patients treated with atorvastatin
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LGMN expression is increased in hepatocellular carcinoma cells relative to normal hepatocytes in the same specimens
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secretion of pro-legumain is inhibited by treatment with brefeldin A
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the enzyme expression is down-regulated in plantlets treated with salicylic acid
the enzyme expression is up-regulated in plantlets treated with abscisic acid
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
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