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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

Engineering

Engineering on EC 3.4.22.34 - Legumain

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
D147G
the mutant shows reduced proteolytic activity
D147S
the mutant shows reduced proteolytic activity
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
H47A
-
site-directed mutagenesis, 54% activity compared to 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
additional information
-
construction of null-legumain mice