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EC Tree
The taxonomic range for the selected organisms is: Phaseolus vulgaris
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hydrolysis of proteins and small molecule substrates at -Asn-/-Xaa- bonds
Synonyms
legumain, phaseolin, asparaginyl endopeptidase, lysosomal cysteine proteinase, vacuolar processing enzyme, hemoglobinase, asparagine endopeptidase, vicilin peptidohydrolase, hllgm, hllgm2,
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asparaginyl-specific cysteine endopeptidase
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Asparaginyl endopeptidase
Bean endopeptidase
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vacuolar processing enzyme
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Vicilin peptidohydrolase
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-
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Asparaginyl endopeptidase
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-
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Asparaginyl endopeptidase
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Proteinase B
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-
-
-
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hydrolysis of peptide bond
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hydrolysis of peptide bond
hydrolysis of peptide bond
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-
-
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hydrolysis of peptide bond
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-
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acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide + H2O
acetyl-Tyr-Val-Ala-Asp + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-(tert-butyl)Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
best synthetic substrate
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Gly-Ala-Asn + 7-amino-4-methylcoumarin
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low activity
-
?
benzyloxycarbonyl-Leu-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Ala-Asn + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Phe-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Pro-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Pro-Ala-Asn + 7-amino-4-methylcoumarin
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low activity
-
?
benzyloxycarbonyl-Tyr-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Tyr-Ala-Asn + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Val-Ala-Asn-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Val-Ala-Asn + 7-amino-4-methylcoumarin
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-
-
?
Boc-Asn-4-nitrophenyl ester + H2O
Boc-Asn + 4-nitrophenol
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-
-
-
?
Dnp-Pro-Glu-Ala-Asn-NH2 + H2O
Dnp-Pro-Glu-Ala-Asn + NH3
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-
-
-
?
ETRNGVEE + H2O
ETRN + GVEE
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-
-
-
?
neurotensin + H2O
?
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-
?
protein + H2O
peptides
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-
-
?
SESENGLEET + H2O
SESEN + GLEET
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-
-
-
?
tert-butoxycarbonyl-Asn nitrophenyl ester + H2O
tert-butoxycarbonyl-Asn + 4-nitrophenol
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-
-
-
?
tetanus toxoid C fragment + H2O
3 fragments
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cleavage sites are at Asn26, Asn97, and Asn372, but not Asn337
-
?
Z-Ala-Ala-Asn-7-amido-4-methylcoumarin + H2O
Z-Ala-Ala-Asn + 7-amino-4-methylcoumarin
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-
-
-
?
additional information
?
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phaseolin + H2O
?
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-
?
phaseolin + H2O
?
initiation of phaseolin proteolysis, enyme plays a key role in mobilization of phaseolin during and after kidney bean germination
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?
additional information
?
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substrate specificity for P3 position residues
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?
additional information
?
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the enzyme hydrolyzes peptide bonds with Asn in P1
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-
?
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phaseolin + H2O
?
initiation of phaseolin proteolysis, enyme plays a key role in mobilization of phaseolin during and after kidney bean germination
-
?
protein + H2O
peptides
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-
-
?
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iodoacetamide
11.6% remaining activity
iodoacetate
55.8 remaining activity
N-ethylmaleimide
16.6% remaining activity
diisopropyl fluorophosphate
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not
ovocystatin
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weak inhibition, from egg-white
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additional information
no inhibition with EDTA, PMSF, pepstatin A, leupeptin, and E-64
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additional information
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no inhibition with EDTA, PMSF, pepstatin A, leupeptin, and E-64
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additional information
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phenylmethylsulfonyl fluoride
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additional information
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not: EDTA
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7.04
purified enzyme, substrate casein
additional information
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-
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5
-
with substrate acetyl-Tyr-Val-Ala-Asp-4-methylcoumarin-7-amide
5.4
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with substrate benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide
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legumain-like proteinase LLP
SwissProt
brenda
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germinated, developmental pattern
brenda
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brenda
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-
brenda
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-
brenda
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VPE1_PHAVU
484
0
53389
Swiss-Prot
-
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38100
x * 38100, mature enzyme, SDS-PAGE, x * 53400, pre-proenzyme, SDS-PAGE
53400
x * 38100, mature enzyme, SDS-PAGE, x * 53400, pre-proenzyme, SDS-PAGE
23800
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Phaseolus vulgaris, gel filtration
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?
x * 38100, mature enzyme, SDS-PAGE, x * 53400, pre-proenzyme, SDS-PAGE
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no glycoprotein
but enzyme contains 1 putative N-glycosylation site at N326
proteolytic modification
putative cleavage site is N367-E368
proteolytic modification
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autoactivation by removal of the propeptide, activation after arrival in the vacuole
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native enzyme from germinated seeds, to homogeneity
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DNA and amino acid sequence determination and analysis
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Csoma, C.; Polgar, L.
Proteinase from germinating bean cotyledons. Evidence for involvement of a thiol group in catalysis
Biochem. J.
222
769-776
1984
Phaseolus vulgaris
brenda
Rotari, V.I.; Dando, P.M.; Barrett, A.J.
Legumain forms from plants and animals differ in their specificity
Biol. Chem.
382
953-959
2001
Phaseolus vulgaris, Sus scrofa
brenda
Senyuk, V.; Rotari, V.; Becker, C.; Zakharov, A.; Hortmann, C.; Mntz, K.; Vaintraub, I.
Does an asparaginyl-specific cysteine endopeptidase trigger phaseolin degradation in cotyledons of kidney bean seedlings ?
Eur. J. Biochem.
258
546-558
1998
Phaseolus vulgaris (O24325), Phaseolus vulgaris
brenda
Hara-Nishimura, I.
Plant legumain, asparaginyl endopeptidase
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1310-1313
2004
Arabidopsis thaliana, Canavalia ensiformis, Ricinus communis, Glycine max, Vigna mungo, Phaseolus vulgaris, Vigna aconitifolia
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brenda
3.4.22.34 Legumain
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The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 
