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Literature summary for 3.4.22.34 extracted from

  • Dall, E.; Brandstetter, H.
    Structure and function of legumain in health and disease (2016), Biochimie, 122, 126-150 .
    View publication on PubMed
Search for more literature for 3.4.22.34

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Bos taurus
Hg2+
-
 Bos taurus
additional information the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A Bos taurus
additional information the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A Homo sapiens
additional information the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A Mammalia
additional information the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A Schistosoma mansoni
additional information the enzyme is not inhibited by the broad spectrum cysteine protease inhibitors E-64, PMSF nor by the aspartate protease inhibitor pepstatin A unidentified plant

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Mammalia 5829
-
extracellular
-
 Mammalia
-
-
lysosome
-
 Mammalia 5764
-
nucleus
-
 Mammalia 5634
-
vacuole
-
 unidentified plant 5773
-

Organism

Organism UniProt Comment Textmining
Bos taurus Q95M12
-
-
Homo sapiens Q99538
-
-
Mammalia
-
-
-
Schistosoma mansoni P09841
-
-
unidentified plant
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme harbours 4 N-glycosylation sites resulting in a molecular weight of about 56000 Da of the fully glycosylated proenzyme Homo sapiens
proteolytic modification human prolegumain starts with a signal peptide (Met1-Ala17) that is released during trafficking, followed by a short 8 amino acid N-terminal propeptide (Val18-Asp25), the cysteine protease domain (Gly26-Asn323) and a C-terminal prodomain (Asp324-Tyr433) Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
breast cancer cell legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer Homo sapiens
-
colorectal cancer cell legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer Homo sapiens
-
gastric cancer cell legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer Homo sapiens
-
ovary cancer cell legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer Homo sapiens
-
pericarp
-
 unidentified plant
-
prostate gland cancer cell legumain is overexpressed in the majority of human solid tumours, including breast cancer, colorectal cancer, ovarian cancer, prostate cancer and gastric cancer Homo sapiens
-
seed
-
 unidentified plant
-
vegetative cell
-
 unidentified plant
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
11S/12S proglobulin + H2O
-
 unidentified plant ?
-
 ?
acetoacetyl-CoA synthetase + H2O
-
 Mammalia ?
-
 ?
Albumin + H2O
-
 unidentified plant ?
-
 ?
annexin A2 + H2O
-
 Mammalia ?
-
 ?
Bovine serum albumin + H2O
-
 Schistosoma mansoni ?
-
 ?
cathepsin B + H2O
-
 Mammalia ?
-
 ?
cathepsin H + H2O
-
 Mammalia ?
-
 ?
cathepsin L + H2O
-
 Mammalia ?
-
 ?
cathepsin S + H2O
-
 Mammalia ?
-
 ?
cyclic knottin + H2O
-
 unidentified plant ?
-
 ?
cystatin C + H2O
-
 Mammalia ?
-
 ?
cystatin E + H2O
-
 Mammalia ?
-
 ?
Fibronectin + H2O
-
 Mammalia ?
-
 ?
Gliadin + H2O
-
 unidentified plant ?
-
 ?
globulin + H2O
-
 unidentified plant ?
-
 ?
glutelin + H2O
-
 unidentified plant ?
-
 ?
Hemoglobin + H2O
-
 Schistosoma mansoni ?
-
 ?
Kalata-type cyclic peptide + H2O
-
 unidentified plant ?
-
 ?
additional information contrasting its endopeptidase activity, legumain can develop a carboxypeptidase activity which remains stable at neutral pH Mammalia ?
-
 ?
additional information ideal cleavage sequence: Pro-Thr-Asn (P3-P2-P1) Homo sapiens ?
-
 ?
additional information ideal cleavage sequence: Thr-Ala-Asn (P3-P2-P1) Schistosoma mansoni ?
-
 ?
additional information plant legumain shows a preference for bulky residues at P3 position unidentified plant ?
-
 ?
myelin basic protein + H2O
-
 Mammalia ?
-
 ?
proconcanavalin A + H2O
-
 unidentified plant ?
-
 ?
progelatinase A + H2O
-
 Mammalia ?
-
 ?
prolegumain + H2O
-
 Schistosoma mansoni ?
-
 ?
prolegumain + H2O
-
 unidentified plant ?
-
 ?
Schistosoma cathepsin B + H2O
-
 Schistosoma mansoni ?
-
 ?
serine protease inhibitor precursor + H2O
-
 unidentified plant ?
-
 ?
Tau-protein + H2O
-
 Mammalia ?
-
 ?
Tetanus toxin C-terminal fragment + H2O
-
 Mammalia ?
-
 ?

General Information

General Information Comment Organism
malfunction in pathological settings, such as cancer or Alzheimer's disease, the proper association of legumain activities with the corresponding cellular compartments is breached Mammalia
physiological function legumain promotes cell migration and its overexpression is associated with enhanced tissue invasion and metastasis. It promotes tumorigenesis and correlates with poor prognosis in different cancer types Homo sapiens
physiological function plant legumains are key enzymes in the processing and activation of seed storage proteins during seed maturation. Plants legumains are important components of the immune system. Plant legumains are discussed as main mediators of programmed cell death unidentified plant
physiological function the lysosomal enzyme contributes to antigen processing for class II MHC presentation Mammalia