Samiksha Jaiswal (Editor)

Legumain

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EC number
  
3.4.22.34

IntEnz
  
IntEnz view

ExPASy
  
NiceZyme view

CAS number
  
149371-18-6

BRENDA
  
BRENDA entry

KEGG
  
KEGG entry

Legumain

Legumain (EC 3.4.22.34, asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 gene product or LGMN (Homo sapiens), vicilin peptidohydrolase, bean endopeptidase) is an enzyme that in humans is encoded by the LGMN gene (previous symbol PRSC1).

Contents

Distribution

This enzyme was originally identified in the vacuoles of legume seeds, and was subsequently identified the lysosomes of mammals and Schistosoma mansoni. They are now known to be present in a range of plants and animals.

Reaction and specificity

This enzyme catalyses the following chemical reaction:

Hydrolysis of proteins and small molecule substrates at -Asn-Xaa- bonds

Both plant and animal legumains are most active in acidic environments.

Prodomain processing

Legmains are produced as inactive precursor zymogens. their C-terminal domain binds over their active site (where a substrate would normally bind), inhibiting activity. Once in the acidic environment of the vacuole or lysosome, the prodomain is cleaved off to reveal the active enzyme.

Mechanism

Legumain is a cysteine protease from the C13 family of the CD clan of proteases (MEROPS). It uses a catalytic triad of Cysteine-Histidine-Asparagine in its active site to perform covalent proteolysis of its substrate.

References

Legumain Wikipedia