An example AEP: Human legumain with catalytic triad in red, bound to product in black. (PDB: 4AW9)
Human pro-legumain with catalytic triad in red, bound to its auto-inhibitory C-terminal prodomain in green. (PDB: 4FGU)
Identifiers
EC no.
3.4.22.34
CAS no.
149371-18-6
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Search
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articles
PubMed
articles
NCBI
proteins
Asparagine endopeptidase (AEP, mammalian legumain, δ-secretase; EC 3.4.22.34) is a proteolytic enzyme from C13 peptidase family which hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile (hence also called cysteine protease). It is also known as asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 gene product or LGMN (Homo sapiens), vicilin peptidohydrolase and bean endopeptidase. In humans it is encoded by the LGMN gene (previous symbol PRSC1).[1][2][3]
It hydrolyzes substrates at the C-terminus of asparagine residues. Discovered in 1996 in beans, its homologues have been identified in plants, protozoa, vertebrates, and helminths. The enzyme has been implicated in several human diseases such as cancer, atherosclerosis and inflammation .[4] It can be detected in spleen, liver, brain, testis tissue and heart[5] and the protein is mostly localised to lysosomes and endosomes. It is also interesting that AEP is activated in age-dependent manner.[6]
^Hara-Nishimura I (1998). "Asparaginyl endopeptidase". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 746–749.
^Dalton JP, Brindley PJ (1998). "Schistosome legumain". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 749–754.
^Chen JM, Rawlings ND, Stevens RA, Barrett AJ (December 1998). "Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Letters. 441 (3): 361–5. doi:10.1016/S0014-5793(98)01574-9. PMID 9891971. S2CID 46043484.
^Zhang Z, Xie M, Ye K (October 2016). "Asparagine endopeptidase is an innovative therapeutic target for neurodegenerative diseases". Expert Opinion on Therapeutic Targets. 20 (10): 1237–45. doi:10.1080/14728222.2016.1182990. PMC 5315368. PMID 27115710.
^Chen JM, Dando PM, Stevens RA, Fortunato M, Barrett AJ (October 1998). "Cloning and expression of mouse legumain, a lysosomal endopeptidase". The Biochemical Journal. 335 ( Pt 1) (1): 111–7. doi:10.1042/bj3350111. PMC 1219758. PMID 9742219.
^Zhao L, Hua T, Crowley C, Ru H, Ni X, Shaw N, Jiao L, Ding W, Qu L, Hung LW, Huang W, Liu L, Ye K, Ouyang S, Cheng G, Liu ZJ (March 2014). "Structural analysis of asparaginyl endopeptidase reveals the activation mechanism and a reversible intermediate maturation stage". Cell Research. 24 (3): 344–58. doi:10.1038/cr.2014.4. PMC 3945893. PMID 24407422.
and 18 Related for: Asparagine endopeptidase information
Asparagineendopeptidase (AEP, mammalian legumain, δ-secretase; EC 3.4.22.34) is a proteolytic enzyme from C13 peptidase family which hydrolyses a peptide...
residues in family N4 asparagine peptide lyases are N1100, Y1227, E1249 and R1282. Family N6 includes autoprocessing endopeptidases involved in type III...
a mathematical book by James H. Wilkinson, published in 1965 asparagineendopeptidase, an enzyme auditory evoked potential AEP Building, Columbus, Ohio...
acid Metalloproteases - using a metal, usually zinc Asparagine peptide lyases - using an asparagine to perform an elimination reaction (not requiring water)...
modifications. Endopeptidases are enzymes that add water to an internal peptide bond in a peptide chain and break that bond. Three common endopeptidases that come...
neutrophil form of elastase (EC 3.4.21.37) is 218 amino acids long, with two asparagine-linked carbohydrate chains (see glycosylation). It is present in azurophil...
required for this. In the case of kalata B1 the indicated glycine (G) and asparagine (N) amino acids are the terminal residues that are linked in a peptide...
as glutamic acid (E) on the interior and asparagine (R), Serine (and lysine (K) on the exterior. Asparagine residues may serve as an important oligosaccharide...
Cys248-Cys430. They all have four potential N-glycosylation sites. These occur at asparagine (Asn) amino acid numbers 96, 135, 155, and 192 in humans and at similar...
D, Silvente-Poirot S (May 2003). "Identification of tyrosine 189 and asparagine 358 of the cholecystokinin 2 receptor in direct interaction with the crucial...
category of proteins called proline-rich proteins. PRR23A contains less asparagine, threonine, and lysine compared to other human proteins. This protein...
of oxytocin by brain synaptic membranes: role of aminopeptidases and endopeptidases". Peptides. 12 (5): 1119–1125. doi:10.1016/0196-9781(91)90068-z. PMID 1800950...
the cysteine protease triad (cysteine, a histidine and an aspartate or asparagine). The C-terminus of USP18 is primarily responsible for negative regulation...
sarcoplasmic reticulum as well as hydroxylation of aspartic acid and asparagine in epidermal growth factor-like domains of various proteins. As early...
pressure. Serpin A12 has three possible glycosylation sites located at asparagine residues. These can be post-translational modifications that may change...
extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position. GRCh38: Ensembl release 89: ENSG00000242550...
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