$VAR1 = undef;
Summary for peptidase M08.001: leishmanolysin
Names | |
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MEROPS Name | leishmanolysin |
Other names | Gp63 g.p. (Leishmania sp.), major surface protein (Msp), promastigote surface endopeptidase, promastigote surface protease, PSP, TbMSP-A (Trypanosoma brucei), TbMSP-B (Trypanosoma brucei), TbMSP-C (Trypanosoma brucei) |
Domain architecture |
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MEROPS Classification | |
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Classification | Clan MA >> Subclan MA(M) >> Family M8 >> Subfamily (none) >> M08.001 |
Holotype | leishmanolysin (Leishmania major), Uniprot accession P08148 (peptidase unit: 101-602), MERNUM MER0001165 |
History | Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London. |
Activity | |||
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Catalytic type | Metallo | ||
Peplist | Included in the Peplist with identifier PL00151 | ||
NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.24 (Metalloendopeptidases) >> Peptidase 3.4.24.36 | ||
Enzymology | BRENDA database | ||
Proteolytic events | CutDB database (4 cleavages) | ||
Physiology | Cleaves CD4 on surface of T lymphocytes. Protects promastigotes from lysis by complement. Facilitates migration of the parasite through extracellular matrix (McGwire et al., 2003). | ||
Pharmaceutical relevance | Being the most abundant protein of the surface membrane of the promastigote form of Leishmania sp., leishmanolysin is a target for vaccine production. The activity of the enzyme may well also contribute to infection of the host, so inhibitors may have therapeutic value (McGwire et al., 2003; Yao et al., 2003). | ||
Pathways | KEGG | African trypanosomiasis | |
Cleavage site specificity | Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here. | ||
Cleavage pattern | l/-/al/yls/kr/k/- (based on 20 cleavages) |
Specificity matrix | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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